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Specific phospholipid recognition by human immunodeficiency virus type‐1 neutralizing anti‐gp41 2F5 antibody
Author(s) -
Sánchez-Martínez Silvia,
Lorizate Maier,
Katinger Hermann,
Kunert Renate,
Basañez Gorka,
Nieva José L.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.03.067
Subject(s) - epitope , gp41 , monoclonal antibody , cardiolipin , chemistry , liposome , phospholipid , antibody , virology , lipid bilayer , biochemistry , membrane , biology , immunology
HIV‐1 neutralizing monoclonal antibody (Mab) 2F5 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.