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J. Biol. Chem., Vol. 278, Issue 25, 22257-22264, June 20, 2003

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The Merozoite Surface Protein 1 Complex of Human Malaria Parasite Plasmodium falciparum

INTERACTIONS AND ARRANGEMENTS OF SUBUNITS^*

Christian W. Kauth, Christian Epp, Hermann Bujard  and Rolf Lutz

From the Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH), Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany

The major protein component at the surface of merozoites, the infectious form of blood stage malaria parasites, is the merozoite surface protein 1 (MSP-1) complex. In the human malaria parasite Plasmodium falciparum, this complex is generated by proteolytic cleavage of a 190-kDa glycosylphosphatidylinositol-anchored precursor into four major fragments, which remain non-covalently associated. Here, we describe the in vitro reconstitution of the MSP-1 complex of P. falciparum strain 3D7 from its heterologously produced subunits. We provide evidence for the arrangement of the subunits within the complex and show how they interact with each other. Our data indicate that the conformation assumed by the reassembled complex as well as by the heterologously produced 190-kDa precursor corresponds to the native one. Based on these results we propose a first structural model for the MSP-1 complex. Together with access to faithfully produced material, this information will advance further structure-function studies of MSP-1 that plays an essential role during invasion of erythrocytes by the parasite and that is considered a promising candidate for a malaria vaccine.

Received for publication, March 5, 2003 , and in revised form, March 19, 2003.

^* This work was supported by the research fund of the Ministerium fuer Wissenschaft, Forschung und Kunst Baden-Wuerttemberg, and Deutsche Forschungsgemeinschaft Grant SFB 544. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. E-mail: h.bujard{at}zmbh.uni-heidelberg.de.

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