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Originally published In Press as doi:10.1074/jbc.M011709200 on February 1, 2001

J. Biol. Chem., Vol. 276, Issue 18, 15249-15255, May 4, 2001
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A Homologue of N-Ethylmaleimide-sensitive Factor in the Malaria Parasite Plasmodium falciparum Is Exported and Localized in Vesicular Structures in the Cytoplasm of Infected Erythrocytes in the Brefeldin A-sensitive Pathway*

Mitsuko HayashiDagger §, Shinya TaniguchiDagger , Yuki Ishizuka, Hye-Sook Kim, Yusuke Wataya, Akitsugu Yamamoto||, and Yoshinori Moriyama**

From the Departments of Biochemistry and  Medicinal Informatics, Faculty of Pharmaceutical Sciences, Okayama University, Okayama 700-8530, Japan and the || Department of Physiology, Kansai Medical University, Moriguchi, Osaka 570-8506, Japan

N-Ethylmaleimide-sensitive factor (NSF) and its homologues play a central role in vesicular trafficking in eukaryotic cells. We have identified a NSF homologue in Plasmodium falciparum (PfNSF). The reported PfNSF gene sequence (GenBankTM accession number CAB10575) indicated that PfNSF comprises 783 amino acids with a calculated molecular weight of 89,133. The overall identities of its gene and amino acid sequences with those of rat NSF are 50.9 and 48.8%, respectively. Reverse transcription-polymerase chain reaction analysis and Northern blotting with total P. falciparum RNA indicated expression of the PfNSF gene. Polyclonal antibodies against a conserved region of NSF specifically recognized an 89-kDa polypeptide in the parasite cells. After homogenization of the parasite cells, ~90% of an 89-kDa polypeptide is associated with particulate fraction, suggesting membrane-bound nature of PfNSF. PfNSF was present within both the parasite cells and the vesicular structure outside of the parasite cells. The export of PfNSF outside of the parasite cells appears to occur at the early trophozoite stage and to terminate at the merozoite stage. The export of PfNSF is inhibited by brefeldin A, with 9 µM causing 50% inhibition. Immunoelectromicroscopy indicated that intracellular PfNSF was associated with organelles such as food vacuoles and that extracellular PfNSF was associated with vesicular structures in the erythrocyte cytoplasm. These results indicate that PfNSF expressed in the malaria parasite is exported to the extracellular space and then localized in intraerythrocytic vesicles in a brefeldin A-sensitive manner. It is suggested that a vesicular transport mechanism is involved in protein export targeted to erythrocyte membranes during intraerythrocytic development of the malaria parasite.

* This work was supported in part by Grant-in-aid 08281105 for Scientific Research on Priority Areas from the Ministry of Education, Science, Sports and Culture of Japan.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) CAB10575.

Dagger The first two authors contributed equally to the present work.

§ Supported by the Hayashi Memorial Foundation for Female Natural Scientists and by a Research Fellowship from the Japan Society for Promotion of Science for Young Scientists.

** To whom correspondence should be addressed: Dept. of Biochemistry, Faculty of Pharmaceutical Sciences, Okayama University, Okayama 700-8530, Japan. Tel. and Fax: 81-86-251-7933; E-mail: moriyama@pheasant.pharm.okayama-u.ac.jp.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.