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Molecular Partitioning during Host Cell Penetration by Toxoplasma gondii
Author(s) -
Charron Audra J.,
Sibley L. David
Publication year - 2004
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2004.00228.x
Subject(s) - biology , raft , lipid raft , transmembrane protein , microbiology and biotechnology , toxoplasma gondii , membrane protein , parasite hosting , vacuole , membrane , biochemistry , cytoplasm , antibody , signal transduction , immunology , chemistry , receptor , organic chemistry , world wide web , computer science , copolymer , polymer
During invasion by Toxoplasma gondii , host cell transmembrane proteins are excluded from the forming parasitophorous vacuole membrane (PVM) by the tight apposition of host and parasite cellular membranes. Previous studies suggested that the basis for the selective partitioning of membrane constituents may be a preference for membrane microdomains, and this hypothesis was herein tested. The partitioning of a diverse group of molecular reporters for raft and nonraft membrane subdomains was monitored during parasite invasion by time‐lapse video or confocal microscopy. Unexpectedly, both raft and nonraft lipid probes, as well as both raft and nonraft cytosolic leaflet proteins, flowed unhindered past the host–parasite junction into the PVM. Moreover, neither a raft‐associated type 1 transmembrane protein nor its raft‐dissociated counterpart accessed the PVM, while a multispanning membrane raft protein readily did so. Considered together with previous data, these studies demonstrate that selective partitioning at the host–parasite interface is a highly complex process, in which raft association favors, but is neither necessary nor sufficient for, inclusion into the T. gondii PVM.