Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer

HIV-1 uses its envelope protein (Env), a large glycoprotein present on the viral surface, to enter target cells. Env forms trimers on the viral surface. Structural studies of solubilized Env trimers have provided important insights into viral entry and antibody binding, but soluble trimers lack seve...
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Autor*in:	Jeong Hyun Lee [verfasserIn] Gabriel Ozorowski Andrew B Ward

Format:	Artikel
Sprache:	Englisch

Erschienen:	2016

Rechteinformationen:	Nutzungsrecht: Copyright © 2016, American Association for the Advancement of Science. © COPYRIGHT 2016 American Association for the Advancement of Science

Schlagwörter:	Human immunodeficiency virus--HIV Cells Glycoproteins HIV Envelope Protein gp120 - ultrastructure HIV-1 - physiology HIV Envelope Protein gp41 - genetics HIV Envelope Protein gp120 - genetics HIV Envelope Protein gp41 - ultrastructure Antibodies, Monoclonal - immunology HIV Envelope Protein gp120 - chemistry Antibodies, Neutralizing - immunology HIV Envelope Protein gp41 - chemistry Proteins Observations HIV (Viruses) Health aspects Structure

Übergeordnetes Werk:	Enthalten in: Science - Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883, 351(2016), 6277, Seite 1043-1048
Übergeordnetes Werk:	volume:351 ; year:2016 ; number:6277 ; pages:1043-1048

Links:	Volltext Link aufrufen Link aufrufen

DOI / URN:	10.1126/science.aad2450

Katalog-ID:	OLC1972821679

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520			\|a HIV-1 uses its envelope protein (Env), a large glycoprotein present on the viral surface, to enter target cells. Env forms trimers on the viral surface. Structural studies of solubilized Env trimers have provided important insights into viral entry and antibody binding, but soluble trimers lack several important insoluble regions of the native protein. Lee et al. used cryo-electron microscopy to solve the structure of a trimeric Env protein of HIV-1, missing only its cytoplasmic tail, in complex with broadly neutralizing antibodies. A more complete understanding of Env's structure may aid in vaccine design ef orts. Science, this issue p. 1043 The envelope glycoprotein trimer (Env) on the surface of HIV-1 recognizes CD4+ T cells and mediates viral entry. During this process, Env undergoes substantial conformational rearrangements, making it difficult to study in its native state. Soluble stabilized trimers have provided valuable insights into the Env structure, but they lack the hydrophobic membrane proximal external region (MPER, an important target of broadly neutralizing antibodies), the transmembrane domain, and the cytoplasmic tail. Here we present (i) a cryogenic electron microscopy (cryo-EM) structure of a clade B virus Env, which lacks only the cytoplasmic tail and is stabilized by the broadly neutralizing antibody PGT151, at a resolution of 4.2 angstroms and (ii) a reconstruction of this form of Env in complex with PGT151 and MPER-targeting antibody 10E8 at a resolution of 8.8 angstroms. These structures provide new insights into the wild-type Env structure.
540			\|a Nutzungsrecht: Copyright © 2016, American Association for the Advancement of Science.
540			\|a © COPYRIGHT 2016 American Association for the Advancement of Science
650		4	\|a Human immunodeficiency virus--HIV
650		4	\|a Cells
650		4	\|a Glycoproteins
650		4	\|a HIV Envelope Protein gp120 - ultrastructure
650		4	\|a HIV-1 - physiology
650		4	\|a HIV Envelope Protein gp41 - genetics
650		4	\|a HIV Envelope Protein gp120 - genetics
650		4	\|a HIV Envelope Protein gp41 - ultrastructure
650		4	\|a Antibodies, Monoclonal - immunology
650		4	\|a HIV Envelope Protein gp120 - chemistry
650		4	\|a Antibodies, Neutralizing - immunology
650		4	\|a HIV Envelope Protein gp41 - chemistry
650		4	\|a Proteins
650		4	\|a Observations
650		4	\|a HIV (Viruses)
650		4	\|a Health aspects
650		4	\|a Structure
700	0		\|a Gabriel Ozorowski \|4 oth
700	0		\|a Andrew B Ward \|4 oth
773	0	8	\|i Enthalten in \|t Science \|d Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 \|g 351(2016), 6277, Seite 1043-1048 \|w (DE-627)12931482X \|w (DE-600)128410-1 \|w (DE-576)014533189 \|x 0036-8075 \|7 nnns
773	1	8	\|g volume:351 \|g year:2016 \|g number:6277 \|g pages:1043-1048
856	4	1	\|u http://dx.doi.org/10.1126/science.aad2450 \|3 Volltext
856	4	2	\|u http://www.ncbi.nlm.nih.gov/pubmed/26941313
856	4	2	\|u http://search.proquest.com/docview/1770405630
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912			\|a SSG-OLC-PHA
912			\|a SSG-OLC-DE-84
912			\|a SSG-OPC-FOR
912			\|a GBV_ILN_11
912			\|a GBV_ILN_20
912			\|a GBV_ILN_21
912			\|a GBV_ILN_22
912			\|a GBV_ILN_23
912			\|a GBV_ILN_24
912			\|a GBV_ILN_30
912			\|a GBV_ILN_31
912			\|a GBV_ILN_39
912			\|a GBV_ILN_40
912			\|a GBV_ILN_47
912			\|a GBV_ILN_55
912			\|a GBV_ILN_59
912			\|a GBV_ILN_60
912			\|a GBV_ILN_62
912			\|a GBV_ILN_65
912			\|a GBV_ILN_69
912			\|a GBV_ILN_70
912			\|a GBV_ILN_73
912			\|a GBV_ILN_92
912			\|a GBV_ILN_101
912			\|a GBV_ILN_110
912			\|a GBV_ILN_120
912			\|a GBV_ILN_131
912			\|a GBV_ILN_170
912			\|a GBV_ILN_171
912			\|a GBV_ILN_179
912			\|a GBV_ILN_181
912			\|a GBV_ILN_211
912			\|a GBV_ILN_252
912			\|a GBV_ILN_259
912			\|a GBV_ILN_290
912			\|a GBV_ILN_600
912			\|a GBV_ILN_601
912			\|a GBV_ILN_647
912			\|a GBV_ILN_754
912			\|a GBV_ILN_2001
912			\|a GBV_ILN_2003
912			\|a GBV_ILN_2005
912			\|a GBV_ILN_2006
912			\|a GBV_ILN_2007
912			\|a GBV_ILN_2008
912			\|a GBV_ILN_2012
912			\|a GBV_ILN_2015
912			\|a GBV_ILN_2018
912			\|a GBV_ILN_2020
912			\|a GBV_ILN_2026
912			\|a GBV_ILN_2027
912			\|a GBV_ILN_2116
912			\|a GBV_ILN_2120
912			\|a GBV_ILN_2121
912			\|a GBV_ILN_2173
912			\|a GBV_ILN_2219
912			\|a GBV_ILN_2221
912			\|a GBV_ILN_2279
912			\|a GBV_ILN_2286
912			\|a GBV_ILN_4012
912			\|a GBV_ILN_4035
912			\|a GBV_ILN_4036
912			\|a GBV_ILN_4125
912			\|a GBV_ILN_4219
912			\|a GBV_ILN_4251
912			\|a GBV_ILN_4277
912			\|a GBV_ILN_4302
912			\|a GBV_ILN_4305
912			\|a GBV_ILN_4306
912			\|a GBV_ILN_4307
912			\|a GBV_ILN_4310
912			\|a GBV_ILN_4314
912			\|a GBV_ILN_4317
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912			\|a GBV_ILN_4320
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publishDate	2016
allfields	10.1126/science.aad2450 doi PQ20160430 (DE-627)OLC1972821679 (DE-599)GBVOLC1972821679 (PRQ)c2034-4b618f9ba8a7e9fad8537115d099477a404313131a676da3a5d1da690c76d3a0 (KEY)0063888920160000351627701043cryoemstructureofanativefullyglycosylatedcleavedhi DE-627 ger DE-627 rakwb eng 500 DNB LING fid Jeong Hyun Lee verfasserin aut Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier HIV-1 uses its envelope protein (Env), a large glycoprotein present on the viral surface, to enter target cells. Env forms trimers on the viral surface. Structural studies of solubilized Env trimers have provided important insights into viral entry and antibody binding, but soluble trimers lack several important insoluble regions of the native protein. Lee et al. used cryo-electron microscopy to solve the structure of a trimeric Env protein of HIV-1, missing only its cytoplasmic tail, in complex with broadly neutralizing antibodies. A more complete understanding of Env's structure may aid in vaccine design ef orts. Science, this issue p. 1043 The envelope glycoprotein trimer (Env) on the surface of HIV-1 recognizes CD4+ T cells and mediates viral entry. During this process, Env undergoes substantial conformational rearrangements, making it difficult to study in its native state. Soluble stabilized trimers have provided valuable insights into the Env structure, but they lack the hydrophobic membrane proximal external region (MPER, an important target of broadly neutralizing antibodies), the transmembrane domain, and the cytoplasmic tail. Here we present (i) a cryogenic electron microscopy (cryo-EM) structure of a clade B virus Env, which lacks only the cytoplasmic tail and is stabilized by the broadly neutralizing antibody PGT151, at a resolution of 4.2 angstroms and (ii) a reconstruction of this form of Env in complex with PGT151 and MPER-targeting antibody 10E8 at a resolution of 8.8 angstroms. These structures provide new insights into the wild-type Env structure. Nutzungsrecht: Copyright © 2016, American Association for the Advancement of Science. © COPYRIGHT 2016 American Association for the Advancement of Science Human immunodeficiency virus--HIV Cells Glycoproteins HIV Envelope Protein gp120 - ultrastructure HIV-1 - physiology HIV Envelope Protein gp41 - genetics HIV Envelope Protein gp120 - genetics HIV Envelope Protein gp41 - ultrastructure Antibodies, Monoclonal - immunology HIV Envelope Protein gp120 - chemistry Antibodies, Neutralizing - immunology HIV Envelope Protein gp41 - chemistry Proteins Observations HIV (Viruses) Health aspects Structure Gabriel Ozorowski oth Andrew B Ward oth Enthalten in Science Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 351(2016), 6277, Seite 1043-1048 (DE-627)12931482X (DE-600)128410-1 (DE-576)014533189 0036-8075 nnns volume:351 year:2016 number:6277 pages:1043-1048 http://dx.doi.org/10.1126/science.aad2450 Volltext http://www.ncbi.nlm.nih.gov/pubmed/26941313 http://search.proquest.com/docview/1770405630 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-IBL SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_30 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_92 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_131 GBV_ILN_170 GBV_ILN_171 GBV_ILN_179 GBV_ILN_181 GBV_ILN_211 GBV_ILN_252 GBV_ILN_259 GBV_ILN_290 GBV_ILN_600 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2012 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2173 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4320 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4700 AR 351 2016 6277 1043-1048
spelling	10.1126/science.aad2450 doi PQ20160430 (DE-627)OLC1972821679 (DE-599)GBVOLC1972821679 (PRQ)c2034-4b618f9ba8a7e9fad8537115d099477a404313131a676da3a5d1da690c76d3a0 (KEY)0063888920160000351627701043cryoemstructureofanativefullyglycosylatedcleavedhi DE-627 ger DE-627 rakwb eng 500 DNB LING fid Jeong Hyun Lee verfasserin aut Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier HIV-1 uses its envelope protein (Env), a large glycoprotein present on the viral surface, to enter target cells. Env forms trimers on the viral surface. Structural studies of solubilized Env trimers have provided important insights into viral entry and antibody binding, but soluble trimers lack several important insoluble regions of the native protein. Lee et al. used cryo-electron microscopy to solve the structure of a trimeric Env protein of HIV-1, missing only its cytoplasmic tail, in complex with broadly neutralizing antibodies. A more complete understanding of Env's structure may aid in vaccine design ef orts. Science, this issue p. 1043 The envelope glycoprotein trimer (Env) on the surface of HIV-1 recognizes CD4+ T cells and mediates viral entry. During this process, Env undergoes substantial conformational rearrangements, making it difficult to study in its native state. Soluble stabilized trimers have provided valuable insights into the Env structure, but they lack the hydrophobic membrane proximal external region (MPER, an important target of broadly neutralizing antibodies), the transmembrane domain, and the cytoplasmic tail. Here we present (i) a cryogenic electron microscopy (cryo-EM) structure of a clade B virus Env, which lacks only the cytoplasmic tail and is stabilized by the broadly neutralizing antibody PGT151, at a resolution of 4.2 angstroms and (ii) a reconstruction of this form of Env in complex with PGT151 and MPER-targeting antibody 10E8 at a resolution of 8.8 angstroms. These structures provide new insights into the wild-type Env structure. Nutzungsrecht: Copyright © 2016, American Association for the Advancement of Science. © COPYRIGHT 2016 American Association for the Advancement of Science Human immunodeficiency virus--HIV Cells Glycoproteins HIV Envelope Protein gp120 - ultrastructure HIV-1 - physiology HIV Envelope Protein gp41 - genetics HIV Envelope Protein gp120 - genetics HIV Envelope Protein gp41 - ultrastructure Antibodies, Monoclonal - immunology HIV Envelope Protein gp120 - chemistry Antibodies, Neutralizing - immunology HIV Envelope Protein gp41 - chemistry Proteins Observations HIV (Viruses) Health aspects Structure Gabriel Ozorowski oth Andrew B Ward oth Enthalten in Science Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 351(2016), 6277, Seite 1043-1048 (DE-627)12931482X (DE-600)128410-1 (DE-576)014533189 0036-8075 nnns volume:351 year:2016 number:6277 pages:1043-1048 http://dx.doi.org/10.1126/science.aad2450 Volltext http://www.ncbi.nlm.nih.gov/pubmed/26941313 http://search.proquest.com/docview/1770405630 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-IBL SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_30 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_92 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_131 GBV_ILN_170 GBV_ILN_171 GBV_ILN_179 GBV_ILN_181 GBV_ILN_211 GBV_ILN_252 GBV_ILN_259 GBV_ILN_290 GBV_ILN_600 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2012 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2173 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4320 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4700 AR 351 2016 6277 1043-1048
allfields_unstemmed	10.1126/science.aad2450 doi PQ20160430 (DE-627)OLC1972821679 (DE-599)GBVOLC1972821679 (PRQ)c2034-4b618f9ba8a7e9fad8537115d099477a404313131a676da3a5d1da690c76d3a0 (KEY)0063888920160000351627701043cryoemstructureofanativefullyglycosylatedcleavedhi DE-627 ger DE-627 rakwb eng 500 DNB LING fid Jeong Hyun Lee verfasserin aut Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier HIV-1 uses its envelope protein (Env), a large glycoprotein present on the viral surface, to enter target cells. Env forms trimers on the viral surface. Structural studies of solubilized Env trimers have provided important insights into viral entry and antibody binding, but soluble trimers lack several important insoluble regions of the native protein. Lee et al. used cryo-electron microscopy to solve the structure of a trimeric Env protein of HIV-1, missing only its cytoplasmic tail, in complex with broadly neutralizing antibodies. A more complete understanding of Env's structure may aid in vaccine design ef orts. Science, this issue p. 1043 The envelope glycoprotein trimer (Env) on the surface of HIV-1 recognizes CD4+ T cells and mediates viral entry. During this process, Env undergoes substantial conformational rearrangements, making it difficult to study in its native state. Soluble stabilized trimers have provided valuable insights into the Env structure, but they lack the hydrophobic membrane proximal external region (MPER, an important target of broadly neutralizing antibodies), the transmembrane domain, and the cytoplasmic tail. Here we present (i) a cryogenic electron microscopy (cryo-EM) structure of a clade B virus Env, which lacks only the cytoplasmic tail and is stabilized by the broadly neutralizing antibody PGT151, at a resolution of 4.2 angstroms and (ii) a reconstruction of this form of Env in complex with PGT151 and MPER-targeting antibody 10E8 at a resolution of 8.8 angstroms. These structures provide new insights into the wild-type Env structure. Nutzungsrecht: Copyright © 2016, American Association for the Advancement of Science. © COPYRIGHT 2016 American Association for the Advancement of Science Human immunodeficiency virus--HIV Cells Glycoproteins HIV Envelope Protein gp120 - ultrastructure HIV-1 - physiology HIV Envelope Protein gp41 - genetics HIV Envelope Protein gp120 - genetics HIV Envelope Protein gp41 - ultrastructure Antibodies, Monoclonal - immunology HIV Envelope Protein gp120 - chemistry Antibodies, Neutralizing - immunology HIV Envelope Protein gp41 - chemistry Proteins Observations HIV (Viruses) Health aspects Structure Gabriel Ozorowski oth Andrew B Ward oth Enthalten in Science Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 351(2016), 6277, Seite 1043-1048 (DE-627)12931482X (DE-600)128410-1 (DE-576)014533189 0036-8075 nnns volume:351 year:2016 number:6277 pages:1043-1048 http://dx.doi.org/10.1126/science.aad2450 Volltext http://www.ncbi.nlm.nih.gov/pubmed/26941313 http://search.proquest.com/docview/1770405630 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-IBL SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_30 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_92 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_131 GBV_ILN_170 GBV_ILN_171 GBV_ILN_179 GBV_ILN_181 GBV_ILN_211 GBV_ILN_252 GBV_ILN_259 GBV_ILN_290 GBV_ILN_600 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2012 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2173 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4320 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4700 AR 351 2016 6277 1043-1048
allfieldsGer	10.1126/science.aad2450 doi PQ20160430 (DE-627)OLC1972821679 (DE-599)GBVOLC1972821679 (PRQ)c2034-4b618f9ba8a7e9fad8537115d099477a404313131a676da3a5d1da690c76d3a0 (KEY)0063888920160000351627701043cryoemstructureofanativefullyglycosylatedcleavedhi DE-627 ger DE-627 rakwb eng 500 DNB LING fid Jeong Hyun Lee verfasserin aut Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier HIV-1 uses its envelope protein (Env), a large glycoprotein present on the viral surface, to enter target cells. Env forms trimers on the viral surface. Structural studies of solubilized Env trimers have provided important insights into viral entry and antibody binding, but soluble trimers lack several important insoluble regions of the native protein. Lee et al. used cryo-electron microscopy to solve the structure of a trimeric Env protein of HIV-1, missing only its cytoplasmic tail, in complex with broadly neutralizing antibodies. A more complete understanding of Env's structure may aid in vaccine design ef orts. Science, this issue p. 1043 The envelope glycoprotein trimer (Env) on the surface of HIV-1 recognizes CD4+ T cells and mediates viral entry. During this process, Env undergoes substantial conformational rearrangements, making it difficult to study in its native state. Soluble stabilized trimers have provided valuable insights into the Env structure, but they lack the hydrophobic membrane proximal external region (MPER, an important target of broadly neutralizing antibodies), the transmembrane domain, and the cytoplasmic tail. Here we present (i) a cryogenic electron microscopy (cryo-EM) structure of a clade B virus Env, which lacks only the cytoplasmic tail and is stabilized by the broadly neutralizing antibody PGT151, at a resolution of 4.2 angstroms and (ii) a reconstruction of this form of Env in complex with PGT151 and MPER-targeting antibody 10E8 at a resolution of 8.8 angstroms. These structures provide new insights into the wild-type Env structure. Nutzungsrecht: Copyright © 2016, American Association for the Advancement of Science. © COPYRIGHT 2016 American Association for the Advancement of Science Human immunodeficiency virus--HIV Cells Glycoproteins HIV Envelope Protein gp120 - ultrastructure HIV-1 - physiology HIV Envelope Protein gp41 - genetics HIV Envelope Protein gp120 - genetics HIV Envelope Protein gp41 - ultrastructure Antibodies, Monoclonal - immunology HIV Envelope Protein gp120 - chemistry Antibodies, Neutralizing - immunology HIV Envelope Protein gp41 - chemistry Proteins Observations HIV (Viruses) Health aspects Structure Gabriel Ozorowski oth Andrew B Ward oth Enthalten in Science Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 351(2016), 6277, Seite 1043-1048 (DE-627)12931482X (DE-600)128410-1 (DE-576)014533189 0036-8075 nnns volume:351 year:2016 number:6277 pages:1043-1048 http://dx.doi.org/10.1126/science.aad2450 Volltext http://www.ncbi.nlm.nih.gov/pubmed/26941313 http://search.proquest.com/docview/1770405630 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-IBL SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_30 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_92 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_131 GBV_ILN_170 GBV_ILN_171 GBV_ILN_179 GBV_ILN_181 GBV_ILN_211 GBV_ILN_252 GBV_ILN_259 GBV_ILN_290 GBV_ILN_600 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2012 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2173 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4320 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4700 AR 351 2016 6277 1043-1048
allfieldsSound	10.1126/science.aad2450 doi PQ20160430 (DE-627)OLC1972821679 (DE-599)GBVOLC1972821679 (PRQ)c2034-4b618f9ba8a7e9fad8537115d099477a404313131a676da3a5d1da690c76d3a0 (KEY)0063888920160000351627701043cryoemstructureofanativefullyglycosylatedcleavedhi DE-627 ger DE-627 rakwb eng 500 DNB LING fid Jeong Hyun Lee verfasserin aut Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer 2016 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier HIV-1 uses its envelope protein (Env), a large glycoprotein present on the viral surface, to enter target cells. Env forms trimers on the viral surface. Structural studies of solubilized Env trimers have provided important insights into viral entry and antibody binding, but soluble trimers lack several important insoluble regions of the native protein. Lee et al. used cryo-electron microscopy to solve the structure of a trimeric Env protein of HIV-1, missing only its cytoplasmic tail, in complex with broadly neutralizing antibodies. A more complete understanding of Env's structure may aid in vaccine design ef orts. Science, this issue p. 1043 The envelope glycoprotein trimer (Env) on the surface of HIV-1 recognizes CD4+ T cells and mediates viral entry. During this process, Env undergoes substantial conformational rearrangements, making it difficult to study in its native state. Soluble stabilized trimers have provided valuable insights into the Env structure, but they lack the hydrophobic membrane proximal external region (MPER, an important target of broadly neutralizing antibodies), the transmembrane domain, and the cytoplasmic tail. Here we present (i) a cryogenic electron microscopy (cryo-EM) structure of a clade B virus Env, which lacks only the cytoplasmic tail and is stabilized by the broadly neutralizing antibody PGT151, at a resolution of 4.2 angstroms and (ii) a reconstruction of this form of Env in complex with PGT151 and MPER-targeting antibody 10E8 at a resolution of 8.8 angstroms. These structures provide new insights into the wild-type Env structure. Nutzungsrecht: Copyright © 2016, American Association for the Advancement of Science. © COPYRIGHT 2016 American Association for the Advancement of Science Human immunodeficiency virus--HIV Cells Glycoproteins HIV Envelope Protein gp120 - ultrastructure HIV-1 - physiology HIV Envelope Protein gp41 - genetics HIV Envelope Protein gp120 - genetics HIV Envelope Protein gp41 - ultrastructure Antibodies, Monoclonal - immunology HIV Envelope Protein gp120 - chemistry Antibodies, Neutralizing - immunology HIV Envelope Protein gp41 - chemistry Proteins Observations HIV (Viruses) Health aspects Structure Gabriel Ozorowski oth Andrew B Ward oth Enthalten in Science Washington, DC : AAAS, American Assoc. for the Advancement of Science, 1883 351(2016), 6277, Seite 1043-1048 (DE-627)12931482X (DE-600)128410-1 (DE-576)014533189 0036-8075 nnns volume:351 year:2016 number:6277 pages:1043-1048 http://dx.doi.org/10.1126/science.aad2450 Volltext http://www.ncbi.nlm.nih.gov/pubmed/26941313 http://search.proquest.com/docview/1770405630 GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-LING SSG-OLC-PHY SSG-OLC-CHE SSG-OLC-MAT SSG-OLC-FOR SSG-OLC-SPO SSG-OLC-IBL SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_30 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_47 GBV_ILN_55 GBV_ILN_59 GBV_ILN_60 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_92 GBV_ILN_101 GBV_ILN_110 GBV_ILN_120 GBV_ILN_131 GBV_ILN_170 GBV_ILN_171 GBV_ILN_179 GBV_ILN_181 GBV_ILN_211 GBV_ILN_252 GBV_ILN_259 GBV_ILN_290 GBV_ILN_600 GBV_ILN_601 GBV_ILN_647 GBV_ILN_754 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2012 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2116 GBV_ILN_2120 GBV_ILN_2121 GBV_ILN_2173 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_2279 GBV_ILN_2286 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4251 GBV_ILN_4277 GBV_ILN_4302 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4314 GBV_ILN_4317 GBV_ILN_4318 GBV_ILN_4320 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4700 AR 351 2016 6277 1043-1048
language	English
source	Enthalten in Science 351(2016), 6277, Seite 1043-1048 volume:351 year:2016 number:6277 pages:1043-1048
sourceStr	Enthalten in Science 351(2016), 6277, Seite 1043-1048 volume:351 year:2016 number:6277 pages:1043-1048
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Human immunodeficiency virus--HIV Cells Glycoproteins HIV Envelope Protein gp120 - ultrastructure HIV-1 - physiology HIV Envelope Protein gp41 - genetics HIV Envelope Protein gp120 - genetics HIV Envelope Protein gp41 - ultrastructure Antibodies, Monoclonal - immunology HIV Envelope Protein gp120 - chemistry Antibodies, Neutralizing - immunology HIV Envelope Protein gp41 - chemistry Proteins Observations HIV (Viruses) Health aspects Structure
dewey-raw	500
isfreeaccess_bool	false
container_title	Science
authorswithroles_txt_mv	Jeong Hyun Lee @@aut@@ Gabriel Ozorowski @@oth@@ Andrew B Ward @@oth@@
publishDateDaySort_date	2016-01-01T00:00:00Z
hierarchy_top_id	12931482X
dewey-sort	3500
id	OLC1972821679
language_de	englisch
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author	Jeong Hyun Lee
spellingShingle	Jeong Hyun Lee ddc 500 fid LING misc Human immunodeficiency virus--HIV misc Cells misc Glycoproteins misc HIV Envelope Protein gp120 - ultrastructure misc HIV-1 - physiology misc HIV Envelope Protein gp41 - genetics misc HIV Envelope Protein gp120 - genetics misc HIV Envelope Protein gp41 - ultrastructure misc Antibodies, Monoclonal - immunology misc HIV Envelope Protein gp120 - chemistry misc Antibodies, Neutralizing - immunology misc HIV Envelope Protein gp41 - chemistry misc Proteins misc Observations misc HIV (Viruses) misc Health aspects misc Structure Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer
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topic_title	500 DNB LING fid Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer Human immunodeficiency virus--HIV Cells Glycoproteins HIV Envelope Protein gp120 - ultrastructure HIV-1 - physiology HIV Envelope Protein gp41 - genetics HIV Envelope Protein gp120 - genetics HIV Envelope Protein gp41 - ultrastructure Antibodies, Monoclonal - immunology HIV Envelope Protein gp120 - chemistry Antibodies, Neutralizing - immunology HIV Envelope Protein gp41 - chemistry Proteins Observations HIV (Viruses) Health aspects Structure
topic	ddc 500 fid LING misc Human immunodeficiency virus--HIV misc Cells misc Glycoproteins misc HIV Envelope Protein gp120 - ultrastructure misc HIV-1 - physiology misc HIV Envelope Protein gp41 - genetics misc HIV Envelope Protein gp120 - genetics misc HIV Envelope Protein gp41 - ultrastructure misc Antibodies, Monoclonal - immunology misc HIV Envelope Protein gp120 - chemistry misc Antibodies, Neutralizing - immunology misc HIV Envelope Protein gp41 - chemistry misc Proteins misc Observations misc HIV (Viruses) misc Health aspects misc Structure
topic_unstemmed	ddc 500 fid LING misc Human immunodeficiency virus--HIV misc Cells misc Glycoproteins misc HIV Envelope Protein gp120 - ultrastructure misc HIV-1 - physiology misc HIV Envelope Protein gp41 - genetics misc HIV Envelope Protein gp120 - genetics misc HIV Envelope Protein gp41 - ultrastructure misc Antibodies, Monoclonal - immunology misc HIV Envelope Protein gp120 - chemistry misc Antibodies, Neutralizing - immunology misc HIV Envelope Protein gp41 - chemistry misc Proteins misc Observations misc HIV (Viruses) misc Health aspects misc Structure
topic_browse	ddc 500 fid LING misc Human immunodeficiency virus--HIV misc Cells misc Glycoproteins misc HIV Envelope Protein gp120 - ultrastructure misc HIV-1 - physiology misc HIV Envelope Protein gp41 - genetics misc HIV Envelope Protein gp120 - genetics misc HIV Envelope Protein gp41 - ultrastructure misc Antibodies, Monoclonal - immunology misc HIV Envelope Protein gp120 - chemistry misc Antibodies, Neutralizing - immunology misc HIV Envelope Protein gp41 - chemistry misc Proteins misc Observations misc HIV (Viruses) misc Health aspects misc Structure
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title	Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer
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title_full	Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer
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title_sort	cryo-em structure of a native, fully glycosylated, cleaved hiv-1 envelope trimer
title_auth	Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer
abstract	HIV-1 uses its envelope protein (Env), a large glycoprotein present on the viral surface, to enter target cells. Env forms trimers on the viral surface. Structural studies of solubilized Env trimers have provided important insights into viral entry and antibody binding, but soluble trimers lack several important insoluble regions of the native protein. Lee et al. used cryo-electron microscopy to solve the structure of a trimeric Env protein of HIV-1, missing only its cytoplasmic tail, in complex with broadly neutralizing antibodies. A more complete understanding of Env's structure may aid in vaccine design ef orts. Science, this issue p. 1043 The envelope glycoprotein trimer (Env) on the surface of HIV-1 recognizes CD4+ T cells and mediates viral entry. During this process, Env undergoes substantial conformational rearrangements, making it difficult to study in its native state. Soluble stabilized trimers have provided valuable insights into the Env structure, but they lack the hydrophobic membrane proximal external region (MPER, an important target of broadly neutralizing antibodies), the transmembrane domain, and the cytoplasmic tail. Here we present (i) a cryogenic electron microscopy (cryo-EM) structure of a clade B virus Env, which lacks only the cytoplasmic tail and is stabilized by the broadly neutralizing antibody PGT151, at a resolution of 4.2 angstroms and (ii) a reconstruction of this form of Env in complex with PGT151 and MPER-targeting antibody 10E8 at a resolution of 8.8 angstroms. These structures provide new insights into the wild-type Env structure.
abstractGer	HIV-1 uses its envelope protein (Env), a large glycoprotein present on the viral surface, to enter target cells. Env forms trimers on the viral surface. Structural studies of solubilized Env trimers have provided important insights into viral entry and antibody binding, but soluble trimers lack several important insoluble regions of the native protein. Lee et al. used cryo-electron microscopy to solve the structure of a trimeric Env protein of HIV-1, missing only its cytoplasmic tail, in complex with broadly neutralizing antibodies. A more complete understanding of Env's structure may aid in vaccine design ef orts. Science, this issue p. 1043 The envelope glycoprotein trimer (Env) on the surface of HIV-1 recognizes CD4+ T cells and mediates viral entry. During this process, Env undergoes substantial conformational rearrangements, making it difficult to study in its native state. Soluble stabilized trimers have provided valuable insights into the Env structure, but they lack the hydrophobic membrane proximal external region (MPER, an important target of broadly neutralizing antibodies), the transmembrane domain, and the cytoplasmic tail. Here we present (i) a cryogenic electron microscopy (cryo-EM) structure of a clade B virus Env, which lacks only the cytoplasmic tail and is stabilized by the broadly neutralizing antibody PGT151, at a resolution of 4.2 angstroms and (ii) a reconstruction of this form of Env in complex with PGT151 and MPER-targeting antibody 10E8 at a resolution of 8.8 angstroms. These structures provide new insights into the wild-type Env structure.
abstract_unstemmed	HIV-1 uses its envelope protein (Env), a large glycoprotein present on the viral surface, to enter target cells. Env forms trimers on the viral surface. Structural studies of solubilized Env trimers have provided important insights into viral entry and antibody binding, but soluble trimers lack several important insoluble regions of the native protein. Lee et al. used cryo-electron microscopy to solve the structure of a trimeric Env protein of HIV-1, missing only its cytoplasmic tail, in complex with broadly neutralizing antibodies. A more complete understanding of Env's structure may aid in vaccine design ef orts. Science, this issue p. 1043 The envelope glycoprotein trimer (Env) on the surface of HIV-1 recognizes CD4+ T cells and mediates viral entry. During this process, Env undergoes substantial conformational rearrangements, making it difficult to study in its native state. Soluble stabilized trimers have provided valuable insights into the Env structure, but they lack the hydrophobic membrane proximal external region (MPER, an important target of broadly neutralizing antibodies), the transmembrane domain, and the cytoplasmic tail. Here we present (i) a cryogenic electron microscopy (cryo-EM) structure of a clade B virus Env, which lacks only the cytoplasmic tail and is stabilized by the broadly neutralizing antibody PGT151, at a resolution of 4.2 angstroms and (ii) a reconstruction of this form of Env in complex with PGT151 and MPER-targeting antibody 10E8 at a resolution of 8.8 angstroms. These structures provide new insights into the wild-type Env structure.
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container_issue	6277
title_short	Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer
url	http://dx.doi.org/10.1126/science.aad2450 http://www.ncbi.nlm.nih.gov/pubmed/26941313 http://search.proquest.com/docview/1770405630
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fullrecord_marcxml	<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a2200265 4500</leader><controlfield tag="001">OLC1972821679</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230714183635.0</controlfield><controlfield tag="007">tu</controlfield><controlfield tag="008">160427s2016 xx \|\|\|\|\| 00\| \|\|eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1126/science.aad2450</subfield><subfield code="2">doi</subfield></datafield><datafield tag="028" ind1="5" ind2="2"><subfield code="a">PQ20160430</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)OLC1972821679</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVOLC1972821679</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(PRQ)c2034-4b618f9ba8a7e9fad8537115d099477a404313131a676da3a5d1da690c76d3a0</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(KEY)0063888920160000351627701043cryoemstructureofanativefullyglycosylatedcleavedhi</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="082" ind1="0" ind2="4"><subfield code="a">500</subfield><subfield code="q">DNB</subfield></datafield><datafield tag="084" ind1=" " ind2=" "><subfield code="a">LING</subfield><subfield code="2">fid</subfield></datafield><datafield tag="100" ind1="0" ind2=" "><subfield code="a">Jeong Hyun Lee</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2016</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">ohne Hilfsmittel zu benutzen</subfield><subfield code="b">n</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Band</subfield><subfield code="b">nc</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">HIV-1 uses its envelope protein (Env), a large glycoprotein present on the viral surface, to enter target cells. Env forms trimers on the viral surface. Structural studies of solubilized Env trimers have provided important insights into viral entry and antibody binding, but soluble trimers lack several important insoluble regions of the native protein. Lee et al. used cryo-electron microscopy to solve the structure of a trimeric Env protein of HIV-1, missing only its cytoplasmic tail, in complex with broadly neutralizing antibodies. A more complete understanding of Env's structure may aid in vaccine design ef orts. Science, this issue p. 1043 The envelope glycoprotein trimer (Env) on the surface of HIV-1 recognizes CD4+ T cells and mediates viral entry. During this process, Env undergoes substantial conformational rearrangements, making it difficult to study in its native state. Soluble stabilized trimers have provided valuable insights into the Env structure, but they lack the hydrophobic membrane proximal external region (MPER, an important target of broadly neutralizing antibodies), the transmembrane domain, and the cytoplasmic tail. Here we present (i) a cryogenic electron microscopy (cryo-EM) structure of a clade B virus Env, which lacks only the cytoplasmic tail and is stabilized by the broadly neutralizing antibody PGT151, at a resolution of 4.2 angstroms and (ii) a reconstruction of this form of Env in complex with PGT151 and MPER-targeting antibody 10E8 at a resolution of 8.8 angstroms. These structures provide new insights into the wild-type Env structure.</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">Nutzungsrecht: Copyright © 2016, American Association for the Advancement of Science.</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">© COPYRIGHT 2016 American Association for the Advancement of Science</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Human immunodeficiency virus--HIV</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cells</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Glycoproteins</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">HIV Envelope Protein gp120 - ultrastructure</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">HIV-1 - physiology</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">HIV Envelope 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Cryo-EM structure of a native, fully glycosylated, cleaved HIV-1 envelope trimer

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