Cryo-EM structures of HIV-1 trimer bound to CD4-mimetics BNM-III-170 and M48U1 adopt a CD4-bound open conformation

Nat Commun. 2021 Mar 29;12(1):1950. doi: 10.1038/s41467-021-21816-x.

Abstract

Human immunodeficiency virus-1 (HIV-1), the causative agent of AIDS, impacts millions of people. Entry into target cells is mediated by the HIV-1 envelope (Env) glycoprotein interacting with host receptor CD4, which triggers conformational changes allowing binding to a coreceptor and subsequent membrane fusion. Small molecule or peptide CD4-mimetic drugs mimic CD4's Phe43 interaction with Env by inserting into the conserved Phe43 pocket on Env subunit gp120. Here, we present single-particle cryo-EM structures of CD4-mimetics BNM-III-170 and M48U1 bound to a BG505 native-like Env trimer plus the CD4-induced antibody 17b at 3.7 Å and 3.9 Å resolution, respectively. CD4-mimetic-bound BG505 exhibits canonical CD4-induced conformational changes including trimer opening, formation of the 4-stranded gp120 bridging sheet, displacement of the V1V2 loop, and formation of a compact and elongated gp41 HR1C helical bundle. We conclude that CD4-induced structural changes on both gp120 and gp41 Env subunits are induced by binding to the gp120 Phe43 pocket.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Binding Sites
  • Biomimetic Materials / chemistry
  • Biomimetic Materials / metabolism
  • CD4 Antigens / antagonists & inhibitors
  • CD4 Antigens / chemistry*
  • CD4 Antigens / genetics
  • CD4 Antigens / metabolism
  • CHO Cells
  • Cloning, Molecular
  • Cricetulus
  • Cryoelectron Microscopy
  • Gene Expression
  • Genetic Vectors / chemistry
  • Genetic Vectors / metabolism
  • Guanidines / chemistry*
  • Guanidines / metabolism
  • HEK293 Cells
  • HIV Envelope Protein gp120 / chemistry*
  • HIV Envelope Protein gp120 / genetics
  • HIV Envelope Protein gp120 / metabolism
  • HIV Envelope Protein gp41 / chemistry*
  • HIV Envelope Protein gp41 / genetics
  • HIV Envelope Protein gp41 / metabolism
  • HIV-1 / chemistry*
  • HIV-1 / metabolism
  • Humans
  • Indenes / chemistry*
  • Indenes / metabolism
  • Models, Molecular
  • Protein Binding
  • Protein Conformation, alpha-Helical
  • Protein Conformation, beta-Strand
  • Protein Interaction Domains and Motifs
  • Protein Multimerization
  • Receptors, Virus / antagonists & inhibitors
  • Receptors, Virus / chemistry*
  • Receptors, Virus / genetics
  • Receptors, Virus / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Small Molecule Libraries / chemistry
  • Small Molecule Libraries / metabolism

Substances

  • BNM-III-170
  • CD4 Antigens
  • Guanidines
  • HIV Envelope Protein gp120
  • HIV Envelope Protein gp41
  • Indenes
  • Receptors, Virus
  • Recombinant Proteins
  • Small Molecule Libraries