AEGiS-07IAC: Synthetic peptides derived from the principal neutralizing domain (PND) of human immunodeficiency virus type 1 (HIV-1) enhance HIV-1 infection.

7th International AIDS Conference


Florence, Italy — June 16-21, 1991

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Synthetic peptides derived from the principal neutralizing domain (PND) of human immunodeficiency virus type 1 (HIV-1) enhance HIV-1 infection.

Int Conf AIDS 1991 Jun 16-21; 7:41 (abstract no. M.A.77)
DeRossi A, Pasti M, Mammano F, Panozzo M, Dettin M, DiBello C, Chieco-Bianchi L; Institute of Oncology, Institute of Industrial Chemistry, University of Padova, Italy

OBJECTIVE: To investigate biological properties of PND from different HIV-1 strains.

METHODS: 24-mer peptides derived from PND (301-324 aminoacid sequence) of different HIV-1 strains were synthesized on solid support using a peptide synthetizer (Applied Biosystems 431A). Target cell (MOLT-3 and H938) infection with MN, IIIB, and RF HIV-1 strains was carried out in the presence of scalar amounts of peptides. Virus yield was evaluated by reverse transcriptase assay and CAT assay.

RESULTS: Peptide designed from the V3-PND of HIV-1 MN strain enhanced viral infection. The activity of HIV-1 HTLV-IIIB- derived peptide was at least tenfold less efficient, while no enhancing effect was shown by HIV-1 RF specific peptide. This enhancing effect occurred in the early steps of viral infection and was not strain-restricted in that both MN- and IIIB-derived peptides were able to increase heterologous virus expression, including that of the RF strain. Both MN- and IIIB- derived peptides were able to block in a dose-dependent manner the CD4 down-regulation induced by the monosialoganglioside GM1, while peptides without enhancing effect did not. MN-derived peptide induced an increase in CD4 epitopes on the cell membrane, and was able to partially block CD4 internalization induced by the phorbol ester 12-0-tetradecanoylphorbol 13 acetate.

CONCLUSIONS: These findings suggest that the viral enhancement induced by the PND-derived peptides occurred through a mechanism involving cellular CD4 viral receptor.

Keywords: AEGIS, HIV-1, HIV Infections, Antigens, CD4, Peptides, Epitopes, RNA-Directed DNA Polymerase, Cats, Animal, Human, ICA7KWDaegis,hiv-1,hivinfections,antigens,cd4,peptides,epitopes,rna-directeddnapolymerase,cats,animal,human,ica7
910616
MA77

Copyright © 1991 - International AIDS Society (IAS). Reproduction of this abstract (other than one copy for personal reference) must be cleared through the IAS.