Sánchez-Martínez Silvia, Lorizate Maier, Hermann Katinger, Kunert Renate, Basañez Gorka, Nieva José L
Biofisika Unitatea (CSIC-UPV/EHU) and Biokimika Saila, Euskal Herriko Unibertsitatea, Posta Kutxa 644, 48080 Bilbao, Spain.
FEBS Lett. 2006 Apr 17;580(9):2395-99. doi: 10.1016/j.febslet.2006.03.067.
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.
HIV-1中和单克隆抗体（Mab）2F5识别一个膜分区gp41序列。最近已证实其与心磷脂发生反应的能力。在此，我们通过比较脂质双层中的分配与对分散在溶液中的分子种类的识别，研究了Mab2F5与磷脂相互作用的特异性。使用基于脂质体的ELISA，我们证明了其与心磷脂双层的优先结合。当比较不同的可溶性溶血衍生物抑制Mab2F5与固定化HIV-1肽表位结合的能力时，只有二溶血心磷脂能有效阻断这一过程。二溶血心磷脂也与天然功能性gp41竞争2F5识别。因此，我们的数据支持2F5对心磷脂的特异性识别，这种识别不依赖于脂质双层组装，且涉及表位结合位点。这些发现可能与理解HIV-1免疫逃逸的分子基础有关。
