PMID: 11909736Mar 23, 2002Paper

A role for Toxoplasma gondii type 1 ser/thr protein phosphatase in host cell invasion

Microbes and Infection
Violaine DelormeIsabelle Tardieux

Abstract

Host cell invasion by Toxoplasma gondii tachyzoites relies on many coordinated processes. The tachyzoite participates in invasion by providing an actomyosin-dependent force driving it into the nascent parasitophorous vacuole as well as by releasing molecules which contribute to the vacuole membrane. Exposure to type 1/2A protein phosphatase inhibitors, okadaic acid (OA) or tautomycin significantly impairs tachyzoite invasiveness. Furthermore, the tachyzoite extract contains a biochemically active type 1, but not a type 2A, serine-threonine protein phosphatase, which is immunologically related to eukaryotic phosphatase type 1 catalytic subunit. When tachyzoite extracts are incubated with a monoclonal antibody reactive to human type 1 catalytic subunit, other T. gondii molecules are coprecipitated among which one competes with the inhibitory toxin OA. Finally, in vitro phosphate labelling assays indicate that the biochemically characterized PP1 activity controls the phosphorylation of several proteins. Taken together, these data strongly suggest that the type 1 phosphatase activity detected in invasive tachyzoites is implicated in the control of the host cell invasion process.

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Citations

Jul 9, 2005·The Journal of Biological Chemistry·Xing W ZhouVern B Carruthers
Jun 13, 2003·Molecular Biology of the Cell·Violaine DelormeIsabelle Tardieux
Dec 5, 2013·Molecular and Biochemical Parasitology·Cécile GalletLinda Kohl
Jun 27, 2012·Annals of the New York Academy of Sciences·Caroline M Weight, Simon R Carding
Jul 29, 2008·Microbes and Infection·Jorge E ArayaJorge González
Jul 16, 2008·Molecular and Biochemical Parasitology·Mikhail A Kutuzov, Alexandra V Andreeva
May 31, 2017·Molecular Microbiology·Chunlin Yang, Gustavo Arrizabalaga
Jul 27, 2021·Parasitology Research·Jenny Nancy Gómez-SandovalM Magdalena Aguirre-García

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