Discrete regions of HIV-1 gp41 defined by syncytia-inhibiting affinity-purified human antibodies

S. Vanini, R. Longhi, A. Lazzarin, E. Vigo, A. G. Siccardi, G. Viale

Research output: Contribution to journalArticlepeer-review


Objective: Fine mapping of HIV-1 gp41 fusion-critical sites. Design and methods: Antibodies from human HIV-1-positive sera were affinity-purified on a panel of synthetic overlapping peptides spanning residues 526-682 of the extracellular portion of HIV-1 gp41. The syncytium-inhibiting capacity of the immunopurified antibodies and their differential reactivity on the synthetic peptides were tested. Results: This approach enabled the identification of residues 583-591 (ARILAVERY), 595-599 (QQLLG), 603-609 (CSGKLIC) and 664-673 (ELLELDKWAS) as possibly involved in the fusion process. Reduction in the anti-ARILAVERY, anti-CSGKLIC and anti-ELLELDKWAS antibody titres and frequencies correlates with disease progression. Syncytia-inhibition capacity of sera did not correlate with the presence of high-titre antibodies reacting with any of the peptides tested, suggesting that most fusion-affecting antibodies are not directed towards gp41. Conclusions: This strategy may be relevant for understanding the contribution of anti-gp41 antibodies in protecting against the pathogenic effects of the virus and in the design of an effective env vaccine.

Original languageEnglish
Pages (from-to)167-174
Number of pages8
JournalAIDS (London, England)
Issue number2
Publication statusPublished - 1993


  • Affinity-purification
  • Epitope mapping
  • HIV-1 gp41
  • Syncytia-inhibiting human serum antibodies

ASJC Scopus subject areas

  • Immunology
  • Immunology and Allergy


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