DC-SIGN-mediated internalization of HIV is required for trans-enhancement of T cell infection. Academic Article uri icon

Overview

abstract

  • Fusion of the human immunodeficiency virus (HIV) to the plasma membrane of target cells is mediated by interaction of its envelope glycoprotein, gp120, with CD4 and appropriate chemokine receptors. gp120 additionally binds to DC-SIGN, a C-type lectin expressed on immature dendritic cells. This interaction does not result in viral fusion, but instead contributes to enhanced infection in trans of target cells that express CD4 and chemokine receptors. Here we show that DC-SIGN mediates rapid internalization of intact HIV into a low pH nonlysosomal compartment. Internalized virus retains competence to infect target cells. Removal of the DC-SIGN cytoplasmic tail reduced viral uptake and abrogated the trans-enhancement of T cell infection. We propose that HIV binds to DC-SIGN to gain access to an intracellular compartment that contributes to augmentation or retention of viral infectivity.

publication date

  • January 1, 2002

Research

keywords

  • Cell Adhesion Molecules
  • HIV
  • Lectins
  • Lectins, C-Type
  • Receptors, Cell Surface
  • T-Lymphocytes

Identity

Scopus Document Identifier

  • 0036172314

Digital Object Identifier (DOI)

  • 10.1016/s1074-7613(02)00259-5

PubMed ID

  • 11825572

Additional Document Info

volume

  • 16

issue

  • 1