Parasite Calcineurin Regulates Host Cell Recognition and Attachment by Apicomplexans

Cell Host Microbe. 2015 Jun 24. pii: S1931-3128(15)00251-6. doi: 10.1016/j.chom.2015.06.003. [Epub ahead of print]
 

Paul AS¹, Saha S², Engelberg K², Jiang RH¹, Coleman BI², Kosber AL¹, Chen CT², Ganter M¹, Espy N¹, Gilberger TW³, Gubbels MJ², Duraisingh MT⁴.

Apicomplexans invade a variety of metazoan host cells through mechanisms involving host cell receptor engagement and secretion of parasite factors to facilitate cellular attachment. We find that the parasite homolog of calcineurin, a calcium-regulated phosphatase complex central to signal transduction in eukaryotes, also contributes to host cell invasion by the malaria parasite Plasmodium falciparum and related Toxoplasma gondii. Using reverse-genetic and chemical-genetic approaches, we determine that calcineurin critically regulates and stabilizes attachment of extracellular P. falciparum to host erythrocytes before intracellular entry and has similar functions in host cell engagement by T. gondii. Calcineurin-mediated Plasmodium invasion is strongly associated with host receptors required for host cell recognition, and calcineurin function distinguishes this form of receptor-mediated attachment from a second mode of host-parasite adhesion independent of host receptors. This specific role of calcineurin in coordinating physical interactions with host cells highlights an ancestral mechanism for parasitism used by apicomplexans.
Copyright © 2015 Elsevier Inc. All rights reserved.

PMID:

26118996

[PubMed - as supplied by publisher]