Maria F Perdomo

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Introduction Due to the great variability and high glycosylation of gp120, possible targets for a fusion inhibitor include the CD4 binding region of gp120. Here we describe a method by which peptides corresponding to residues 25 to 64 of the CD4 receptor have been coupled to a major antigen, the gal-alpha 1,3-gal disaccharide, towards which humans have(More)
The great variability and high glycosylation of gp120 poses a great challenge for the design of a functional immune therapy. The binding region of the CD4 receptor to gp120, however, is well conserved and may constitute a target to limit viral entry and infectivity. Our strategy consists in using a preexisting pool of natural antibodies directed toward the(More)
In vitro studies on HIV (HIV-1) replication and neutralization are usually performed in human cell cultures supplemented with FBS instead of human serum (HS). Here we show that in contrast to FBS, addition of increasing amounts of human serum from noninfected donors to the cell culture directly correlates with an increase in HIV-1 replication in vitro. This(More)
We have previously proposed a method by which natural antibodies can be redirected toward a known pathogen. We could show that CD4-derived peptides coupled to the galα1,3gal sugar moiety, a specificity held by natural antibodies, were able to neutralize HIV. Importantly, the antibody-peptide-antigen complexes activated the innate immune system through the(More)
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