Journal
FEBS LETTERS
Volume 580, Issue 9, Pages 2395-2399Publisher
WILEY
DOI: 10.1016/j.febslet.2006.03.067
Keywords
HIV-1; HIV-1 gp41; HIV-1 neutralization; Mab2F5; cardiolipin; antiphospholipid antibody
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HIV-1 neutralizing monoclonal antibody (Mab) 2175 recognizes a membrane-partitioning gp41 sequence. Just recently its capacity to react with cardiolipin has been demonstrated. Here, we have studied the specificity of Mab2F5-phospholipid interactions comparing partitioning into lipid bilayers with recognition of molecular species dispersed in solution. Using a liposome-based ELISA we demonstrate a preferential association with cardiolipin bilayers. When different soluble lysoderivatives were compared in their capacity to inhibit Mab2F5 binding to immobilized HIV-1 peptide epitope, only dilysocardiolipin resulted effective in blocking the process. Dilyso-cardiolipin also competed with native-functional gp41 for 2F5 recognition. Thus, our data support specific cardiolipin recognition by 2F5 that is not dependent on lipid bilayer assembly and involves the epitope-binding site. These findings might be of relevance for understanding the molecular basis of HIV-1 immune evasion. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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