Specific Phospholipid Recognition by Human Immunodeficiency Virus Type-1 Neutralizing Anti-gp41 2f5 Antibody.
From: Biofisika Unitatea (CSIC-UPV/EHU) and Biokimika Saila, Euskal Herriko Unibertsitatea, Posta Kutxa 644, 48080 Bilbao, Spain.
FEBS letters
- Publish Date: Apr 2006
- ISSN: 0014-5793
- Volume: 580
- Issue: 9
- Pages: 2395-99
- Medium: Print
- Language: English
- Citation (JAMA): Sánchez-Martínez Silvia, Lorizate Maier, Hermann Katinger, et al. Specific Phospholipid Recognition by Human Immunodeficiency Virus Type-1 Neutralizing Anti-gp41 2f5 Antibody.. FEBS Lett. Apr 2006;580:2395-99
Abstract
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.
Mesh Headings (Keywords): Animals, Antibodies, Monoclonal, Antibodies, Viral, Binding Sites, Antibody, Cardiolipins, Epitope Mapping, Epitopes, HIV Envelope Protein gp41, HIV-1, Humans, Lipid Bilayers, Membrane Fusion, Peptides
Check for Full Text / PubMed Unique Identifier (PMID): 16616522
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