Antibodies to HIV-1 gp41 Recognize Synthetic Peptides of Human IFN-α and IFN-β

Abstract

Based on our finding that a common epitope exists between HIV-1 gp41 and human type I interferons (IFN-α and IFN-β), and increased levels of antibodies against human IFN-α and IFN-β 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-α/β receptor binding site on human IFN-α and IFN-β, while normal mouse serum (pooled normal sera) did not. The anti-rspg41 antisera after adsorption by IFN-β sepharose column lost the activity of interaction with both synthetic peptides. In another experiment, rsgp41 could bind to sepharose column conjugated with anti-IFN-β 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-α and IFN-β, suggesting that increased levels of antibodies against IFN-α and IFN-β in HIV-1-infected individuals could be induced by gp41.