期刊
MOLECULAR AND BIOCHEMICAL PARASITOLOGY
卷 153, 期 1, 页码 31-40出版社
ELSEVIER
DOI: 10.1016/j.molbiopara.2007.01.015
关键词
malaria; Plasmodium vivax; MSP-1 structure; dimer; merozoite surface protein
资金
- MRC [MC_U117532067, MC_U117533887] Funding Source: UKRI
- Medical Research Council [MC_U117532067, MC_U117533887] Funding Source: researchfish
- Medical Research Council [MC_U117532067, MC_U117533887] Funding Source: Medline
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.
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