Deciphering the role of monosaccharides during phage infection of Staphylococcus aureus
Abstract As phages are extensively investigated as novel therapy tools but also as transfer agents for antibiotic resistance genes, thorough understanding of phage—host interactions becomes crucial. Prerequisite for phage infection is its adhesion to the host surface. Herein, we used atomic force mi...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Arbez, Baptiste [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2022 |
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| Schlagwörter: |
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| Anmerkung: |
© Tsinghua University Press 2022 |
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| Übergeordnetes Werk: |
Enthalten in: Nano research - [S.l.] : Tsinghua Press, 2008, 15(2022), 10 vom: 16. Juli, Seite 9234-9242 |
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| Übergeordnetes Werk: |
volume:15 ; year:2022 ; number:10 ; day:16 ; month:07 ; pages:9234-9242 |
| Links: |
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| DOI / URN: |
10.1007/s12274-022-4600-3 |
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| Katalog-ID: |
SPR051027208 |
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| 100 | 1 | |a Arbez, Baptiste |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Deciphering the role of monosaccharides during phage infection of Staphylococcus aureus |
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| 520 | |a Abstract As phages are extensively investigated as novel therapy tools but also as transfer agents for antibiotic resistance genes, thorough understanding of phage—host interactions becomes crucial. Prerequisite for phage infection is its adhesion to the host surface. Herein, we used atomic force microscopy-based single-particle force spectroscopy with phage-decorated tips to decipher the adhesion of phage 187 on living Staphylococcus aureus cells. We found that addition of free N-acetyl-D-glucosamine was able to decrease phage adhesion, suggesting that this monosaccharide plays major role in phage 187 infection of S. aureus. Moreover, phage 187 adhesion on monosaccharide-coated model surfaces combined with plaque forming unit counts suggested that a direct link can be established between the propensity to bind to a saccharide and the capability of the latter to inhibit phage infection. On a nanoscale level, single-particle force spectroscopy was successfully used to identify a major receptor required for phage 187 infection of S. aureus but also evidenced that this receptor was responsible for phage adhesion on host-cells. Our work demonstrates that single-particle force spectroscopy is a powerful platform to screen and predict the molecular target of phages on their host surfaces. | ||
| 650 | 4 | |a atomic force microscopy |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a single-particle force spectroscopy |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a phage 187 |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a phage—bacteria interactions |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Gardette, Marion |4 aut | |
| 700 | 1 | |a Gantzer, Christophe |4 aut | |
| 700 | 1 | |a Vilà, Neus |4 aut | |
| 700 | 1 | |a Bertrand, Isabelle |4 aut | |
| 700 | 1 | |a El-Kirat-Chatel, Sofiane |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Nano research |d [S.l.] : Tsinghua Press, 2008 |g 15(2022), 10 vom: 16. Juli, Seite 9234-9242 |w (DE-627)57375361X |w (DE-600)2442216-2 |x 1998-0000 |7 nnns |
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10.1007/s12274-022-4600-3 doi (DE-627)SPR051027208 (SPR)s12274-022-4600-3-e DE-627 ger DE-627 rakwb eng Arbez, Baptiste verfasserin aut Deciphering the role of monosaccharides during phage infection of Staphylococcus aureus 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Tsinghua University Press 2022 Abstract As phages are extensively investigated as novel therapy tools but also as transfer agents for antibiotic resistance genes, thorough understanding of phage—host interactions becomes crucial. Prerequisite for phage infection is its adhesion to the host surface. Herein, we used atomic force microscopy-based single-particle force spectroscopy with phage-decorated tips to decipher the adhesion of phage 187 on living Staphylococcus aureus cells. We found that addition of free N-acetyl-D-glucosamine was able to decrease phage adhesion, suggesting that this monosaccharide plays major role in phage 187 infection of S. aureus. Moreover, phage 187 adhesion on monosaccharide-coated model surfaces combined with plaque forming unit counts suggested that a direct link can be established between the propensity to bind to a saccharide and the capability of the latter to inhibit phage infection. On a nanoscale level, single-particle force spectroscopy was successfully used to identify a major receptor required for phage 187 infection of S. aureus but also evidenced that this receptor was responsible for phage adhesion on host-cells. Our work demonstrates that single-particle force spectroscopy is a powerful platform to screen and predict the molecular target of phages on their host surfaces. atomic force microscopy (dpeaa)DE-He213 single-particle force spectroscopy (dpeaa)DE-He213 phage 187 (dpeaa)DE-He213 phage—bacteria interactions (dpeaa)DE-He213 Gardette, Marion aut Gantzer, Christophe aut Vilà, Neus aut Bertrand, Isabelle aut El-Kirat-Chatel, Sofiane aut Enthalten in Nano research [S.l.] : Tsinghua Press, 2008 15(2022), 10 vom: 16. Juli, Seite 9234-9242 (DE-627)57375361X (DE-600)2442216-2 1998-0000 nnns volume:15 year:2022 number:10 day:16 month:07 pages:9234-9242 https://dx.doi.org/10.1007/s12274-022-4600-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 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_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 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_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 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_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 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_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 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_4393 GBV_ILN_4700 AR 15 2022 10 16 07 9234-9242 |
| spelling |
10.1007/s12274-022-4600-3 doi (DE-627)SPR051027208 (SPR)s12274-022-4600-3-e DE-627 ger DE-627 rakwb eng Arbez, Baptiste verfasserin aut Deciphering the role of monosaccharides during phage infection of Staphylococcus aureus 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Tsinghua University Press 2022 Abstract As phages are extensively investigated as novel therapy tools but also as transfer agents for antibiotic resistance genes, thorough understanding of phage—host interactions becomes crucial. Prerequisite for phage infection is its adhesion to the host surface. Herein, we used atomic force microscopy-based single-particle force spectroscopy with phage-decorated tips to decipher the adhesion of phage 187 on living Staphylococcus aureus cells. We found that addition of free N-acetyl-D-glucosamine was able to decrease phage adhesion, suggesting that this monosaccharide plays major role in phage 187 infection of S. aureus. Moreover, phage 187 adhesion on monosaccharide-coated model surfaces combined with plaque forming unit counts suggested that a direct link can be established between the propensity to bind to a saccharide and the capability of the latter to inhibit phage infection. On a nanoscale level, single-particle force spectroscopy was successfully used to identify a major receptor required for phage 187 infection of S. aureus but also evidenced that this receptor was responsible for phage adhesion on host-cells. Our work demonstrates that single-particle force spectroscopy is a powerful platform to screen and predict the molecular target of phages on their host surfaces. atomic force microscopy (dpeaa)DE-He213 single-particle force spectroscopy (dpeaa)DE-He213 phage 187 (dpeaa)DE-He213 phage—bacteria interactions (dpeaa)DE-He213 Gardette, Marion aut Gantzer, Christophe aut Vilà, Neus aut Bertrand, Isabelle aut El-Kirat-Chatel, Sofiane aut Enthalten in Nano research [S.l.] : Tsinghua Press, 2008 15(2022), 10 vom: 16. Juli, Seite 9234-9242 (DE-627)57375361X (DE-600)2442216-2 1998-0000 nnns volume:15 year:2022 number:10 day:16 month:07 pages:9234-9242 https://dx.doi.org/10.1007/s12274-022-4600-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 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_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 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_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 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_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 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_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 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_4393 GBV_ILN_4700 AR 15 2022 10 16 07 9234-9242 |
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10.1007/s12274-022-4600-3 doi (DE-627)SPR051027208 (SPR)s12274-022-4600-3-e DE-627 ger DE-627 rakwb eng Arbez, Baptiste verfasserin aut Deciphering the role of monosaccharides during phage infection of Staphylococcus aureus 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Tsinghua University Press 2022 Abstract As phages are extensively investigated as novel therapy tools but also as transfer agents for antibiotic resistance genes, thorough understanding of phage—host interactions becomes crucial. Prerequisite for phage infection is its adhesion to the host surface. Herein, we used atomic force microscopy-based single-particle force spectroscopy with phage-decorated tips to decipher the adhesion of phage 187 on living Staphylococcus aureus cells. We found that addition of free N-acetyl-D-glucosamine was able to decrease phage adhesion, suggesting that this monosaccharide plays major role in phage 187 infection of S. aureus. Moreover, phage 187 adhesion on monosaccharide-coated model surfaces combined with plaque forming unit counts suggested that a direct link can be established between the propensity to bind to a saccharide and the capability of the latter to inhibit phage infection. On a nanoscale level, single-particle force spectroscopy was successfully used to identify a major receptor required for phage 187 infection of S. aureus but also evidenced that this receptor was responsible for phage adhesion on host-cells. Our work demonstrates that single-particle force spectroscopy is a powerful platform to screen and predict the molecular target of phages on their host surfaces. atomic force microscopy (dpeaa)DE-He213 single-particle force spectroscopy (dpeaa)DE-He213 phage 187 (dpeaa)DE-He213 phage—bacteria interactions (dpeaa)DE-He213 Gardette, Marion aut Gantzer, Christophe aut Vilà, Neus aut Bertrand, Isabelle aut El-Kirat-Chatel, Sofiane aut Enthalten in Nano research [S.l.] : Tsinghua Press, 2008 15(2022), 10 vom: 16. Juli, Seite 9234-9242 (DE-627)57375361X (DE-600)2442216-2 1998-0000 nnns volume:15 year:2022 number:10 day:16 month:07 pages:9234-9242 https://dx.doi.org/10.1007/s12274-022-4600-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 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_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 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_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 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_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 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_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 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_4393 GBV_ILN_4700 AR 15 2022 10 16 07 9234-9242 |
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10.1007/s12274-022-4600-3 doi (DE-627)SPR051027208 (SPR)s12274-022-4600-3-e DE-627 ger DE-627 rakwb eng Arbez, Baptiste verfasserin aut Deciphering the role of monosaccharides during phage infection of Staphylococcus aureus 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Tsinghua University Press 2022 Abstract As phages are extensively investigated as novel therapy tools but also as transfer agents for antibiotic resistance genes, thorough understanding of phage—host interactions becomes crucial. Prerequisite for phage infection is its adhesion to the host surface. Herein, we used atomic force microscopy-based single-particle force spectroscopy with phage-decorated tips to decipher the adhesion of phage 187 on living Staphylococcus aureus cells. We found that addition of free N-acetyl-D-glucosamine was able to decrease phage adhesion, suggesting that this monosaccharide plays major role in phage 187 infection of S. aureus. Moreover, phage 187 adhesion on monosaccharide-coated model surfaces combined with plaque forming unit counts suggested that a direct link can be established between the propensity to bind to a saccharide and the capability of the latter to inhibit phage infection. On a nanoscale level, single-particle force spectroscopy was successfully used to identify a major receptor required for phage 187 infection of S. aureus but also evidenced that this receptor was responsible for phage adhesion on host-cells. Our work demonstrates that single-particle force spectroscopy is a powerful platform to screen and predict the molecular target of phages on their host surfaces. atomic force microscopy (dpeaa)DE-He213 single-particle force spectroscopy (dpeaa)DE-He213 phage 187 (dpeaa)DE-He213 phage—bacteria interactions (dpeaa)DE-He213 Gardette, Marion aut Gantzer, Christophe aut Vilà, Neus aut Bertrand, Isabelle aut El-Kirat-Chatel, Sofiane aut Enthalten in Nano research [S.l.] : Tsinghua Press, 2008 15(2022), 10 vom: 16. Juli, Seite 9234-9242 (DE-627)57375361X (DE-600)2442216-2 1998-0000 nnns volume:15 year:2022 number:10 day:16 month:07 pages:9234-9242 https://dx.doi.org/10.1007/s12274-022-4600-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 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_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 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_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 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_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 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_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 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_4393 GBV_ILN_4700 AR 15 2022 10 16 07 9234-9242 |
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10.1007/s12274-022-4600-3 doi (DE-627)SPR051027208 (SPR)s12274-022-4600-3-e DE-627 ger DE-627 rakwb eng Arbez, Baptiste verfasserin aut Deciphering the role of monosaccharides during phage infection of Staphylococcus aureus 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Tsinghua University Press 2022 Abstract As phages are extensively investigated as novel therapy tools but also as transfer agents for antibiotic resistance genes, thorough understanding of phage—host interactions becomes crucial. Prerequisite for phage infection is its adhesion to the host surface. Herein, we used atomic force microscopy-based single-particle force spectroscopy with phage-decorated tips to decipher the adhesion of phage 187 on living Staphylococcus aureus cells. We found that addition of free N-acetyl-D-glucosamine was able to decrease phage adhesion, suggesting that this monosaccharide plays major role in phage 187 infection of S. aureus. Moreover, phage 187 adhesion on monosaccharide-coated model surfaces combined with plaque forming unit counts suggested that a direct link can be established between the propensity to bind to a saccharide and the capability of the latter to inhibit phage infection. On a nanoscale level, single-particle force spectroscopy was successfully used to identify a major receptor required for phage 187 infection of S. aureus but also evidenced that this receptor was responsible for phage adhesion on host-cells. Our work demonstrates that single-particle force spectroscopy is a powerful platform to screen and predict the molecular target of phages on their host surfaces. atomic force microscopy (dpeaa)DE-He213 single-particle force spectroscopy (dpeaa)DE-He213 phage 187 (dpeaa)DE-He213 phage—bacteria interactions (dpeaa)DE-He213 Gardette, Marion aut Gantzer, Christophe aut Vilà, Neus aut Bertrand, Isabelle aut El-Kirat-Chatel, Sofiane aut Enthalten in Nano research [S.l.] : Tsinghua Press, 2008 15(2022), 10 vom: 16. Juli, Seite 9234-9242 (DE-627)57375361X (DE-600)2442216-2 1998-0000 nnns volume:15 year:2022 number:10 day:16 month:07 pages:9234-9242 https://dx.doi.org/10.1007/s12274-022-4600-3 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 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_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 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_152 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 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_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 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_2065 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2118 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_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 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_4393 GBV_ILN_4700 AR 15 2022 10 16 07 9234-9242 |
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Enthalten in Nano research 15(2022), 10 vom: 16. Juli, Seite 9234-9242 volume:15 year:2022 number:10 day:16 month:07 pages:9234-9242 |
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Enthalten in Nano research 15(2022), 10 vom: 16. Juli, Seite 9234-9242 volume:15 year:2022 number:10 day:16 month:07 pages:9234-9242 |
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atomic force microscopy single-particle force spectroscopy phage 187 phage—bacteria interactions |
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Arbez, Baptiste @@aut@@ Gardette, Marion @@aut@@ Gantzer, Christophe @@aut@@ Vilà, Neus @@aut@@ Bertrand, Isabelle @@aut@@ El-Kirat-Chatel, Sofiane @@aut@@ |
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Arbez, Baptiste |
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Arbez, Baptiste misc atomic force microscopy misc single-particle force spectroscopy misc phage 187 misc phage—bacteria interactions Deciphering the role of monosaccharides during phage infection of Staphylococcus aureus |
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Deciphering the role of monosaccharides during phage infection of Staphylococcus aureus atomic force microscopy (dpeaa)DE-He213 single-particle force spectroscopy (dpeaa)DE-He213 phage 187 (dpeaa)DE-He213 phage—bacteria interactions (dpeaa)DE-He213 |
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Arbez, Baptiste Gardette, Marion Gantzer, Christophe Vilà, Neus Bertrand, Isabelle El-Kirat-Chatel, Sofiane |
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deciphering the role of monosaccharides during phage infection of staphylococcus aureus |
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Deciphering the role of monosaccharides during phage infection of Staphylococcus aureus |
| abstract |
Abstract As phages are extensively investigated as novel therapy tools but also as transfer agents for antibiotic resistance genes, thorough understanding of phage—host interactions becomes crucial. Prerequisite for phage infection is its adhesion to the host surface. Herein, we used atomic force microscopy-based single-particle force spectroscopy with phage-decorated tips to decipher the adhesion of phage 187 on living Staphylococcus aureus cells. We found that addition of free N-acetyl-D-glucosamine was able to decrease phage adhesion, suggesting that this monosaccharide plays major role in phage 187 infection of S. aureus. Moreover, phage 187 adhesion on monosaccharide-coated model surfaces combined with plaque forming unit counts suggested that a direct link can be established between the propensity to bind to a saccharide and the capability of the latter to inhibit phage infection. On a nanoscale level, single-particle force spectroscopy was successfully used to identify a major receptor required for phage 187 infection of S. aureus but also evidenced that this receptor was responsible for phage adhesion on host-cells. Our work demonstrates that single-particle force spectroscopy is a powerful platform to screen and predict the molecular target of phages on their host surfaces. © Tsinghua University Press 2022 |
| abstractGer |
Abstract As phages are extensively investigated as novel therapy tools but also as transfer agents for antibiotic resistance genes, thorough understanding of phage—host interactions becomes crucial. Prerequisite for phage infection is its adhesion to the host surface. Herein, we used atomic force microscopy-based single-particle force spectroscopy with phage-decorated tips to decipher the adhesion of phage 187 on living Staphylococcus aureus cells. We found that addition of free N-acetyl-D-glucosamine was able to decrease phage adhesion, suggesting that this monosaccharide plays major role in phage 187 infection of S. aureus. Moreover, phage 187 adhesion on monosaccharide-coated model surfaces combined with plaque forming unit counts suggested that a direct link can be established between the propensity to bind to a saccharide and the capability of the latter to inhibit phage infection. On a nanoscale level, single-particle force spectroscopy was successfully used to identify a major receptor required for phage 187 infection of S. aureus but also evidenced that this receptor was responsible for phage adhesion on host-cells. Our work demonstrates that single-particle force spectroscopy is a powerful platform to screen and predict the molecular target of phages on their host surfaces. © Tsinghua University Press 2022 |
| abstract_unstemmed |
Abstract As phages are extensively investigated as novel therapy tools but also as transfer agents for antibiotic resistance genes, thorough understanding of phage—host interactions becomes crucial. Prerequisite for phage infection is its adhesion to the host surface. Herein, we used atomic force microscopy-based single-particle force spectroscopy with phage-decorated tips to decipher the adhesion of phage 187 on living Staphylococcus aureus cells. We found that addition of free N-acetyl-D-glucosamine was able to decrease phage adhesion, suggesting that this monosaccharide plays major role in phage 187 infection of S. aureus. Moreover, phage 187 adhesion on monosaccharide-coated model surfaces combined with plaque forming unit counts suggested that a direct link can be established between the propensity to bind to a saccharide and the capability of the latter to inhibit phage infection. On a nanoscale level, single-particle force spectroscopy was successfully used to identify a major receptor required for phage 187 infection of S. aureus but also evidenced that this receptor was responsible for phage adhesion on host-cells. Our work demonstrates that single-particle force spectroscopy is a powerful platform to screen and predict the molecular target of phages on their host surfaces. © Tsinghua University Press 2022 |
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| title_short |
Deciphering the role of monosaccharides during phage infection of Staphylococcus aureus |
| url |
https://dx.doi.org/10.1007/s12274-022-4600-3 |
| remote_bool |
true |
| author2 |
Gardette, Marion Gantzer, Christophe Vilà, Neus Bertrand, Isabelle El-Kirat-Chatel, Sofiane |
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Gardette, Marion Gantzer, Christophe Vilà, Neus Bertrand, Isabelle El-Kirat-Chatel, Sofiane |
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| doi_str |
10.1007/s12274-022-4600-3 |
| up_date |
2024-07-03T19:19:44.150Z |
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| score |
7.3995275 |