Structural basis of glycan276-dependent recognition by HIV-1 broadly neutralizing antibodies

Cottrell, Christopher A.; Manne, Kartik; Kong, Rui; Wang, Shuishu; Zhou, Tongqing; Chuang, Gwo-Yu; Edwards, Robert J.; Henderson, Rory; Janowska, Katarzyna; Kopp, Megan; Lin, Bob C.; Louder, Mark K.; Olia, Adam S.; Rawi, Reda; Shen, Chen‐Hsiang; Taft, Justin; Torres, Jonathan L.; Wu, Nelson R.; Zhang, Baoshan; Doria‐Rose, Nicole A.; Cohen, Myron S.; Haynes, Barton F.; Shapiro, Lawrence; Ward, Andrew B.; Acharya, Priyamvada; Mascola, John R.; Kwong, Peter D.

doi:10.1016/j.celrep.2021.109922

Cited by 6 publications

(1 citation statement)

References 87 publications

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“…These evasion mechanisms must allow access to the CD4-binding site (CD4bs) by the membrane-distal domain of CD4, which is the size of a single immunoglobulin domain (Ryu et al, 1990;Wang et al, 1990). Some antibodies, such VRC01-class antibodies, mimic CD4 binding with their heavy chains, allowing for their neutralization of most circulating HIV-1 isolates (Huang et al, 2016;Wu et al, 2010;; other antibodies, such as the glycan276-dependent antibody VRC40 (Cottrell et al, 2021), evolve favorable binding interactions with glycans surrounding the CD4bs. These antibodies, however, require unusual complementarity determining regions (CDRs) or extensive somatic hypermutation (SHM), and generally developed only after a long period of chronic infection, making them difficult to elicit by vaccination.…”

Section: Introductionmentioning

confidence: 99%

Structural basis for llama nanobody recognition and neutralization of HIV-1 at the CD4-binding site

Zhou,

Chen,

Gorman

et al. 2022

Structure

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Section: Introductionmentioning

confidence: 99%

Structural basis for llama nanobody recognition and neutralization of HIV-1 at the CD4-binding site

Zhou,

Chen,

Gorman

et al. 2022

Structure

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HIV-1 neutralizing antibodies elicited in humans by a prefusion-stabilized envelope trimer form a reproducible class targeting fusion peptide

et al. 2023

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B cell repertoire sequencing of HIV-1 pediatric elite-neutralizers identifies multiple broadly neutralizing antibody clonotypes

Kumar

Bajpai²,

Joyce

et al. 2023

Preprint

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A limited subset of HIV–1 infected adult individuals typically after at least 2–3 years of chronic infection, develop broadly neutralizing antibodies (bnAbs), suggesting that highly conserved neutralizing epitopes on the HIV-1 envelope glycoprotein are difficult for B cell receptors to effectively target, during natural infection. Recent studies have shown the evolution of bnAbs in HIV–1 infected infants. We used bulk BCR sequencing (BCR–seq) to profile the B cell receptors from longitudinal samples (3 time points) collected from a rare pair of antiretroviral–naive, HIV–1 infected pediatric monozygotic twins (AIIMS–329 and AIIMS–330) who displayed elite plasma neutralizing activity against HIV–1. BCR–seq of both twins revealed convergent antibody characteristics including V–gene use, CDRH3 lengths and somatic hypermutation (SHM). Further, antibody clonotypes with genetic features similar to highly potent bnAbs isolated from adults showed ongoing development in donor AIIMS–330 but not in AIIMS–329, corroborating our earlier findings based on plasma bnAbs responses. An increase in SHM was observed in sequences of the IgA isotype from AIIMS–330. This study is an important step toward defining specific features of the antibody repertoire and shared clonotype maturation that are associated with the development of HIV-1 elite–neutralizing activity. Some of the shared lineages identified in this pair of identical twins, who had acquired HIV-1 infection by vertical transmission, may have been elicited by exposure to common HIV–1 antigens. Defining the sequences of such shared clonotypes in a large number of children can shed light on the role of specific B cell receptor features in the response to HIV–1 infection.

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Structural basis of glycan276-dependent recognition by HIV-1 broadly neutralizing antibodies

Cited by 6 publications

References 87 publications

Structural basis for llama nanobody recognition and neutralization of HIV-1 at the CD4-binding site

Structural basis for llama nanobody recognition and neutralization of HIV-1 at the CD4-binding site

HIV-1 neutralizing antibodies elicited in humans by a prefusion-stabilized envelope trimer form a reproducible class targeting fusion peptide

B cell repertoire sequencing of HIV-1 pediatric elite-neutralizers identifies multiple broadly neutralizing antibody clonotypes

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