Human antibodies to immunodominant C5 region of HIV-1 gp120 cross-react with HLA class I on activated cells

C. De Santis, L. Lopalco, P. Robbioni, R. Longhi, G. Rappocciolo, A. G. Siccardi, A. Beretta

Research output: Contribution to journalArticle

Abstract

Cross-reactive antibodies to HLA class I and HIV-1 gp120 were detected in the sera of HIV-1-positive individuals, and were found to share the same epitope specificity as a gp120-HLA class I cross-reactive monoclonal antibody (M38). The amino acid residues of HLA recognized by both M38 and the patient antibodies occur as a clustered pair in the HLA-C α1 domain. These sequences (KYKR and RKLR) are shared by almost all HLA-C alleles and are available to antibody binding only on β2-microglobulin-dissociated HLA heavy chains expressed on activated cells. Similar to M38, the antibody- binding sites on HIV-1 gp120 were mapped to two noncontiguous stretches of amino acids (KYK and KAKR), which flank a hydrophobic area of the immunodominant C5 region involved in gp41 binding. Serum antibodies immunoaffinity purified on synthetic HLA and gp120 peptides representing the M38-reactive regions were shown to bind to both HLA and gp120 in Western blot, as well as to membrane-bound HLA heavy chains, and to exhibit selective complement-mediated lysis of activated T cells. No serum antibodies could be detected that bind to the gp120 C5 region (peptide IEPLGVAPT) flanked by the two HLA-like sequences.

Original languageEnglish
Pages (from-to)157-162
Number of pages6
JournalAIDS Research and Human Retroviruses
Volume10
Issue number2
Publication statusPublished - 1994

ASJC Scopus subject areas

  • Immunology
  • Virology

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    De Santis, C., Lopalco, L., Robbioni, P., Longhi, R., Rappocciolo, G., Siccardi, A. G., & Beretta, A. (1994). Human antibodies to immunodominant C5 region of HIV-1 gp120 cross-react with HLA class I on activated cells. AIDS Research and Human Retroviruses, 10(2), 157-162.