Unusual properties of Plasmodium falciparum actin: new insights into microfilament dynamics of apicomplexan parasites.

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Schuler H, Mueller AK, Matuschewski K

Unusual properties of Plasmodium falciparum actin: new insights into microfilament dynamics of apicomplexan parasites.

FEBS Lett. 2005 Jan 31;579(3):655-60. doi: 10.1016/j.febslet.2004.12.037.

PubMed ID
15670824 [ View in PubMed
]
Abstract

Plasmodium falciparum, the etiologic agent of malaria, is a facultative intracellular parasite of the phylum Apicomplexa. A limited turnover of microfilaments takes place beneath the parasite plasma membrane, but the cytoplasm of apicomplexans is virtually devoid of F-actin. We produced Plasmodium actin in yeast. Purified recombinant Plasmodium actin polymerized inefficiently unless both gelsolin and phalloidin were added. The resulting actin polymers appeared fragmented in the fluorescence microscope. Plasmodium actin bound DNaseI about 200 times weaker than bovine non-muscle actin. Our findings suggest that the unique properties of Plasmodium actin can explain some of the unusual features of apicomplexan parasite microfilaments.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Actin-1P86287Details