Extended antibody-framework-to-antigen distance observed exclusively with broad HIV-1-neutralizing antibodies recognizing glycan-dense surfaces

Here, the authors analyse the distance between the body of an antibody and a protein antigen denoted as the Antibody-Framework-to-Antigen Distance (AFAD) for about 2000 non-redundant antibody-protein antigen complexes in the Protein Data Bank. They observe that antibodies with exceptionally long AFA...

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Autores principales: Myungjin Lee, Anita Changela, Jason Gorman, Reda Rawi, Tatsiana Bylund, Cara W. Chao, Bob C. Lin, Mark K. Louder, Adam S. Olia, Baoshan Zhang, Nicole A. Doria-Rose, Susan Zolla-Pazner, Lawrence Shapiro, Gwo-Yu Chuang, Peter D. Kwong
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/c6314cb8177848269383e9f05a200718
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spelling oai:doaj.org-article:c6314cb8177848269383e9f05a2007182021-11-14T12:36:39ZExtended antibody-framework-to-antigen distance observed exclusively with broad HIV-1-neutralizing antibodies recognizing glycan-dense surfaces10.1038/s41467-021-26579-z2041-1723https://doaj.org/article/c6314cb8177848269383e9f05a2007182021-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-26579-zhttps://doaj.org/toc/2041-1723Here, the authors analyse the distance between the body of an antibody and a protein antigen denoted as the Antibody-Framework-to-Antigen Distance (AFAD) for about 2000 non-redundant antibody-protein antigen complexes in the Protein Data Bank. They observe that antibodies with exceptionally long AFADs were all broad HIV-1-neutralizing antibodies that targeted densely glycosylated regions on the HIV-1-envelope trimer. The connection between long AFAD and dense glycan was further validated by the cryo-EM structure of antibody 2909 recognizing a glycan hole and by glycan shielding analyses based on molecular dynamics simulations.Myungjin LeeAnita ChangelaJason GormanReda RawiTatsiana BylundCara W. ChaoBob C. LinMark K. LouderAdam S. OliaBaoshan ZhangNicole A. Doria-RoseSusan Zolla-PaznerLawrence ShapiroGwo-Yu ChuangPeter D. KwongNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Myungjin Lee
Anita Changela
Jason Gorman
Reda Rawi
Tatsiana Bylund
Cara W. Chao
Bob C. Lin
Mark K. Louder
Adam S. Olia
Baoshan Zhang
Nicole A. Doria-Rose
Susan Zolla-Pazner
Lawrence Shapiro
Gwo-Yu Chuang
Peter D. Kwong
Extended antibody-framework-to-antigen distance observed exclusively with broad HIV-1-neutralizing antibodies recognizing glycan-dense surfaces
description Here, the authors analyse the distance between the body of an antibody and a protein antigen denoted as the Antibody-Framework-to-Antigen Distance (AFAD) for about 2000 non-redundant antibody-protein antigen complexes in the Protein Data Bank. They observe that antibodies with exceptionally long AFADs were all broad HIV-1-neutralizing antibodies that targeted densely glycosylated regions on the HIV-1-envelope trimer. The connection between long AFAD and dense glycan was further validated by the cryo-EM structure of antibody 2909 recognizing a glycan hole and by glycan shielding analyses based on molecular dynamics simulations.
format article
author Myungjin Lee
Anita Changela
Jason Gorman
Reda Rawi
Tatsiana Bylund
Cara W. Chao
Bob C. Lin
Mark K. Louder
Adam S. Olia
Baoshan Zhang
Nicole A. Doria-Rose
Susan Zolla-Pazner
Lawrence Shapiro
Gwo-Yu Chuang
Peter D. Kwong
author_facet Myungjin Lee
Anita Changela
Jason Gorman
Reda Rawi
Tatsiana Bylund
Cara W. Chao
Bob C. Lin
Mark K. Louder
Adam S. Olia
Baoshan Zhang
Nicole A. Doria-Rose
Susan Zolla-Pazner
Lawrence Shapiro
Gwo-Yu Chuang
Peter D. Kwong
author_sort Myungjin Lee
title Extended antibody-framework-to-antigen distance observed exclusively with broad HIV-1-neutralizing antibodies recognizing glycan-dense surfaces
title_short Extended antibody-framework-to-antigen distance observed exclusively with broad HIV-1-neutralizing antibodies recognizing glycan-dense surfaces
title_full Extended antibody-framework-to-antigen distance observed exclusively with broad HIV-1-neutralizing antibodies recognizing glycan-dense surfaces
title_fullStr Extended antibody-framework-to-antigen distance observed exclusively with broad HIV-1-neutralizing antibodies recognizing glycan-dense surfaces
title_full_unstemmed Extended antibody-framework-to-antigen distance observed exclusively with broad HIV-1-neutralizing antibodies recognizing glycan-dense surfaces
title_sort extended antibody-framework-to-antigen distance observed exclusively with broad hiv-1-neutralizing antibodies recognizing glycan-dense surfaces
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/c6314cb8177848269383e9f05a200718
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