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Broadly cross-reactive human antibodies that inhibit genogroup I and II noroviruses

The rational development of norovirus vaccine candidates requires a deep understanding of the antigenic diversity and mechanisms of neutralization of the virus. Here, we isolate and characterize a panel of broadly cross-reactive naturally occurring human monoclonal IgMs, IgAs and IgGs reactive with...

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Autores principales: Alvarado, Gabriela, Salmen, Wilhelm, Ettayebi, Khalil, Hu, Liya, Sankaran, Banumathi, Estes, Mary K., Venkataram Prasad, B. V., Crowe, James E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8280134/
https://www.ncbi.nlm.nih.gov/pubmed/34262046
http://dx.doi.org/10.1038/s41467-021-24649-w
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author Alvarado, Gabriela
Salmen, Wilhelm
Ettayebi, Khalil
Hu, Liya
Sankaran, Banumathi
Estes, Mary K.
Venkataram Prasad, B. V.
Crowe, James E.
author_facet Alvarado, Gabriela
Salmen, Wilhelm
Ettayebi, Khalil
Hu, Liya
Sankaran, Banumathi
Estes, Mary K.
Venkataram Prasad, B. V.
Crowe, James E.
author_sort Alvarado, Gabriela
collection PubMed
description The rational development of norovirus vaccine candidates requires a deep understanding of the antigenic diversity and mechanisms of neutralization of the virus. Here, we isolate and characterize a panel of broadly cross-reactive naturally occurring human monoclonal IgMs, IgAs and IgGs reactive with human norovirus (HuNoV) genogroup I or II (GI or GII). We note three binding patterns and identify monoclonal antibodies (mAbs) that neutralize at least one GI or GII HuNoV strain when using a histo-blood group antigen (HBGA) blocking assay. The HBGA blocking assay and a virus neutralization assay using human intestinal enteroids reveal that the GII-specific mAb NORO-320, mediates HBGA blocking and neutralization of multiple GII genotypes. The Fab form of NORO-320 neutralizes GII.4 infection more potently than the mAb, however, does not block HBGA binding. The crystal structure of NORO-320 Fab in complex with GII.4 P-domain shows that the antibody recognizes a highly conserved region in the P-domain distant from the HBGA binding site. Dynamic light scattering analysis of GII.4 virus-like particles with mAb NORO-320 shows severe aggregation, suggesting neutralization is by steric hindrance caused by multivalent cross-linking. Aggregation was not observed with the Fab form of NORO-320, suggesting that this clone also has additional inhibitory features.
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spelling pubmed-82801342021-07-20 Broadly cross-reactive human antibodies that inhibit genogroup I and II noroviruses Alvarado, Gabriela Salmen, Wilhelm Ettayebi, Khalil Hu, Liya Sankaran, Banumathi Estes, Mary K. Venkataram Prasad, B. V. Crowe, James E. Nat Commun Article The rational development of norovirus vaccine candidates requires a deep understanding of the antigenic diversity and mechanisms of neutralization of the virus. Here, we isolate and characterize a panel of broadly cross-reactive naturally occurring human monoclonal IgMs, IgAs and IgGs reactive with human norovirus (HuNoV) genogroup I or II (GI or GII). We note three binding patterns and identify monoclonal antibodies (mAbs) that neutralize at least one GI or GII HuNoV strain when using a histo-blood group antigen (HBGA) blocking assay. The HBGA blocking assay and a virus neutralization assay using human intestinal enteroids reveal that the GII-specific mAb NORO-320, mediates HBGA blocking and neutralization of multiple GII genotypes. The Fab form of NORO-320 neutralizes GII.4 infection more potently than the mAb, however, does not block HBGA binding. The crystal structure of NORO-320 Fab in complex with GII.4 P-domain shows that the antibody recognizes a highly conserved region in the P-domain distant from the HBGA binding site. Dynamic light scattering analysis of GII.4 virus-like particles with mAb NORO-320 shows severe aggregation, suggesting neutralization is by steric hindrance caused by multivalent cross-linking. Aggregation was not observed with the Fab form of NORO-320, suggesting that this clone also has additional inhibitory features. Nature Publishing Group UK 2021-07-14 /pmc/articles/PMC8280134/ /pubmed/34262046 http://dx.doi.org/10.1038/s41467-021-24649-w Text en © The Author(s) 2021, corrected publication 2021 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Alvarado, Gabriela
Salmen, Wilhelm
Ettayebi, Khalil
Hu, Liya
Sankaran, Banumathi
Estes, Mary K.
Venkataram Prasad, B. V.
Crowe, James E.
Broadly cross-reactive human antibodies that inhibit genogroup I and II noroviruses
title Broadly cross-reactive human antibodies that inhibit genogroup I and II noroviruses
title_full Broadly cross-reactive human antibodies that inhibit genogroup I and II noroviruses
title_fullStr Broadly cross-reactive human antibodies that inhibit genogroup I and II noroviruses
title_full_unstemmed Broadly cross-reactive human antibodies that inhibit genogroup I and II noroviruses
title_short Broadly cross-reactive human antibodies that inhibit genogroup I and II noroviruses
title_sort broadly cross-reactive human antibodies that inhibit genogroup i and ii noroviruses
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8280134/
https://www.ncbi.nlm.nih.gov/pubmed/34262046
http://dx.doi.org/10.1038/s41467-021-24649-w
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