Stronger binding affinities of gp120/CD4 in Catarrhini provide insights into HIV/host interactions.

ABSTRACT: Human immunodeficiency virus-1 (HIV-1) exploits the viral gp120 protein and host CD4/CCR5 receptors for the pandemic infection to humans. The host co-receptors of not only humans but also several primates and HIV-model mice can interact with the HIV receptor. However, the molecular mechanisms of these interactions remain unclear. Using Shaik et al. (2019)'s gp120/CD4/CCR5 structure of HIV-1B and human, here, we investigate the molecular dynamics between HIV sub-lineages (B, C, N, and O) and potential hosts in Euarchontoglires (primates and rodents). Although both host genes show similar protein structures conserved in all animals, CD4 gene demonstrates significantly stronger binding affinities in Catarrhini (apes and Old-World monkeys). Its

SUBMITTER: Li V 

PROVIDER: S-EPMC11607582 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature