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

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...

Full description

Bibliographic Details
Main Authors: 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
Format: Article
Language:English
Published: Nature Portfolio 2021-11-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-26579-z
Description
Summary: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.
ISSN:2041-1723

Similar Items