Helical ordering of envelope‐associated proteins and glycoproteins in respiratory syncytial virus
Abstract Human respiratory syncytial virus (RSV) causes severe respiratory illness in children and the elderly. Here, using cryogenic electron microscopy and tomography combined with computational image analysis and three‐dimensional reconstruction, we show that there is extensive helical ordering o...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Conley, Michaela J [verfasserIn] Short, Judith M [verfasserIn] Burns, Andrew M [verfasserIn] Streetley, James [verfasserIn] Hutchings, Joshua [verfasserIn] Bakker, Saskia E [verfasserIn] Power, B Joanne [verfasserIn] Jaffery, Hussain [verfasserIn] Haney, Joanne [verfasserIn] Zanetti, Giulia [verfasserIn] Murcia, Pablo R [verfasserIn] Stewart, Murray [verfasserIn] Fearns, Rachel [verfasserIn] Vijayakrishnan, Swetha [verfasserIn] Bhella, David [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2021 |
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| Schlagwörter: |
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| Anmerkung: |
© The Author(s) 2021 |
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| Übergeordnetes Werk: |
Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 41(2021), 3 vom: 22. Dez. |
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| Übergeordnetes Werk: |
volume:41 ; year:2021 ; number:3 ; day:22 ; month:12 |
| Links: |
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| DOI / URN: |
10.15252/embj.2021109728 |
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| Katalog-ID: |
SPR058111506 |
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| 100 | 1 | |a Conley, Michaela J |e verfasserin |0 (orcid)0000-0002-3457-1149 |4 aut | |
| 245 | 1 | 0 | |a Helical ordering of envelope‐associated proteins and glycoproteins in respiratory syncytial virus |
| 264 | 1 | |c 2021 | |
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| 500 | |a © The Author(s) 2021 | ||
| 520 | |a Abstract Human respiratory syncytial virus (RSV) causes severe respiratory illness in children and the elderly. Here, using cryogenic electron microscopy and tomography combined with computational image analysis and three‐dimensional reconstruction, we show that there is extensive helical ordering of the envelope‐associated proteins and glycoproteins of RSV filamentous virions. We calculated a 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope. These data define a helical lattice of M‐dimers, showing how M is oriented relative to the viral envelope. Glycoproteins that stud the viral envelope were also found to be helically ordered, a property that was coordinated by the M‐layer. Furthermore, envelope glycoproteins clustered in pairs, a feature that may have implications for the conformation of fusion (F) glycoprotein epitopes that are the principal target for vaccine and monoclonal antibody development. We also report the presence, in authentic virus infections, of N‐RNA rings packaged within RSV virions. These data provide molecular insight into the organisation of the virion and the mechanism of its assembly. | ||
| 520 | |a Synopsis CryoEM and tomography analysis of the human pathogen respiratory syncytial virus shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer, which in turn coordinates helical ordering and clustering of viral glycoproteins. 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope.Respiratory syncytial virus filamentous virions have a helically ordered matrix layer that is formed by a lattice of M dimers.Viral glycoproteins embedded in the envelope also show helical ordering and frequently cluster in pairs, these properties are coordinated by the underlying matrix layer.In addition to packing multiple copies of the viral genome in the form of helical ribonucleoprotein complexes or nucleocapsids, virions also package an abundance of ring‐shaped assemblies likely formed of the viral nucleocapsid protein (N) and RNA. | ||
| 520 | |a Graphical Abstract CryoEM and tomography analysis of the human pathogen RSV shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer that in turn coordinates helical ordering and clustering of viral glycoproteins. | ||
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| 650 | 4 | |a cryo‐ET |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a glycoprotein |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a matrix protein |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a virus structure |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Short, Judith M |e verfasserin |0 (orcid)0000-0002-9008-6607 |4 aut | |
| 700 | 1 | |a Burns, Andrew M |e verfasserin |0 (orcid)0000-0003-2540-5461 |4 aut | |
| 700 | 1 | |a Streetley, James |e verfasserin |0 (orcid)0000-0001-7808-605X |4 aut | |
| 700 | 1 | |a Hutchings, Joshua |e verfasserin |0 (orcid)0000-0001-6841-8583 |4 aut | |
| 700 | 1 | |a Bakker, Saskia E |e verfasserin |0 (orcid)0000-0003-3958-4421 |4 aut | |
| 700 | 1 | |a Power, B Joanne |e verfasserin |0 (orcid)0000-0001-6706-3872 |4 aut | |
| 700 | 1 | |a Jaffery, Hussain |e verfasserin |0 (orcid)0000-0002-1408-3260 |4 aut | |
| 700 | 1 | |a Haney, Joanne |e verfasserin |0 (orcid)0000-0001-9635-8207 |4 aut | |
| 700 | 1 | |a Zanetti, Giulia |e verfasserin |0 (orcid)0000-0003-1905-0342 |4 aut | |
| 700 | 1 | |a Murcia, Pablo R |e verfasserin |0 (orcid)0000-0002-4352-394X |4 aut | |
| 700 | 1 | |a Stewart, Murray |e verfasserin |4 aut | |
| 700 | 1 | |a Fearns, Rachel |e verfasserin |0 (orcid)0000-0003-0783-7498 |4 aut | |
| 700 | 1 | |a Vijayakrishnan, Swetha |e verfasserin |0 (orcid)0000-0002-1895-1272 |4 aut | |
| 700 | 1 | |a Bhella, David |e verfasserin |0 (orcid)0000-0003-2096-8310 |4 aut | |
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10.15252/embj.2021109728 doi (DE-627)SPR058111506 (SPR)embj.2021109728-e DE-627 ger DE-627 rakwb eng Conley, Michaela J verfasserin (orcid)0000-0002-3457-1149 aut Helical ordering of envelope‐associated proteins and glycoproteins in respiratory syncytial virus 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2021 Abstract Human respiratory syncytial virus (RSV) causes severe respiratory illness in children and the elderly. Here, using cryogenic electron microscopy and tomography combined with computational image analysis and three‐dimensional reconstruction, we show that there is extensive helical ordering of the envelope‐associated proteins and glycoproteins of RSV filamentous virions. We calculated a 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope. These data define a helical lattice of M‐dimers, showing how M is oriented relative to the viral envelope. Glycoproteins that stud the viral envelope were also found to be helically ordered, a property that was coordinated by the M‐layer. Furthermore, envelope glycoproteins clustered in pairs, a feature that may have implications for the conformation of fusion (F) glycoprotein epitopes that are the principal target for vaccine and monoclonal antibody development. We also report the presence, in authentic virus infections, of N‐RNA rings packaged within RSV virions. These data provide molecular insight into the organisation of the virion and the mechanism of its assembly. Synopsis CryoEM and tomography analysis of the human pathogen respiratory syncytial virus shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer, which in turn coordinates helical ordering and clustering of viral glycoproteins. 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope.Respiratory syncytial virus filamentous virions have a helically ordered matrix layer that is formed by a lattice of M dimers.Viral glycoproteins embedded in the envelope also show helical ordering and frequently cluster in pairs, these properties are coordinated by the underlying matrix layer.In addition to packing multiple copies of the viral genome in the form of helical ribonucleoprotein complexes or nucleocapsids, virions also package an abundance of ring‐shaped assemblies likely formed of the viral nucleocapsid protein (N) and RNA. Graphical Abstract CryoEM and tomography analysis of the human pathogen RSV shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer that in turn coordinates helical ordering and clustering of viral glycoproteins. cryo‐EM (dpeaa)DE-He213 cryo‐ET (dpeaa)DE-He213 glycoprotein (dpeaa)DE-He213 matrix protein (dpeaa)DE-He213 virus structure (dpeaa)DE-He213 Short, Judith M verfasserin (orcid)0000-0002-9008-6607 aut Burns, Andrew M verfasserin (orcid)0000-0003-2540-5461 aut Streetley, James verfasserin (orcid)0000-0001-7808-605X aut Hutchings, Joshua verfasserin (orcid)0000-0001-6841-8583 aut Bakker, Saskia E verfasserin (orcid)0000-0003-3958-4421 aut Power, B Joanne verfasserin (orcid)0000-0001-6706-3872 aut Jaffery, Hussain verfasserin (orcid)0000-0002-1408-3260 aut Haney, Joanne verfasserin (orcid)0000-0001-9635-8207 aut Zanetti, Giulia verfasserin (orcid)0000-0003-1905-0342 aut Murcia, Pablo R verfasserin (orcid)0000-0002-4352-394X aut Stewart, Murray verfasserin aut Fearns, Rachel verfasserin (orcid)0000-0003-0783-7498 aut Vijayakrishnan, Swetha verfasserin (orcid)0000-0002-1895-1272 aut Bhella, David verfasserin (orcid)0000-0003-2096-8310 aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 41(2021), 3 vom: 22. Dez. (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:41 year:2021 number:3 day:22 month:12 https://dx.doi.org/10.15252/embj.2021109728 X:SPRINGER Resolving-System kostenfrei Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 41 2021 3 22 12 |
| spelling |
10.15252/embj.2021109728 doi (DE-627)SPR058111506 (SPR)embj.2021109728-e DE-627 ger DE-627 rakwb eng Conley, Michaela J verfasserin (orcid)0000-0002-3457-1149 aut Helical ordering of envelope‐associated proteins and glycoproteins in respiratory syncytial virus 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2021 Abstract Human respiratory syncytial virus (RSV) causes severe respiratory illness in children and the elderly. Here, using cryogenic electron microscopy and tomography combined with computational image analysis and three‐dimensional reconstruction, we show that there is extensive helical ordering of the envelope‐associated proteins and glycoproteins of RSV filamentous virions. We calculated a 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope. These data define a helical lattice of M‐dimers, showing how M is oriented relative to the viral envelope. Glycoproteins that stud the viral envelope were also found to be helically ordered, a property that was coordinated by the M‐layer. Furthermore, envelope glycoproteins clustered in pairs, a feature that may have implications for the conformation of fusion (F) glycoprotein epitopes that are the principal target for vaccine and monoclonal antibody development. We also report the presence, in authentic virus infections, of N‐RNA rings packaged within RSV virions. These data provide molecular insight into the organisation of the virion and the mechanism of its assembly. Synopsis CryoEM and tomography analysis of the human pathogen respiratory syncytial virus shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer, which in turn coordinates helical ordering and clustering of viral glycoproteins. 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope.Respiratory syncytial virus filamentous virions have a helically ordered matrix layer that is formed by a lattice of M dimers.Viral glycoproteins embedded in the envelope also show helical ordering and frequently cluster in pairs, these properties are coordinated by the underlying matrix layer.In addition to packing multiple copies of the viral genome in the form of helical ribonucleoprotein complexes or nucleocapsids, virions also package an abundance of ring‐shaped assemblies likely formed of the viral nucleocapsid protein (N) and RNA. Graphical Abstract CryoEM and tomography analysis of the human pathogen RSV shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer that in turn coordinates helical ordering and clustering of viral glycoproteins. cryo‐EM (dpeaa)DE-He213 cryo‐ET (dpeaa)DE-He213 glycoprotein (dpeaa)DE-He213 matrix protein (dpeaa)DE-He213 virus structure (dpeaa)DE-He213 Short, Judith M verfasserin (orcid)0000-0002-9008-6607 aut Burns, Andrew M verfasserin (orcid)0000-0003-2540-5461 aut Streetley, James verfasserin (orcid)0000-0001-7808-605X aut Hutchings, Joshua verfasserin (orcid)0000-0001-6841-8583 aut Bakker, Saskia E verfasserin (orcid)0000-0003-3958-4421 aut Power, B Joanne verfasserin (orcid)0000-0001-6706-3872 aut Jaffery, Hussain verfasserin (orcid)0000-0002-1408-3260 aut Haney, Joanne verfasserin (orcid)0000-0001-9635-8207 aut Zanetti, Giulia verfasserin (orcid)0000-0003-1905-0342 aut Murcia, Pablo R verfasserin (orcid)0000-0002-4352-394X aut Stewart, Murray verfasserin aut Fearns, Rachel verfasserin (orcid)0000-0003-0783-7498 aut Vijayakrishnan, Swetha verfasserin (orcid)0000-0002-1895-1272 aut Bhella, David verfasserin (orcid)0000-0003-2096-8310 aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 41(2021), 3 vom: 22. Dez. (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:41 year:2021 number:3 day:22 month:12 https://dx.doi.org/10.15252/embj.2021109728 X:SPRINGER Resolving-System kostenfrei Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 41 2021 3 22 12 |
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10.15252/embj.2021109728 doi (DE-627)SPR058111506 (SPR)embj.2021109728-e DE-627 ger DE-627 rakwb eng Conley, Michaela J verfasserin (orcid)0000-0002-3457-1149 aut Helical ordering of envelope‐associated proteins and glycoproteins in respiratory syncytial virus 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2021 Abstract Human respiratory syncytial virus (RSV) causes severe respiratory illness in children and the elderly. Here, using cryogenic electron microscopy and tomography combined with computational image analysis and three‐dimensional reconstruction, we show that there is extensive helical ordering of the envelope‐associated proteins and glycoproteins of RSV filamentous virions. We calculated a 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope. These data define a helical lattice of M‐dimers, showing how M is oriented relative to the viral envelope. Glycoproteins that stud the viral envelope were also found to be helically ordered, a property that was coordinated by the M‐layer. Furthermore, envelope glycoproteins clustered in pairs, a feature that may have implications for the conformation of fusion (F) glycoprotein epitopes that are the principal target for vaccine and monoclonal antibody development. We also report the presence, in authentic virus infections, of N‐RNA rings packaged within RSV virions. These data provide molecular insight into the organisation of the virion and the mechanism of its assembly. Synopsis CryoEM and tomography analysis of the human pathogen respiratory syncytial virus shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer, which in turn coordinates helical ordering and clustering of viral glycoproteins. 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope.Respiratory syncytial virus filamentous virions have a helically ordered matrix layer that is formed by a lattice of M dimers.Viral glycoproteins embedded in the envelope also show helical ordering and frequently cluster in pairs, these properties are coordinated by the underlying matrix layer.In addition to packing multiple copies of the viral genome in the form of helical ribonucleoprotein complexes or nucleocapsids, virions also package an abundance of ring‐shaped assemblies likely formed of the viral nucleocapsid protein (N) and RNA. Graphical Abstract CryoEM and tomography analysis of the human pathogen RSV shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer that in turn coordinates helical ordering and clustering of viral glycoproteins. cryo‐EM (dpeaa)DE-He213 cryo‐ET (dpeaa)DE-He213 glycoprotein (dpeaa)DE-He213 matrix protein (dpeaa)DE-He213 virus structure (dpeaa)DE-He213 Short, Judith M verfasserin (orcid)0000-0002-9008-6607 aut Burns, Andrew M verfasserin (orcid)0000-0003-2540-5461 aut Streetley, James verfasserin (orcid)0000-0001-7808-605X aut Hutchings, Joshua verfasserin (orcid)0000-0001-6841-8583 aut Bakker, Saskia E verfasserin (orcid)0000-0003-3958-4421 aut Power, B Joanne verfasserin (orcid)0000-0001-6706-3872 aut Jaffery, Hussain verfasserin (orcid)0000-0002-1408-3260 aut Haney, Joanne verfasserin (orcid)0000-0001-9635-8207 aut Zanetti, Giulia verfasserin (orcid)0000-0003-1905-0342 aut Murcia, Pablo R verfasserin (orcid)0000-0002-4352-394X aut Stewart, Murray verfasserin aut Fearns, Rachel verfasserin (orcid)0000-0003-0783-7498 aut Vijayakrishnan, Swetha verfasserin (orcid)0000-0002-1895-1272 aut Bhella, David verfasserin (orcid)0000-0003-2096-8310 aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 41(2021), 3 vom: 22. Dez. (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:41 year:2021 number:3 day:22 month:12 https://dx.doi.org/10.15252/embj.2021109728 X:SPRINGER Resolving-System kostenfrei Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 41 2021 3 22 12 |
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10.15252/embj.2021109728 doi (DE-627)SPR058111506 (SPR)embj.2021109728-e DE-627 ger DE-627 rakwb eng Conley, Michaela J verfasserin (orcid)0000-0002-3457-1149 aut Helical ordering of envelope‐associated proteins and glycoproteins in respiratory syncytial virus 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2021 Abstract Human respiratory syncytial virus (RSV) causes severe respiratory illness in children and the elderly. Here, using cryogenic electron microscopy and tomography combined with computational image analysis and three‐dimensional reconstruction, we show that there is extensive helical ordering of the envelope‐associated proteins and glycoproteins of RSV filamentous virions. We calculated a 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope. These data define a helical lattice of M‐dimers, showing how M is oriented relative to the viral envelope. Glycoproteins that stud the viral envelope were also found to be helically ordered, a property that was coordinated by the M‐layer. Furthermore, envelope glycoproteins clustered in pairs, a feature that may have implications for the conformation of fusion (F) glycoprotein epitopes that are the principal target for vaccine and monoclonal antibody development. We also report the presence, in authentic virus infections, of N‐RNA rings packaged within RSV virions. These data provide molecular insight into the organisation of the virion and the mechanism of its assembly. Synopsis CryoEM and tomography analysis of the human pathogen respiratory syncytial virus shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer, which in turn coordinates helical ordering and clustering of viral glycoproteins. 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope.Respiratory syncytial virus filamentous virions have a helically ordered matrix layer that is formed by a lattice of M dimers.Viral glycoproteins embedded in the envelope also show helical ordering and frequently cluster in pairs, these properties are coordinated by the underlying matrix layer.In addition to packing multiple copies of the viral genome in the form of helical ribonucleoprotein complexes or nucleocapsids, virions also package an abundance of ring‐shaped assemblies likely formed of the viral nucleocapsid protein (N) and RNA. Graphical Abstract CryoEM and tomography analysis of the human pathogen RSV shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer that in turn coordinates helical ordering and clustering of viral glycoproteins. cryo‐EM (dpeaa)DE-He213 cryo‐ET (dpeaa)DE-He213 glycoprotein (dpeaa)DE-He213 matrix protein (dpeaa)DE-He213 virus structure (dpeaa)DE-He213 Short, Judith M verfasserin (orcid)0000-0002-9008-6607 aut Burns, Andrew M verfasserin (orcid)0000-0003-2540-5461 aut Streetley, James verfasserin (orcid)0000-0001-7808-605X aut Hutchings, Joshua verfasserin (orcid)0000-0001-6841-8583 aut Bakker, Saskia E verfasserin (orcid)0000-0003-3958-4421 aut Power, B Joanne verfasserin (orcid)0000-0001-6706-3872 aut Jaffery, Hussain verfasserin (orcid)0000-0002-1408-3260 aut Haney, Joanne verfasserin (orcid)0000-0001-9635-8207 aut Zanetti, Giulia verfasserin (orcid)0000-0003-1905-0342 aut Murcia, Pablo R verfasserin (orcid)0000-0002-4352-394X aut Stewart, Murray verfasserin aut Fearns, Rachel verfasserin (orcid)0000-0003-0783-7498 aut Vijayakrishnan, Swetha verfasserin (orcid)0000-0002-1895-1272 aut Bhella, David verfasserin (orcid)0000-0003-2096-8310 aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 41(2021), 3 vom: 22. Dez. (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:41 year:2021 number:3 day:22 month:12 https://dx.doi.org/10.15252/embj.2021109728 X:SPRINGER Resolving-System kostenfrei Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 41 2021 3 22 12 |
| allfieldsSound |
10.15252/embj.2021109728 doi (DE-627)SPR058111506 (SPR)embj.2021109728-e DE-627 ger DE-627 rakwb eng Conley, Michaela J verfasserin (orcid)0000-0002-3457-1149 aut Helical ordering of envelope‐associated proteins and glycoproteins in respiratory syncytial virus 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2021 Abstract Human respiratory syncytial virus (RSV) causes severe respiratory illness in children and the elderly. Here, using cryogenic electron microscopy and tomography combined with computational image analysis and three‐dimensional reconstruction, we show that there is extensive helical ordering of the envelope‐associated proteins and glycoproteins of RSV filamentous virions. We calculated a 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope. These data define a helical lattice of M‐dimers, showing how M is oriented relative to the viral envelope. Glycoproteins that stud the viral envelope were also found to be helically ordered, a property that was coordinated by the M‐layer. Furthermore, envelope glycoproteins clustered in pairs, a feature that may have implications for the conformation of fusion (F) glycoprotein epitopes that are the principal target for vaccine and monoclonal antibody development. We also report the presence, in authentic virus infections, of N‐RNA rings packaged within RSV virions. These data provide molecular insight into the organisation of the virion and the mechanism of its assembly. Synopsis CryoEM and tomography analysis of the human pathogen respiratory syncytial virus shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer, which in turn coordinates helical ordering and clustering of viral glycoproteins. 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope.Respiratory syncytial virus filamentous virions have a helically ordered matrix layer that is formed by a lattice of M dimers.Viral glycoproteins embedded in the envelope also show helical ordering and frequently cluster in pairs, these properties are coordinated by the underlying matrix layer.In addition to packing multiple copies of the viral genome in the form of helical ribonucleoprotein complexes or nucleocapsids, virions also package an abundance of ring‐shaped assemblies likely formed of the viral nucleocapsid protein (N) and RNA. Graphical Abstract CryoEM and tomography analysis of the human pathogen RSV shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer that in turn coordinates helical ordering and clustering of viral glycoproteins. cryo‐EM (dpeaa)DE-He213 cryo‐ET (dpeaa)DE-He213 glycoprotein (dpeaa)DE-He213 matrix protein (dpeaa)DE-He213 virus structure (dpeaa)DE-He213 Short, Judith M verfasserin (orcid)0000-0002-9008-6607 aut Burns, Andrew M verfasserin (orcid)0000-0003-2540-5461 aut Streetley, James verfasserin (orcid)0000-0001-7808-605X aut Hutchings, Joshua verfasserin (orcid)0000-0001-6841-8583 aut Bakker, Saskia E verfasserin (orcid)0000-0003-3958-4421 aut Power, B Joanne verfasserin (orcid)0000-0001-6706-3872 aut Jaffery, Hussain verfasserin (orcid)0000-0002-1408-3260 aut Haney, Joanne verfasserin (orcid)0000-0001-9635-8207 aut Zanetti, Giulia verfasserin (orcid)0000-0003-1905-0342 aut Murcia, Pablo R verfasserin (orcid)0000-0002-4352-394X aut Stewart, Murray verfasserin aut Fearns, Rachel verfasserin (orcid)0000-0003-0783-7498 aut Vijayakrishnan, Swetha verfasserin (orcid)0000-0002-1895-1272 aut Bhella, David verfasserin (orcid)0000-0003-2096-8310 aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 41(2021), 3 vom: 22. Dez. (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:41 year:2021 number:3 day:22 month:12 https://dx.doi.org/10.15252/embj.2021109728 X:SPRINGER Resolving-System kostenfrei Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_211 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 41 2021 3 22 12 |
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The EMBO Journal |
| authorswithroles_txt_mv |
Conley, Michaela J @@aut@@ Short, Judith M @@aut@@ Burns, Andrew M @@aut@@ Streetley, James @@aut@@ Hutchings, Joshua @@aut@@ Bakker, Saskia E @@aut@@ Power, B Joanne @@aut@@ Jaffery, Hussain @@aut@@ Haney, Joanne @@aut@@ Zanetti, Giulia @@aut@@ Murcia, Pablo R @@aut@@ Stewart, Murray @@aut@@ Fearns, Rachel @@aut@@ Vijayakrishnan, Swetha @@aut@@ Bhella, David @@aut@@ |
| publishDateDaySort_date |
2021-12-22T00:00:00Z |
| hierarchy_top_id |
266022529 |
| id |
SPR058111506 |
| language_de |
englisch |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000naa a22002652 4500</leader><controlfield tag="001">SPR058111506</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20241026064809.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">241026s2021 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.15252/embj.2021109728</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR058111506</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)embj.2021109728-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Conley, Michaela J</subfield><subfield code="e">verfasserin</subfield><subfield code="0">(orcid)0000-0002-3457-1149</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Helical ordering of envelope‐associated proteins and glycoproteins in respiratory syncytial virus</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2021</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© The Author(s) 2021</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Human respiratory syncytial virus (RSV) causes severe respiratory illness in children and the elderly. Here, using cryogenic electron microscopy and tomography combined with computational image analysis and three‐dimensional reconstruction, we show that there is extensive helical ordering of the envelope‐associated proteins and glycoproteins of RSV filamentous virions. We calculated a 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope. These data define a helical lattice of M‐dimers, showing how M is oriented relative to the viral envelope. Glycoproteins that stud the viral envelope were also found to be helically ordered, a property that was coordinated by the M‐layer. Furthermore, envelope glycoproteins clustered in pairs, a feature that may have implications for the conformation of fusion (F) glycoprotein epitopes that are the principal target for vaccine and monoclonal antibody development. We also report the presence, in authentic virus infections, of N‐RNA rings packaged within RSV virions. These data provide molecular insight into the organisation of the virion and the mechanism of its assembly.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Synopsis CryoEM and tomography analysis of the human pathogen respiratory syncytial virus shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer, which in turn coordinates helical ordering and clustering of viral glycoproteins. 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope.Respiratory syncytial virus filamentous virions have a helically ordered matrix layer that is formed by a lattice of M dimers.Viral glycoproteins embedded in the envelope also show helical ordering and frequently cluster in pairs, these properties are coordinated by the underlying matrix layer.In addition to packing multiple copies of the viral genome in the form of helical ribonucleoprotein complexes or nucleocapsids, virions also package an abundance of ring‐shaped assemblies likely formed of the viral nucleocapsid protein (N) and RNA.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Graphical Abstract CryoEM and tomography analysis of the human pathogen RSV shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer that in turn coordinates helical ordering and clustering of viral glycoproteins.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">cryo‐EM</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">cryo‐ET</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">glycoprotein</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">matrix 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Conley, Michaela J Short, Judith M Burns, Andrew M Streetley, James Hutchings, Joshua Bakker, Saskia E Power, B Joanne Jaffery, Hussain Haney, Joanne Zanetti, Giulia Murcia, Pablo R Stewart, Murray Fearns, Rachel Vijayakrishnan, Swetha Bhella, David |
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helical ordering of envelope‐associated proteins and glycoproteins in respiratory syncytial virus |
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Helical ordering of envelope‐associated proteins and glycoproteins in respiratory syncytial virus |
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Abstract Human respiratory syncytial virus (RSV) causes severe respiratory illness in children and the elderly. Here, using cryogenic electron microscopy and tomography combined with computational image analysis and three‐dimensional reconstruction, we show that there is extensive helical ordering of the envelope‐associated proteins and glycoproteins of RSV filamentous virions. We calculated a 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope. These data define a helical lattice of M‐dimers, showing how M is oriented relative to the viral envelope. Glycoproteins that stud the viral envelope were also found to be helically ordered, a property that was coordinated by the M‐layer. Furthermore, envelope glycoproteins clustered in pairs, a feature that may have implications for the conformation of fusion (F) glycoprotein epitopes that are the principal target for vaccine and monoclonal antibody development. We also report the presence, in authentic virus infections, of N‐RNA rings packaged within RSV virions. These data provide molecular insight into the organisation of the virion and the mechanism of its assembly. Synopsis CryoEM and tomography analysis of the human pathogen respiratory syncytial virus shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer, which in turn coordinates helical ordering and clustering of viral glycoproteins. 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope.Respiratory syncytial virus filamentous virions have a helically ordered matrix layer that is formed by a lattice of M dimers.Viral glycoproteins embedded in the envelope also show helical ordering and frequently cluster in pairs, these properties are coordinated by the underlying matrix layer.In addition to packing multiple copies of the viral genome in the form of helical ribonucleoprotein complexes or nucleocapsids, virions also package an abundance of ring‐shaped assemblies likely formed of the viral nucleocapsid protein (N) and RNA. Graphical Abstract CryoEM and tomography analysis of the human pathogen RSV shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer that in turn coordinates helical ordering and clustering of viral glycoproteins. © The Author(s) 2021 |
| abstractGer |
Abstract Human respiratory syncytial virus (RSV) causes severe respiratory illness in children and the elderly. Here, using cryogenic electron microscopy and tomography combined with computational image analysis and three‐dimensional reconstruction, we show that there is extensive helical ordering of the envelope‐associated proteins and glycoproteins of RSV filamentous virions. We calculated a 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope. These data define a helical lattice of M‐dimers, showing how M is oriented relative to the viral envelope. Glycoproteins that stud the viral envelope were also found to be helically ordered, a property that was coordinated by the M‐layer. Furthermore, envelope glycoproteins clustered in pairs, a feature that may have implications for the conformation of fusion (F) glycoprotein epitopes that are the principal target for vaccine and monoclonal antibody development. We also report the presence, in authentic virus infections, of N‐RNA rings packaged within RSV virions. These data provide molecular insight into the organisation of the virion and the mechanism of its assembly. Synopsis CryoEM and tomography analysis of the human pathogen respiratory syncytial virus shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer, which in turn coordinates helical ordering and clustering of viral glycoproteins. 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope.Respiratory syncytial virus filamentous virions have a helically ordered matrix layer that is formed by a lattice of M dimers.Viral glycoproteins embedded in the envelope also show helical ordering and frequently cluster in pairs, these properties are coordinated by the underlying matrix layer.In addition to packing multiple copies of the viral genome in the form of helical ribonucleoprotein complexes or nucleocapsids, virions also package an abundance of ring‐shaped assemblies likely formed of the viral nucleocapsid protein (N) and RNA. Graphical Abstract CryoEM and tomography analysis of the human pathogen RSV shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer that in turn coordinates helical ordering and clustering of viral glycoproteins. © The Author(s) 2021 |
| abstract_unstemmed |
Abstract Human respiratory syncytial virus (RSV) causes severe respiratory illness in children and the elderly. Here, using cryogenic electron microscopy and tomography combined with computational image analysis and three‐dimensional reconstruction, we show that there is extensive helical ordering of the envelope‐associated proteins and glycoproteins of RSV filamentous virions. We calculated a 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope. These data define a helical lattice of M‐dimers, showing how M is oriented relative to the viral envelope. Glycoproteins that stud the viral envelope were also found to be helically ordered, a property that was coordinated by the M‐layer. Furthermore, envelope glycoproteins clustered in pairs, a feature that may have implications for the conformation of fusion (F) glycoprotein epitopes that are the principal target for vaccine and monoclonal antibody development. We also report the presence, in authentic virus infections, of N‐RNA rings packaged within RSV virions. These data provide molecular insight into the organisation of the virion and the mechanism of its assembly. Synopsis CryoEM and tomography analysis of the human pathogen respiratory syncytial virus shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer, which in turn coordinates helical ordering and clustering of viral glycoproteins. 16 Å resolution sub‐tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope.Respiratory syncytial virus filamentous virions have a helically ordered matrix layer that is formed by a lattice of M dimers.Viral glycoproteins embedded in the envelope also show helical ordering and frequently cluster in pairs, these properties are coordinated by the underlying matrix layer.In addition to packing multiple copies of the viral genome in the form of helical ribonucleoprotein complexes or nucleocapsids, virions also package an abundance of ring‐shaped assemblies likely formed of the viral nucleocapsid protein (N) and RNA. Graphical Abstract CryoEM and tomography analysis of the human pathogen RSV shows the formation of filamentous virions that exhibit helical ordering of the envelope associated matrix protein layer that in turn coordinates helical ordering and clustering of viral glycoproteins. © The Author(s) 2021 |
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