AI Article Synopsis
- Many bnAbs that recognize Env glycans are present in HIV-infected individuals, yet it's challenging to stimulate their production due to the poor immunogenic nature of these glycans.
- Research shows that certain bnAbs can cross-react with N-glycans from a parasitic worm, Schistosoma mansoni, suggesting that harnessing this cross-reactivity may help develop vaccines that effectively target glycan-dependent epitopes in HIV-1.
Article Abstract
The HIV-1 Envelope glycoprotein (Env) is the sole target for broadly neutralizing antibodies (bnAbs). Env is heavily glycosylated with host-derived N-glycans, and many bnAbs bind to, or are dependent upon, Env glycans for neutralization. Although glycan-binding bnAbs are frequently detected in HIV-infected individuals, attempts to elicit them have been unsuccessful because of the poor immunogenicity of Env N-glycans. Here, we report cross-reactivity of glycan-binding bnAbs with self- and non-self N-glycans and glycoprotein antigens from different life-stages of Schistosoma mansoni. Using the IAVI Protocol C HIV infection cohort, we examine the relationship between S. mansoni seropositivity and development of bnAbs targeting glycan-dependent epitopes. We show that the unmutated common ancestor of the N332/V3-specific bnAb lineage PCDN76, isolated from an HIV-infected donor with S. mansoni seropositivity, binds to S. mansoni cercariae while lacking reactivity to gp120. Overall, these results present a strategy for elicitation of glycan-reactive bnAbs which could be exploited in HIV-1 vaccine development.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10073069 | PMC |
| http://dx.doi.org/10.1016/j.celrep.2022.110611 | DOI Listing |
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