IRIS publication 243940012
Viral infection modulation and neutralization by camelid nanobodies
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TY - JOUR - Desmyter, A,Farenc, C,Mahony, J,Spinelli, S,Bebeacua, C,Blangy, S,Veesler, D,van Sinderen, D,Cambillau, C - 2013 - April - Proceedings of The National Academy of Sciences of The United States of America - Viral infection modulation and neutralization by camelid nanobodies - Validated - Altmetric: 1 () - LACTOCOCCUS-LACTIS PHAGES RECEPTOR-BINDING PROTEIN ELECTRON-MICROSCOPY MAXIMUM-LIKELIHOOD ANTIBODY FRAGMENT CRYSTAL-STRUCTURE ESCHERICHIA-COLI TAIL BASEPLATE MECHANISM - 110 - 1371 - 1379 - Lactococcal phages belong to a large family of Siphoviridae and infect Lactococcus lactis, a Gram-positive bacterium used in commercial dairy fermentations. These phages are believed to recognize and bind specifically to pellicle polysaccharides covering the entire bacterium. The phage TP901-1 baseplate, located at the tip of the tail, harbors 18 trimeric receptor binding proteins (RBPs) promoting adhesion to a specific lactococcal strain. Phage TP901-1 adhesion does not require major conformational changes or Ca2+, which contrasts other lactococcal phages. Here, we produced and characterized llama nanobodies raised against the purified baseplate and the Tal protein of phage TP901-1 as tools to dissect the molecular determinants of phage TP901-1 infection. Using a set of complementary techniques, surface plasmon resonance, EM, and X-ray crystallography in a hybrid approach, we identified binders to the three components of the baseplate, analyzed their affinity for their targets, and determined their epitopes as well as their functional impact on TP901-1 phage infectivity. We determined the X-ray structures of three nanobodies in complex with the RBP. Two of them bind to the saccharide binding site of the RBP and are able to fully neutralize TP901-1 phage infectivity, even after 15 passages,. These results provide clear evidence for a practical use of nanobodies in circumventing lactococcal phages viral infection in dairy fermentation. - 10.1073/pnas.1301336110 DA - 2013/04 ER -
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@article{V243940012, = {Desmyter, A and Farenc, C and Mahony, J and Spinelli, S and Bebeacua, C and Blangy, S and Veesler, D and van Sinderen, D and Cambillau, C }, = {2013}, = {April}, = {Proceedings of The National Academy of Sciences of The United States of America}, = {Viral infection modulation and neutralization by camelid nanobodies}, = {Validated}, = {Altmetric: 1 ()}, = {LACTOCOCCUS-LACTIS PHAGES RECEPTOR-BINDING PROTEIN ELECTRON-MICROSCOPY MAXIMUM-LIKELIHOOD ANTIBODY FRAGMENT CRYSTAL-STRUCTURE ESCHERICHIA-COLI TAIL BASEPLATE MECHANISM}, = {110}, pages = {1371--1379}, = {{Lactococcal phages belong to a large family of Siphoviridae and infect Lactococcus lactis, a Gram-positive bacterium used in commercial dairy fermentations. These phages are believed to recognize and bind specifically to pellicle polysaccharides covering the entire bacterium. The phage TP901-1 baseplate, located at the tip of the tail, harbors 18 trimeric receptor binding proteins (RBPs) promoting adhesion to a specific lactococcal strain. Phage TP901-1 adhesion does not require major conformational changes or Ca2+, which contrasts other lactococcal phages. Here, we produced and characterized llama nanobodies raised against the purified baseplate and the Tal protein of phage TP901-1 as tools to dissect the molecular determinants of phage TP901-1 infection. Using a set of complementary techniques, surface plasmon resonance, EM, and X-ray crystallography in a hybrid approach, we identified binders to the three components of the baseplate, analyzed their affinity for their targets, and determined their epitopes as well as their functional impact on TP901-1 phage infectivity. We determined the X-ray structures of three nanobodies in complex with the RBP. Two of them bind to the saccharide binding site of the RBP and are able to fully neutralize TP901-1 phage infectivity, even after 15 passages,. These results provide clear evidence for a practical use of nanobodies in circumventing lactococcal phages viral infection in dairy fermentation.}}, = {10.1073/pnas.1301336110}, source = {IRIS} }
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AUTHORS | Desmyter, A,Farenc, C,Mahony, J,Spinelli, S,Bebeacua, C,Blangy, S,Veesler, D,van Sinderen, D,Cambillau, C | ||
YEAR | 2013 | ||
MONTH | April | ||
JOURNAL_CODE | Proceedings of The National Academy of Sciences of The United States of America | ||
TITLE | Viral infection modulation and neutralization by camelid nanobodies | ||
STATUS | Validated | ||
TIMES_CITED | Altmetric: 1 () | ||
SEARCH_KEYWORD | LACTOCOCCUS-LACTIS PHAGES RECEPTOR-BINDING PROTEIN ELECTRON-MICROSCOPY MAXIMUM-LIKELIHOOD ANTIBODY FRAGMENT CRYSTAL-STRUCTURE ESCHERICHIA-COLI TAIL BASEPLATE MECHANISM | ||
VOLUME | 110 | ||
ISSUE | |||
START_PAGE | 1371 | ||
END_PAGE | 1379 | ||
ABSTRACT | Lactococcal phages belong to a large family of Siphoviridae and infect Lactococcus lactis, a Gram-positive bacterium used in commercial dairy fermentations. These phages are believed to recognize and bind specifically to pellicle polysaccharides covering the entire bacterium. The phage TP901-1 baseplate, located at the tip of the tail, harbors 18 trimeric receptor binding proteins (RBPs) promoting adhesion to a specific lactococcal strain. Phage TP901-1 adhesion does not require major conformational changes or Ca2+, which contrasts other lactococcal phages. Here, we produced and characterized llama nanobodies raised against the purified baseplate and the Tal protein of phage TP901-1 as tools to dissect the molecular determinants of phage TP901-1 infection. Using a set of complementary techniques, surface plasmon resonance, EM, and X-ray crystallography in a hybrid approach, we identified binders to the three components of the baseplate, analyzed their affinity for their targets, and determined their epitopes as well as their functional impact on TP901-1 phage infectivity. We determined the X-ray structures of three nanobodies in complex with the RBP. Two of them bind to the saccharide binding site of the RBP and are able to fully neutralize TP901-1 phage infectivity, even after 15 passages,. These results provide clear evidence for a practical use of nanobodies in circumventing lactococcal phages viral infection in dairy fermentation. | ||
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DOI_LINK | 10.1073/pnas.1301336110 | ||
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