Chlamydia interfere with an interaction between the mannose-6-phosphate receptor and sorting nexins to counteract host restriction

Elwell, Cherilyn A.; Czudnochowski, Nadine; von Dollen, John; Johnson, Jeffrey R.; Nakagawa, Rachel; Mirrashidi, Kathleen; Krogan, Nevan J.; Engel, Joanne N.; Rosenberg, Oren S.

doi:10.7554/eLife.22709

Title: Chlamydia interfere with an interaction between the mannose-6-phosphate receptor and sorting nexins to counteract host restriction

Journal Article · 01 March 2017 · eLife

DOI: https://doi.org/10.7554/eLife.22709 · OSTI ID:1629796

^[1];

^[2]; von Dollen, John ^[3]; Johnson, Jeffrey R. ^[3]; Nakagawa, Rachel ^[2]; Mirrashidi, Kathleen ^[2]; Krogan, Nevan J. ^[4]; Engel, Joanne N. ^[5];

^[2]

Univ. of California, San Francisco, CA (United States). Dept. of Medicine; DOE/OSTI
Univ. of California, San Francisco, CA (United States). Dept. of Medicine
Univ. of California, San Francisco, CA (United States). Dept. of Cellular and Molecular Pharmacology
Univ. of California, San Francisco, CA (United States). Dept. of Cellular and Molecular Pharmacology; California Inst. for Quantitative Biosciences, San Francisco, CA (United States). QB3; Gladstone Institutes, San Francisco, CA (United States)
Univ. of California, San Francisco, CA (United States). Dept. of Medicine; Univ. of California, San Francisco, CA (United States). Dept. of Microbiology and Immunology

Chlamydia trachomatis is an obligate intracellular pathogen that resides in a membrane-bound compartment, the inclusion. The bacteria secrete a unique class of proteins, Incs, which insert into the inclusion membrane and modulate the host-bacterium interface. We previously reported that IncE binds specifically to the Sorting Nexin 5 Phox domain (SNX5-PX) and disrupts retromer trafficking. Here, we present the crystal structure of the SNX5-PX:IncE complex, showing IncE bound to a unique and highly conserved hydrophobic groove on SNX5. Mutagenesis of the SNX5-PX:IncE binding surface disrupts a previously unsuspected interaction between SNX5 and the cation-independent mannose-6-phosphate receptor (CI-MPR). Addition of IncE peptide inhibits the interaction of CI-MPR with SNX5. Finally, C. trachomatis infection interferes with the SNX5:CI-MPR interaction, suggesting that IncE and CI-MPR are dependent on the same binding surface on SNX5. Our results provide new insights into retromer assembly and underscore the power of using pathogens to discover disease-related cell biology.

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Research Organization:: Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1629796

Journal Information:: eLife, Journal Name: eLife Vol. 6; ISSN 2050-084X

Publisher:: eLife Sciences Publications, Ltd.Copyright Statement

Country of Publication:: United States

Language:: English

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