Isolation and functional characterization of a dynamin-like gene from Plasmodium falciparum

Biochemical and Biophysical Research Communications
Huiliang LiHeng Wang

Abstract

A novel dynamin-like GTPase gene, Pfdyn1, was cloned from an asexual stage cDNA library of Plasmodium falciparum Dd2 strain. Pfdyn1 contains a highly conserved N-terminal tripartite GTPase domain, a coiled-coil region, and a C-terminal 129 aa unknown function domain. Like yeast Vps1p, it lacks pleckstrin homology domain and proline-rich region. Western blot analysis showed that Pfdyn1 is a Triton X-100 insoluble protein expressed only in the mature sub-stage. Morphological studies indicated that Pfdyn1 is partly co-localized with PfGRP, a known ER-resident protein, and localizes diffusely with several membrane structures and a 60-100 nm vesicle both inside and on surface of the parasites and also in the cytoplasm of infected erythrocytes. The dsRNA originated by C-terminus fragment of Pfdyn1 inhibits markedly the growth of P. falciparum parasite at the erythrocyte stage. Those data showed that Pfdyn1 is a conservative, membrane related protein and plays an essential role for the survival of Plasmodium parasite.

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Citations

Oct 10, 2012·Molecular and Biochemical Parasitology·Marcel DeponteJude M Przyborski
Nov 6, 2007·Biochemical and Biophysical Research Communications·Suresh H BasagoudanavarD Channe Gowda
May 30, 2007·Microbes and Infection·Sébastien CharneauIsabelle Florent
May 13, 2006·Biochimica Et Biophysica Acta·Tsuneyoshi KuroiwaOsami Misumi
Apr 25, 2006·BioTechniques·Anthony E Brown, Flaminia Catteruccia
Nov 22, 2019·PLoS Pathogens·Luboš Voleman, Pavel Doležal
Sep 3, 2016·FEMS Microbiology Reviews·Emma S Sherling, Christiaan van Ooij
Dec 16, 2020·Parasitology International·Ying ZhangHonglin Jia
May 7, 2021·Frontiers in Cellular and Infection Microbiology·Alexander A Morano, Jeffrey D Dvorin
Aug 25, 2021·MBio·Julie M J VerhoefTaco W A Kooij

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