A 22 kDa protein associated with the Plasmodium falciparum merozoite surface protein-1 complex.

被引:46
作者
Stafford, WHL
Gunder, B
Harris, A
Heidrich, HG
Holder, AA
Blackman, MJ
机构
[1] NATL INST MED RES, DIV PARASITOL, LONDON NW7 1AA, ENGLAND
[2] NATL INST MED RES, SEQUENCING & SYNTH SERV SECT, LONDON NW7 1AA, ENGLAND
[3] MAX PLANCK INST BIOCHEM, D-82152 MARTINSRIED, GERMANY
基金
英国医学研究理事会;
关键词
malaria; Plasmodium falciparum; merozoite surface protein; MSP-1; proteolytic processing; erythrocyte invasion;
D O I
10.1016/0166-6851(96)02696-5
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 Plasmodium falciparum merozoite surface protein-1 (MSP-1) is sythesized as a precursor of similar to 195 kDa and is processed to form a complex of polypeptides on the surface of free merozoites. As a result of a second processing event, the entire MSP-1 complex is shed from the surface, apart from a C-terminal fragment that remains anchored to the merozoite membrane. We have identified a 22 kDa protein (p22) on the surface of merozoites by cell surface radioiodination and indirect immunofluorescence assay on unfixed free merozoites. p22 is also a component of the shed MSP-1 complex where it is present in part as a 19 kDa form (p22(19)) as shown by immunochemical and peptide mapping analyses, The soluble complex contains MSP-1-derived polypeptides and p22 in approximately stoichiometrically equal amounts. N-terminal amino acid sequence analyses of p22/p22(19) showed that the protein is not derived from the MSP-1 precursor.
引用
收藏
页码:159 / 169
页数:11
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