Differential binding of the HIV-1 envelope to phosphatidylserine receptors

Biochim Biophys Acta Biomembr. 2017 Oct;1859(10):1962-1966. doi: 10.1016/j.bbamem.2017.06.007. Epub 2017 Jun 13.

Abstract

Prior work has shown that the HIV-1 envelope of the human immunodeficiency virus (HIV) interacts directly with T-cell immunoglobulin mucin (TIM) family proteins. Herein, we demonstrate that HIV-1 envelope glycoproteins from varying HIV-1 clades bind differentially to TIM proteins and functionally similar proteins acting as phosphatidylserine (PtdSer) receptors. Using enzyme-linked immunosorbent assay (ELISA) and surface plasmon resonance (SPR) technology, we show that lysate containing HIV-1 envelope and recombinant HIV-1 envelope glycoproteins bind TIM-4 and advanced glycosylation end product-specific receptor (AGER). The complex binding of HIV-1 UG21 gp140 to TIM-4 or AGER suggests a biphasic interaction with these proteins.

Keywords: Advanced glycosylation end product-specific receptor; Glycoproteins; Human immunodeficiency virus; Phosphatidylserine; Surface plasmon resonance; T-cell immunoglobulin mucin.

Publication types

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

MeSH terms

  • Cell Line
  • Enzyme-Linked Immunosorbent Assay / methods
  • HEK293 Cells
  • HIV Infections / metabolism
  • HIV-1 / metabolism*
  • Human Immunodeficiency Virus Proteins / metabolism*
  • Humans
  • Membrane Glycoproteins / metabolism
  • Receptor for Advanced Glycation End Products / metabolism
  • Receptors, Cell Surface / metabolism*
  • Receptors, Virus / metabolism
  • Recombinant Proteins / metabolism
  • Viral Envelope Proteins / metabolism*

Substances

  • Human Immunodeficiency Virus Proteins
  • Membrane Glycoproteins
  • Receptor for Advanced Glycation End Products
  • Receptors, Cell Surface
  • Receptors, Virus
  • Recombinant Proteins
  • Viral Envelope Proteins
  • phosphatidylserine receptor