Solution conformation, backbone dynamics and lipid interactions of the intrinsically unstructured malaria surface protein MSP2.

ABSTRACT: Merozoite surface protein 2 (MSP2), one of the most abundant proteins on the surface of the merozoite stage of Plasmodium falciparum, is a potential component of a malaria vaccine, having shown some efficacy in a clinical trial in Papua New Guinea. MSP2 is a GPI-anchored protein consisting of conserved N- and C-terminal domains and a variable central region. Previous studies have shown that it is an intrinsically unstructured protein with a high propensity for fibril formation, in which the conserved N-terminal domain has a key role. Secondary structure predictions suggest that MSP2 contains long stretches of random coil with very little alpha-helix or beta-strand. Circular dichroism spectroscopy confirms this prediction under physiological conditions (pH 7.4) and in more acidic solutions

SUBMITTER: Zhang X 

PROVIDER: S-EPMC4432223 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature