Recapitulation of HIV-1 Env-antibody coevolution in macaques leading to neutralization breadth.
basic_science · Level V
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- Record sourced from PubMed, PMID 33214287.
- Also identified by DOI 10.1126/science.abd2638 and PMC identifier 8040783.
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Abstract
Neutralizing antibodies elicited by HIV-1 coevolve with viral envelope proteins (Env) in distinctive patterns, in some cases acquiring substantial breadth. We report that primary HIV-1 envelope proteins-when expressed by simian-human immunodeficiency viruses in rhesus macaques-elicited patterns of Env-antibody coevolution very similar to those in humans, including conserved immunogenetic, structural, and chemical solutions to epitope recognition and precise Env-amino acid substitutions, insertions, and deletions leading to virus persistence. The structure of one rhesus antibody, capable of neutralizing 49% of a 208-strain panel, revealed a V2 apex mode of recognition like that of human broadly neutralizing antibodies (bNAbs) PGT145 and PCT64-35S. Another rhesus antibody bound the CD4 binding site by CD4 mimicry, mirroring human bNAbs 8ANC131, CH235, and VRC01. Virus-antibody coevolution in macaques can thus recapitulate developmental features of human bNAbs, thereby guiding HIV-1 immunogen design.
Medical subject headings
- Biological Coevolution
- Broadly Neutralizing Antibodies
- HIV Antibodies
- HIV Envelope Protein gp120
- HIV Infections
- HIV-1
- Simian Immunodeficiency Virus