dc.creatorSui, Jianhua
dc.creatorHwang, William C.
dc.creatorPerez, Sandra
dc.creatorWei, Ge
dc.creatorAird, Daniel
dc.creatorChen, Li-Mei
dc.creatorSantelli, Eugenio
dc.creatorStec, Boguslaw
dc.creatorCadwell, Greg
dc.creatorAli, Maryam
dc.creatorWan, Hongquan
dc.creatorMurakami, Akikazu
dc.creatorYammanuru, Anuradha
dc.creatorHan, Thomas
dc.creatorCox, Nancy J.
dc.creatorBankston, Laurie A.
dc.creatorDonis, Ruben O.
dc.creatorLiddington, Robert C.
dc.creatorMarasco, Wayne A.
dc.date2009-03
dc.identifierhttp://hdl.handle.net/11336/96252
dc.identifierSui, Jianhua; Hwang, William C.; Perez, Sandra; Wei, Ge; Aird, Daniel; et al.; Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses; Nature Publishing Group; Nature Structural and Molecular Biology; 16; 3; 3-2009; 265-273
dc.identifier1072-8368
dc.identifier1545-9985
dc.identifierCONICET Digital
dc.identifierCONICET
dc.descriptionInfluenza virus remains a serious health threat, owing to its ability to evade immune surveillance through rapid genetic drift and reassortment. Here we used a human non-immune antibody phage-display library and the H5 hemagglutinin ectodomain to select ten neutralizing antibodies (nAbs) that were effective against all group 1 influenza viruses tested, including H5N1 'bird flu' and the H1N1 'Spanish flu'. The crystal structure of one such nAb bound to H5 shows that it blocks infection by inserting its heavy chain into a conserved pocket in the stem region, thus preventing membrane fusion. Nine of the nAbs employ the germline gene VH1-69, and all seem to use the same neutralizing mechanism. Our data further suggest that this region is recalcitrant to neutralization escape and that nAb-based immunotherapy is a promising strategy for broad-spectrum protection against seasonal and pandemic influenza viruses.
dc.descriptionFil: Sui, Jianhua. Harvard Medical School; Estados Unidos. Dana-farber Cancer Institute; Estados Unidos
dc.descriptionFil: Hwang, William C.. Sanford Burnham Prebys Medical Discovery Institute; Estados Unidos
dc.descriptionFil: Perez, Sandra. National Center For Immunization And Respiratory Diseases; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.descriptionFil: Wei, Ge. Sanford Burnham Prebys Medical Discovery Institute; Estados Unidos
dc.descriptionFil: Aird, Daniel. Harvard Medical School; Estados Unidos. Dana-farber Cancer Institute; Estados Unidos
dc.descriptionFil: Chen, Li-Mei. National Center For Immunization And Respiratory Diseases; Estados Unidos
dc.descriptionFil: Santelli, Eugenio. Sanford Burnham Prebys Medical Discovery Institute; Estados Unidos
dc.descriptionFil: Stec, Boguslaw. Sanford Burnham Prebys Medical Discovery Institute; Estados Unidos
dc.descriptionFil: Cadwell, Greg. Sanford Burnham Prebys Medical Discovery Institute; Estados Unidos
dc.descriptionFil: Ali, Maryam. Dana-farber Cancer Institute; Estados Unidos. Harvard Medical School; Estados Unidos
dc.descriptionFil: Wan, Hongquan. National Center For Immunization And Respiratory Diseases; Estados Unidos
dc.descriptionFil: Murakami, Akikazu. Harvard Medical School; Estados Unidos. Dana-farber Cancer Institute; Estados Unidos
dc.descriptionFil: Yammanuru, Anuradha. Dana-farber Cancer Institute; Estados Unidos. Harvard Medical School; Estados Unidos
dc.descriptionFil: Han, Thomas. Harvard Medical School; Estados Unidos. Dana-farber Cancer Institute; Estados Unidos
dc.descriptionFil: Cox, Nancy J.. National Center For Immunization And Respiratory Diseases; Estados Unidos
dc.descriptionFil: Bankston, Laurie A.. Sanford Burnham Prebys Medical Discovery Institute; Estados Unidos
dc.descriptionFil: Donis, Ruben O.. National Center For Immunization And Respiratory Diseases; Estados Unidos
dc.descriptionFil: Liddington, Robert C.. Sanford Burnham Prebys Medical Discovery Institute; Estados Unidos
dc.descriptionFil: Marasco, Wayne A.. Dana-farber Cancer Institute; Estados Unidos. Harvard Medical School; Estados Unidos
dc.formatapplication/pdf
dc.formatapplication/pdf
dc.languageeng
dc.publisherNature Publishing Group
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/10.1038/nsmb.1566
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/nsmb.1566
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2692245/
dc.rightsinfo:eu-repo/semantics/openAccess
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subjectINFLUENZA
dc.subjectMONOCLONAL ANTIBODIES
dc.subjectIMMUNOTHERAPY
dc.subjectH5N1
dc.subjecthttps://purl.org/becyt/ford/3.4
dc.subjecthttps://purl.org/becyt/ford/3
dc.titleStructural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:ar-repo/semantics/artículo
dc.typeinfo:eu-repo/semantics/publishedVersion


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