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HIV-2 neutralization epitopes are localized in the carboxyl terminal portion of the external envelope.

Goudsmit J, McKeating J, Meloen R, Smit L, Bakker M, Barin F; International Conference on AIDS.

Int Conf AIDS. 1989 Jun 4-9; 5: 480 (abstract no. C.732).

Human Retrovirus Laboratory, Amsterdam, the Netherlands

OBJECTIVE: To localize HIV-2 external envelop domains binding neutralizing antibodies. METHODS: Five hundred overlapping peptides that covered the complete amino acid sequence of the external envelope of the HIV-2 ROD strain were synthesized with the antibody-reactive peptide scanning (PEPSCAN) technique. Sera of HIV-2 infected individuals were used as probe for antibody reactivity. Rabbits were immunized with KLH coupled peptides of domains reactive with human sera. Sera were tested for HIV-2 neutralization. RESULTS: Fifteen domains were identified that bound serum of HIV-2 infected individuals. The majority of the sera reacted with two regions: one in the amino terminal half (aa 108-132) and one in the carboxyl terminal half (aa 303-507) of the external envelope. Each of the human HIV-2 neutralizing sera reacted with several carboxyl terminal epitopes. Sera of rabbits immunized with peptides covering the extreme terminal part of the external envelope neutralized HIV-2. Cross-neutralization with HIV-1 of these sera is under investigation. CONCLUSION: Epitopes localized in the extreme terminal carboxyl part of the HIV-2 external envelope bind natural neutralizing antibodies and immunization of rabbits with these domains results in HIV-2 neutralizing capacity of their serum.

Publication Types:
  • Meeting Abstracts
Keywords:
  • Amino Acid Sequence
  • Animals
  • Epitopes
  • HIV-1
  • HIV-2
  • Humans
  • Peptides
  • Rabbits
  • immunology
Other ID:
  • 00358789
UI: 102179489

From Meeting Abstracts




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