Identification of the DC-SIGN-interactive domains on the envelope glycoprotein of HIV-1 CRF07-BC

Che Feng Liao, Sheng Fan Wang, Yu Ting Lin, David D. Ho, Yi Ming Arthur Chen

Research output: Contribution to journalArticle

4 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)831-839
Number of pages9
JournalAIDS Research and Human Retroviruses
Volume27
Issue number8
DOIs
Publication statusPublished - Aug 1 2011
Externally publishedYes

ASJC Scopus subject areas

  • Immunology
  • Virology
  • Infectious Diseases

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