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Human immunodeficiency virus 1 (HIV-1) conserved epitope regions are highly stable segments of the viral proteome that are essential for structural integrity or the replication cycle (Korenc et al., 2021). Because mutations in these regions often result in a significant loss of viral fitness, they remain relatively invariant across different global strains and subtypes (Mothe et al., 2015). These regions serve as primary targets for the development of "universal" HIV vaccines and broadly neutralizing antibodies (bNAbs), which aim to circumvent the virus's ability to evade the immune system through rapid mutation (Hanke, 2019). Therapeutic strategies focusing on these epitopes, such as the HTI vaccine or bNAbs like VRC01, seek to elicit robust CD8+ T-cell responses or broad antibody-mediated neutralization to control viral replication and reduce the latent reservoir (Walker et al., 2010; Mothe et al., 2015). By targeting the virus's functionally constrained "Achilles' heel," these interventions offer a promising path toward long-term remission or a functional cure for HIV-1 infection (Korenc et al., 2021).
Induction of cytotoxic T-lymphocyte (CTL) responses and production of broadly neutralizing antibodies (bNAbs) that target functionally constrained viral regions, thereby preventing viral escape and inhibiting viral entry across diverse HIV-1 strains (Hanke, 2019; Walker et al., 2010).
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