Alekseeva A S, Tretiakova D S, Chernikov V P, Utkin Yu N, Molotkovsky J G, Vodovozova E L, Boldyrev I A
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, Moscow, 117997, Russia.
Research Institute of Human Morphology, 3 Tsurupa Street, Moscow, 117418, Russia.
Toxicon. 2017 Jul;133:169-179. doi: 10.1016/j.toxicon.2017.05.015. Epub 2017 May 17.
We report that the action of the heterodimeric phospholipases A2 (PLA2s) from Vipera nikolskii, which comprises enzymatically active basic subunit and inactive acidic PLA2 homologue, on the lipid bilayer results in the aggregation and stacking of bilayers. These processes are demonstrated using two independent methods (fluorescence spectroscopy and electron microscopy). Aggregation of bilayers is possible because both subunits of the V. nikolskii heterodimer contain a membrane-binding site (also known as IBS). Thus, when the two IBSs bind to the membrane, the heterodimer acts as a connecting agent. Heterodimers induce aggregation of negatively charged bilayers composed of phosphatidylglycerol and do not induce aggregation of neutral bilayers composed of phosphatidylcholine.
