Antibodies to HIV-1 gp41 recognize synthetic peptides of human IFN-a and IFN-ß

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Based on our finding that a common epitope exists between HIV-1 gp41 and human type I interferons (IFN-a and IFN-ß), and increased levels of antibodies against human IFN-a and IFN-ß were observed in HIV-1-infected individuals, we tried to explain the mechanism of increased levels of antibodies. Mouse antisera recognizing HIV-1 recombinant soluble (rs) gp41 (aa 539-684) interacted with two synthetic peptides sequence-corresponding to the IFN-a/ß receptor binding site on human IFN-a and IFN-ß, while normal mouse serum (pooled normal sera) did not. The anti-rspg41 antisera after adsorption by IFN-ß sepharose column lost the activity of interaction with both synthetic peptides. In another experiment, rsgp41 could bind to sepharose column conjugated with anti-IFN-ß polyclonal antibodies (IgG). These results indicate that the common epitope on gp41 and type I interferons could induce antibodies recognizing the receptor binding site on IFN-a, and IFN-ß, suggesting that increased levels of antibodies against IFN-a and IFN-ß in HIV-1-infected individuals could be induced by gp41.

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International archives of allergy and immunology





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This article was published in International archives of allergy and immunology, Volume 121, Issue 2, Pages 170-172.

The published version is available at .

Copyright © 2000 Karger.

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