Identification of the DC-SIGN-interactive domains on the envelope glycoprotein of HIV-1 CRF07_BC

AIDS Res Hum Retroviruses. 2011 Aug;27(8):831-9. doi: 10.1089/AID.2010.0215. Epub 2011 Jan 17.

Abstract

DC-SIGN, a C-type lection expressed on dendritic cells, enhances HIV-1 infection in cis and in trans. HIV-1 circulating recombinant form (CRF) 07_BC viruses have been the predominant strain found among injection drug users in southern China and Taiwan. The goal of this study was to map the DC-SIGN-interactive domain on the gp120 of CRF07_BC. Pseudotyped viruses containing single (N233Q, N275Q, N330Q, N351Q, N355Q, N381Q, and N387Q), double (N233Q + N275Q, N233Q + N351Q, N275Q + N351Q), or triple (N233Q + N275Q + N351Q) N-glycan mutant gp120 were generated. Capture assays showed that the DC-SIGN-binding capacity of pseudoviruses with N275Q or N351Q decreased significantly. Rabbit antisera against synthetic peptides covering the N275 (R72 antiserum) or N351 (R77 antiserum) region blocked the interaction between wild-type gp120 and DC-SIGN in the capture assay. Furthermore, pseudotype viruses containing gp120 from five different CRF07_BC isolates were generated and R72 and R77 antisera blocked their interactions with DC-SIGN (80% for R72 and 40% for R77, respectively) in the capture assays. In conclusion, the N275 and N351 glycan sites on the CRF07_BC gp120 play an important role in mediating the interaction between gp120 and DC-SIGN. This information is valuable for developing both therapeutic and preventive agents for HIV-1 infection.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Blocking / immunology
  • Antibodies, Blocking / pharmacology
  • Binding Sites / genetics
  • Binding Sites / immunology
  • Cell Adhesion Molecules / immunology
  • Cell Adhesion Molecules / metabolism*
  • Cell Line
  • China
  • Dendritic Cells / immunology
  • Dendritic Cells / metabolism*
  • HIV Envelope Protein gp120 / chemistry
  • HIV Envelope Protein gp120 / genetics
  • HIV Envelope Protein gp120 / immunology
  • HIV Envelope Protein gp120 / metabolism*
  • HIV Infections* / epidemiology
  • HIV Infections* / immunology
  • HIV Infections* / metabolism
  • HIV Infections* / virology
  • HIV-1 / genetics
  • HIV-1 / immunology
  • HIV-1 / isolation & purification
  • HIV-1 / metabolism*
  • Humans
  • Immune Sera
  • Immunoassay
  • Lectins, C-Type / immunology
  • Lectins, C-Type / metabolism*
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Mutation
  • Plasmids
  • Polysaccharides / chemistry
  • Polysaccharides / genetics
  • Polysaccharides / immunology
  • Polysaccharides / metabolism*
  • Protein Binding / drug effects
  • Protein Binding / genetics
  • Protein Binding / immunology
  • Rabbits
  • Receptors, Cell Surface / immunology
  • Receptors, Cell Surface / metabolism*
  • Sequence Analysis, DNA
  • Taiwan
  • Transfection
  • Virus Internalization / drug effects

Substances

  • Antibodies, Blocking
  • Cell Adhesion Molecules
  • DC-specific ICAM-3 grabbing nonintegrin
  • HIV Envelope Protein gp120
  • Immune Sera
  • Lectins, C-Type
  • Polysaccharides
  • Receptors, Cell Surface