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J. Biol. Chem., Vol. 281, Issue 42, 31517-31527, October 20, 2006

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Interactions between Merozoite Surface Proteins 1, 6, and 7 of the Malaria Parasite Plasmodium falciparum^*

Christian W. Kauth, Ute Woehlbier, Michaela Kern¹, Zeleke Mekonnen, Rolf Lutz, Norbert Mücke, Jörg Langowski, and Hermann Bujard²

From the Zentrum fuer Molekulare Biologie der Universitaet Heidelberg, Im Neuenheimer Feld 282, D-69120 Heidelberg and Division of Biophysics of Macromolecules, German Cancer Research Center, D-69120 Heidelberg, Germany

Merozoites of the malaria parasite Plasmodium falciparum expose at their surface a large multiprotein complex, composed of proteolytically processed, noncovalently associated products of at least three genes, msp-1, msp-6, and msp-7. During invasion of erythrocytes, this complex is shed from the surface except for a small glycosylphosphatidylinositol-anchored portion originating from MSP-1. The proteolytic cleavage separating the C-terminal portion of MSP-1 is required for successful invasion. Little is known about the structure and function of the abundant and essential multipartite complex. Using heterologously produced MSP-1, MSP-6, and MSP-7 in precursor and with the exception of MSP-7 in processed form, we have studied in vitro the complex formation between the different proteins to identify the interaction partners within the complex. Both MSP-6₃₆ and MSP-7 bind only to MSP-1 subunits that are shed, but although MSP-6₃₆ contacts just subunit p38, MSP-7 interacts with p83, p30, and p38. The intact C-terminal region of MSP-6 is required for the association with p38 as well as for its multimerization into tetramers. Furthermore, our data suggest that only the processed form and not the precursor form of MSP-1 interacts with MSP-6₃₆. MSP-6- as well as MSP-7-specific rabbit antibodies inhibit parasite multiplication in vitro as shown previously for antibodies directed against MSP-1. Our findings raise interesting questions with regard to proteolysis-mediated mechanisms of maturation of the MSP-1-MSP-6-MSP-7 complex and to the mode by which antibodies directed against this complex interfere with parasite multiplication.

Received for publication, May 15, 2006 , and in revised form, August 18, 2006.

^* This work was supported by funds from the State of Baden-Wuerttemberg and by 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.

¹ Present address: Institute of Molecular Medicine and Experimental Immunology, D-53105 Bonn, Germany.

² To whom correspondence should be addressed. Tel.: 49-6221-54-8214; Fax: 49-6221-54-5892; E-mail: h.bujard{at}zmbh.uni-heidelberg.de.

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