PLASMODIUM-FALCIPARUM PROTEIN ASSOCIATED WITH THE INVASION JUNCTION CONTAINS A CONSERVED OXIDOREDUCTASE DOMAIN

被引:17
作者
HUDSONTAYLOR, DE
DOLAN, SA
KLOTZ, FW
FUJIOKA, H
AIKAWA, M
KOONIN, EV
MILLER, LH
机构
[1] NIAID, MALARIA RES LAB, BETHESDA, MD 20892 USA
[2] WALTER REED ARMY MED CTR, DEPT IMMUNOL, WASHINGTON, DC 20307 USA
[3] CASE WESTERN RESERVE UNIV, INST PATHOL, CLEVELAND, OH 44106 USA
[4] NIH, NATL LIB MED, DIV NATL CTR BIOTECHNOL INFORMAT, BETHESDA, MD 20892 USA
关键词
D O I
10.1111/j.1365-2958.1995.tb02260.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The merozoite cap Protein-1 (MCP-1) of Plasmodium falciparum follows the distribution of the moving junction during invasion of erythrocytes. We have cloned the gene encoding this protein from a cDNA library using a monoclonal antibody, The protein lacks a signal sequence and has no predicted transmembrane domains; none of the antisera reacts with the surfaces of intact merozoites, indicating that the cap distribution is submembranous. MCP-1 is divided into three domains. The N-terminal domain includes a 52-amino-acid region that is highly conserved in a large family of bacterial and eukaryotic proteins. Based on the known functions of two proteins of this family and the pattern of amino acid conservation, it is predicted that this domain may possess oxidereductase activity, since the active cysteine residue of this domain is invariant in all proteins of the family. The other two domains of MCP-1 are not found in any other members of this protein family and may reflect the specific function of MCP-1 in invasion, The middle domain is negatively charged and enriched in glutamate; the C-terminal domain is positively charged and enriched in lysine, By virtue of its positive charge, the C-terminal domain resembles domains in some cytoskeleton-associated proteins and may mediate the interaction of MCP-1 with cytoskeleton in Plasmodium.
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收藏
页码:463 / 471
页数:9
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