Structural studies on Plasmodium vivax merozoite surface protein-1
Details
Publication Year 2007-05,Volume 153,Issue #1,Page 31-40
Journal Title
MOLECULAR AND BIOCHEMICAL PARASITOLOGY
Publication Type
Journal Article
Abstract
Plasmodium vivax infection is the second most common cause of malaria throughout the world. Like other Plasmodium species, P. vivax has a large protein complex, MSP-1, located on the merozoite surface. The C-terminal MSP-1 sub-unit, MSP-1(42), is cleaved during red blood cell invasion, causing the majority of the complex to be shed and leaving only a small 15 kDa sub-unit, MSP-1(19), on the merozite surface. MSP-1(19) is considered a strong vaccine candidate. We have determined the solution structure of MSP-1(19) from P. vivax using nuclear magnetic resonance (NMR) and show that, like in other Plasmodium species, it consists of two EGF-like domains that are oriented head-to-tail. The protein has a flat, disk-like shape with a highly charged surface. When MSP-1(19) is part of the larger MSP-1(42) precursor it exists as an independent domain with no stable contacts to the rest of the sub-unit. Gel filtration and analytical ultracentrifugation experiments indicate that P vivax MSP-1(42), exists as a dimer in solution. MSP-1(19) itself is a monomer, however, 35 amino-acids immediately upstream of its N-terminus are sufficient to cause dimerization. Our data suggest that if MSP-1(42) exists as a dimer in vivo, secondary processing would cause the dissociation of two tightly linked MSP-1(19) proteins on the merozoite surface just prior to invasion. Crown Copyright (C) 2007 Published by Elsevier B.V. All rights reserved.
Publisher
ELSEVIER SCIENCE BV
Keywords
MALARIA VACCINE CANDIDATE; C-TERMINAL FRAGMENT; ERYTHROCYTE INVASION; MONOCLONAL-ANTIBODY; FALCIPARUM MEROZOITES; INHIBITORY ANTIBODIES; CRYSTAL-STRUCTURE; FINE SPECIFICITY; TROSY NMR; IN-VITRO
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Creation Date: 2007-05-01 12:00:00
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