title: Identification of the DC-SIGN-interactive domains on the envelope glycoprotein of HIV-1 CRF07_BC.
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.
authors.affiliation: AIDS Prevention and Research Center, National Yang-Ming University, Taipei, Taiwan.
authors.forename: Che-Feng
authors.initials: CF
authors.lastname: Liao
authors.forename: Sheng-Fan
authors.initials: SF
authors.lastname: Wang
authors.forename: Yu-Ting
authors.initials: YT
authors.lastname: Lin
authors.forename: David D
authors.initials: DD
authors.lastname: Ho
authors.forename: Yi-Ming Arthur
authors.initials: YM
authors.lastname: Chen
mesh_terms: D000818:Animals; D019138:Antibodies, Blocking / Q000276:immunology / Q000494:pharmacology; D001665:Binding Sites / Q000235:genetics / Q000276:immunology; D015815:Cell Adhesion Molecules / Q000276:immunology / Q000378:metabolism*; D002460:Cell Line; D002681:China; D003713:Dendritic Cells / Q000276:immunology / Q000378:metabolism*; D015699:HIV Envelope Protein gp120 / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D015658:HIV Infections / Q000453:epidemiology / Q000276:immunology / Q000378:metabolism / Q000821:virology; D015497:HIV-1 / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007106:Immune Sera; D007118:Immunoassay; D037181:Lectins, C-Type / Q000276:immunology / Q000378:metabolism*; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D010957:Plasmids; D011134:Polysaccharides / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D011485:Protein Binding / Q000187:drug effects / Q000235:genetics / Q000276:immunology; D011817:Rabbits; D011956:Receptors, Cell Surface / Q000276:immunology / Q000378:metabolism*; D017422:Sequence Analysis, DNA; D013624:Taiwan; D014162:Transfection; D053586:Virus Internalization / Q000187:drug effects; D000099215:DC-Specific ICAM-3 Grabbing Nonintegrin
chemical_list: D019138:Antibodies, Blocking; D015815:Cell Adhesion Molecules; D015699:HIV Envelope Protein gp120; D007106:Immune Sera; D037181:Lectins, C-Type; D011134:Polysaccharides; D011956:Receptors, Cell Surface; D000099215:DC-Specific ICAM-3 Grabbing Nonintegrin