Budding of giant unilamellar vesicles induced by an amphitropic protein β2-glycoprotein I

β2-glycoprotein I (β2GPI) is a plasma protein capable of binding reversibly to membranes, and is classified among the amphitropic proteins. Part of the protein intercalates into the outer membrane leaflet, altering the difference between the preferred areas of the membrane leaflets, which results in membrane shape transformations. Budding, as a specific example of such shape transformations, was studied using giant unilamellar vesicles. Our aim was to identify the vesicle parameters that influence the degree of membrane budding by studying this process qualitatively and quantitatively. A simple theoretical model has been developed and assessed against the experimental observations. The results show that β2GPI binds in a concentration dependent manner, causing transitions between vesicle shapes with increasing numbers of buds. Higher numbers of buds are characteristic of larger and/or more flaccid vesicles. When the vesicle membrane is strained, a higher β2GPI concentration is needed to produce the same effects as on the unstrained vesicle. Vesicles were found to be highly individual in their behaviour, so each was treated individually. Specific vesicle behaviour was found to be the consequence of the neck between the main vesicle body and the buds, which could be either open, closed for the exchange of solution, or closed for the exchange of both solution and membrane.

Graphical AbstractResearch Highlights►β2-glycoprotein I induces vesicle budding ►the number of buds is greater for more flaccid and/or larger vesicles ►binding of such proteins to vesicles and vesicle shape are mutually interdependent