User:MDavis98/Merozoite surface protein

Function[edit]
MSP-1 is synthesized at the very beginning of schizogony, or asexual merozoite reproduction. The merozoite first attaches to a red blood cell using its MSP-1 complex. The MSP-1 complex targets spectrin, a complex on the internal surface of the cell membrane of a red blood cell. The majority of the MSP-1 complex is shed upon entry into the red blood cell, but a small portion of the C-terminus, called MSP-119, is conserved. The exact role of MSP-119 remains unknown, but it currently serves as a marker for the formation of the food vacuole. The relative size and location of each segment present on the MSP-1 complex is shown above. SS represents the signal sequence, which is a short sequence present on the N-terminus of new proteins. GA represents the GPI anchor, which is located at the C-terminus of the protein. The function of the MSP-2 complex is not concrete, but current research suggests it has a role in red blood cell invasion due to its degradation shortly after invasion. MSP- 3, 6, 7 and 9 are peripheral membrane proteins that have been shown to form a complex with MSP-1, but the functions of these proteins are largely unknown.