Human immunodeficient virus type 1 gp120 C5 region mimics the HLA class I α1 peptide-binding domain

L. Lopalco, C. De Santis, R. Meneveri, R. Longhi, E. Ginelli, F. Grassi, A. G. Siccardi, A. Beretta

Research output: Contribution to journalArticlepeer-review


Molecular mimicry of major histocompatibility (MHC) antigens by viral glyco-proteins has been suggested as one of the possible mechanisms of induction of an autoimmnune response by human immunodeficiency viruses. A monoclonal antibody (M38) was previously shown to bind to both human immunodeficiency virus type 1 (HIV-1) gp120 and β-2 microglobulin-free HLA class I heavy chains encoded by an HLA C allele. Using HLA C recombinant proteins and synthetic peptides, the M38 class I binding site was mapped to a stretch of 44 amino acids of the α1 domain. The amino acid residues recognized are clustered in two non-contiguous regions at positions 66-69 (KYKR) and 79-82 (RKLR) shared by almost all HLA C alleles. On HIV-1 gp120, M38 binds to two non-contiguous sequences (KYK and KAKR) at positions 490-492 and 505-508 located at the edges of a large hydrophobic region that is apparently involved in binding the transmembrane glycoprotein gp41. The C-terminal gp120 M38-reactive region (KAKR) lies within the immunodominant sequence APTKAKRRVVQREKR, against which the majority of HIV-infected individulals produce antibodies. The results indicate that a functionally important region of HIV-1 gp120 shares similar amino acid sequence motifs with the antigen recognition site of most HLA class I C alleles. The molecular mimicry may be the basis for autoimmune responses in HIV infection.

Original languageEnglish
Pages (from-to)2016-2021
Number of pages6
JournalEuropean Journal of Immunology
Issue number8
Publication statusPublished - 1993


  • Acquired immunodeficiency syndrome
  • Autoimmunity
  • HLA
  • Human immunodeficiency virus

ASJC Scopus subject areas

  • Immunology


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