| Literature DB >> 26118995 |
Kathleen M Mirrashidi1, Cherilyn A Elwell1, Erik Verschueren2, Jeffrey R Johnson2, Andrew Frando1, John Von Dollen2, Oren Rosenberg1, Natali Gulbahce2, Gwendolyn Jang2, Tasha Johnson2, Stefanie Jäger2, Anusha M Gopalakrishnan3, Jessica Sherry1, Joe Dan Dunn3, Andrew Olive4, Bennett Penn1, Michael Shales5, Jeffery S Cox6, Michael N Starnbach4, Isabelle Derre7, Raphael Valdivia3, Nevan J Krogan8, Joanne Engel9.
Abstract
Chlamydia trachomatis is a leading cause of genital and ocular infections for which no vaccine exists. Upon entry into host cells, C. trachomatis resides within a membrane-bound compartment—the inclusion—and secretes inclusion membrane proteins (Incs) that are thought to modulate the host-bacterium interface. To expand our understanding of Inc function(s), we subjected putative C. trachomatis Incs to affinity purification-mass spectroscopy (AP-MS). We identified Inc-human interactions for 38/58 Incs with enrichment in host processes consistent with Chlamydia's intracellular life cycle. There is significant overlap between Inc targets and viral proteins, suggesting common pathogenic mechanisms among obligate intracellular microbes. IncE binds to sorting nexins (SNXs) 5/6, components of the retromer, which relocalizes SNX5/6 to the inclusion membrane and augments inclusion membrane tubulation. Depletion of retromer components enhances progeny production, revealing that retromer restricts Chlamydia infection. This study demonstrates the value of proteomics in unveiling host-pathogen interactions in genetically challenging microbes.Entities:
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Year: 2015 PMID： 26118995 PMCID： PMC4540348 DOI： 10.1016/j.chom.2015.06.004
Source DB: PubMed Journal: Cell Host Microbe ISSN： 1931-3128 Impact factor: 21.023