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- W2308602445 abstract "Efforts to elicit broadly neutralizing antibodies (bNAbs) against HIV-1 require understanding germline bNAb recognition of HIV-1 envelope glycoprotein (Env). The VRC01-class bNAb family derived from the VH1-2*02 germline allele arose in multiple HIV-1–infected donors, yet targets the CD4-binding site on Env with common interactions. Modified forms of the 426c Env that activate germline-reverted B cell receptors are candidate immunogens for eliciting VRC01-class bNAbs. We present structures of germline-reverted VRC01-class bNAbs alone and complexed with 426c-based gp120 immunogens. Germline bNAb–426c gp120 complexes showed preservation of VRC01-class signature residues and gp120 contacts, but detectably different binding modes compared to mature bNAb-gp120 complexes. Unlike typical antibody-antigen interactions, VRC01–class germline antibodies exhibited preformed antigen-binding conformations for recognizing immunogens. Affinity maturation introduced substitutions increasing induced-fit recognition and electropositivity, potentially to accommodate negatively-charged complex-type N-glycans on gp120. These results provide general principles relevant to the unusual evolution of VRC01–class bNAbs and guidelines for structure-based immunogen design." @default.
- W2308602445 created "2016-06-24" @default.
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- W2308602445 date "2016-03-21" @default.
- W2308602445 modified "2023-10-16" @default.
- W2308602445 title "Structural basis for germline antibody recognition of HIV-1 immunogens" @default.
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- W2308602445 doi "https://doi.org/10.7554/elife.13783" @default.
- W2308602445 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4811768" @default.
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