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dc.contributor.authorChin, E.
dc.contributor.authorKirker, Kelly R.
dc.contributor.authorZuck, Meghan
dc.contributor.authorJames, Garth A.
dc.contributor.authorHybiske, K.
dc.date.accessioned2017-01-31T23:40:05Z
dc.date.available2017-01-31T23:40:05Z
dc.date.issued2012-10
dc.identifier.citationChin E, Kirker K, Zuck M, James G, Hybiske K, "Actin recruitment to the Chlamydia inclusion is spatiotemporally regulated by a mechanism that requires host and bacterial factors," PLoS ONE, October 2012 7(10):1-12 To enable screen reader support, press shortcut Ctrl+Alt+Z. To learn about keyboard shortcuts, press shortcut Ctrl+slash. CBE JJCBE Explore Chin E, Kirker K, Zuck M, James G, Hybiske K, "Actin recruitment to the Chlamydia inclusion is spatiotemporally regulated by a mechanism that requires host and bacterial factors," PLoS ONE, October 2012 7(10):1-12en_US
dc.identifier.issn1932-6203
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/12504
dc.description.abstractThe ability to exit host cells at the end of their developmental growth is a critical step for the intracellular bacterium Chlamydia. One exit strategy, extrusion, is mediated by host signaling pathways involved with actin polymerization. Here, we show that actin is recruited to the chlamydial inclusion as a late event, occurring after 20 hours post-infection (hpi) and only within a subpopulation of cells. This event increases significantly in prevalence and extent from 20 to 68 hpi, and actin coats strongly correlated with extrusions. In contrast to what has been reported for other intracellular pathogens, actin nucleation on Chlamydia inclusions did not ‘flash’, but rather exhibited moderate depolymerization dynamics. By using small molecule agents to selectively disrupt host signaling pathways involved with actin nucleation, modulate actin polymerization dynamics and also to disable the synthesis and secretion of chlamydial proteins, we further show that host and bacterial proteins are required for actin coat formation. Transient disruption of either host or bacterial signaling pathways resulted in rapid loss of coats in all infected cells and a reduction in extrusion formation. Inhibition of Chlamydia type III secretion also resulted in rapid loss of actin association on inclusions, thus implicating chlamydial effector proteins(s) as being central factors for engaging with host actin nucleating factors, such as formins. In conclusion, our data illuminate the host and bacterial driven process by which a dense actin matrix is dynamically nucleated and maintained on the Chlamydia inclusion. This late stage event is not ubiquitous for all infected cells in a population, and escalates in prevalence and extent throughout the developmental cycle of Chlamydia, culminating with their exit from the host cell by extrusion. The initiation of actin recruitment by Chlamydia appears to be novel, and may serve as an upstream determinant of the extrusion mechanismen_US
dc.rightsCC BY 4.0en_US
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/legalcodeen_US
dc.titleActin recruitment to the Chlamydia inclusion is spatiotemporally regulated by a mechanism that requires host and bacterial factorsen_US
dc.typeArticleen_US
mus.citation.extentfirstpagee46949en_US
mus.citation.issue10en_US
mus.citation.journaltitlePLoS ONEen_US
mus.citation.volume7en_US
mus.identifier.categoryChemical & Material Sciencesen_US
mus.identifier.categoryEngineering & Computer Scienceen_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.identifier.doi10.1371/journal.pone.0046949en_US
mus.relation.collegeCollege of Agricultureen_US
mus.relation.collegeCollege of Engineeringen_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentCell Biology & Neuroscience.en_US
mus.relation.departmentCenter for Biofilm Engineering.en_US
mus.relation.departmentChemical & Biological Engineering.en_US
mus.relation.departmentChemical Engineering.en_US
mus.relation.departmentChemistry & Biochemistry.en_US
mus.relation.departmentGenetics.en_US
mus.relation.departmentMicrobiology & Immunology.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.relation.researchgroupIT Center.en_US
mus.data.thumbpage8en_US


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