The C-terminal domain of Plasmodium falciparum merozoite surface protein 3 self-assembles into alpha-helical coiled coil tetramer.
Proteins located on the surface of the pathogenic malaria parasite Plasmodium falciparum are objects of intensive studies due to their important role in the invasion of human cells and the accessibility to host antibodies thus making these proteins attractive vaccine candidates. One of these proteins, merozoite surface protein 3 (MSP3) represents a leading component among vaccine candidates; however, little is known about its structure and function. Our biophysical studies suggest that the 40 residue C-terminal domain of MSP3 protein self-assembles into a four-stranded alpha-helical coiled coil structure where alpha-helices are packed "side-by-side". A bioinformatics analysis provides an extended list of known and putative proteins from different species of Plasmodium which have such MSP3-like C-terminal domains. This finding allowed us to extend some conclusions of our studies to a larger group of the malaria surface proteins. Possible structural and functional roles of these highly conserved oligomerization domains in the intact merozoite surface proteins are discussed.
Centre de Recherches de Biochimie Macromoléculaire, CNRS UMR-5237, University of Montpellier 1 and 2, Montpellier, France.
Claire
C
Gondeau
Giampietro
G
Corradin
Frédéric
F
Heitz
Christian
C
Le Peuch
Andrea
A
Balbo
Peter
P
Schuck
Andrey V
AV
Kajava
D000818:Animals; D000953:Antigens, Protozoan / Q000737:chemistry*; D008958:Models, Molecular; D010963:Plasmodium falciparum / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011108:Polymers; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D015800:Protozoan Proteins / Q000737:chemistry*; D014461:Ultracentrifugation
D000953:Antigens, Protozoan; D011108:Polymers; D015800:Protozoan Proteins; C089133:merozoite surface protein 3, Plasmodium