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A DUAL ACTION PEPTIDE GP120 INHIBITOR THAT IS EFFECTIVE AGAINST MULTIPLE HIV‐1 CLADES
Author(s) -
Cocklin Simon,
Gopi Hosahudya,
Baxter Sabine,
Chaiken Irwin
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.4.a465-c
Subject(s) - clade , human immunodeficiency virus (hiv) , virology , tropism , transmission (telecommunications) , entry inhibitor , biology , viral entry , virus , viral replication , gene , genetics , phylogenetics , electrical engineering , engineering
The AIDS epidemic, despite considerable effort, continues to spread at an alarming rate world‐wide, with an estimated 39.4 million people being infected with HIV‐1 as of the end of 2004; the great majority in Third World countries (including Africa, India, China, Myanmar, Thailand, Cambodia and Latin America). Sub‐Saharan Africa remains the hardest hit, with just under 64% of all people living with HIV‐1 residing there, an estimated 25.4 million people. Of the nine major clades of HIV‐1, HIV‐1 clade C accounts for over half of the infections worldwide. The most dominant means of transmission of HIV‐1 globally is by heterosexual intercourse and therefore compounds that could be used in vaginal formulations are increasingly seen as an urgent goal to stop transmission. As a means to this end, we have characterized an improved derivative of the 12p1 peptide, HNG105, against gp120s from clades A, B and C using surface plasmon resonance spectroscopy. HNG105 was found to directly bind to gp120s from clades A, B and C, irrespective of viral tropism, with affinities ranging from low to high nanomolar. In addition, HNG105 inhibited the interactions of these gp120s with their cognate cell surface receptor CD4, and also the coreceptor surrogate antibody 17b. Therefore, HNG105 may well be used alone or in combination with other HIV‐1 entry inhibitors, to provide an effective topical virocide.