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SINC, a type III secreted protein of Chlamydia psittaci, targets the inner nuclear membrane of infected cells and uninfected neighbors

SINC, a new type III secreted protein of the avian and human pathogen Chlamydia psittaci, uniquely targets the nuclear envelope of C. psittaci–infected cells and uninfected neighboring cells. Digitonin-permeabilization studies of SINC-GFP–transfected HeLa cells indicate that SINC targets the inner n...

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Autores principales: Mojica, Sergio A., Hovis, Kelley M., Frieman, Matthew B., Tran, Bao, Hsia, Ru-ching, Ravel, Jacques, Jenkins-Houk, Clifton, Wilson, Katherine L., Bavoil, Patrik M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4436835/
https://www.ncbi.nlm.nih.gov/pubmed/25788290
http://dx.doi.org/10.1091/mbc.E14-11-1530
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author Mojica, Sergio A.
Hovis, Kelley M.
Frieman, Matthew B.
Tran, Bao
Hsia, Ru-ching
Ravel, Jacques
Jenkins-Houk, Clifton
Wilson, Katherine L.
Bavoil, Patrik M.
author_facet Mojica, Sergio A.
Hovis, Kelley M.
Frieman, Matthew B.
Tran, Bao
Hsia, Ru-ching
Ravel, Jacques
Jenkins-Houk, Clifton
Wilson, Katherine L.
Bavoil, Patrik M.
author_sort Mojica, Sergio A.
collection PubMed
description SINC, a new type III secreted protein of the avian and human pathogen Chlamydia psittaci, uniquely targets the nuclear envelope of C. psittaci–infected cells and uninfected neighboring cells. Digitonin-permeabilization studies of SINC-GFP–transfected HeLa cells indicate that SINC targets the inner nuclear membrane. SINC localization at the nuclear envelope was blocked by importazole, confirming SINC import into the nucleus. Candidate partners were identified by proximity to biotin ligase-fused SINC in HEK293 cells and mass spectrometry (BioID). This strategy identified 22 candidates with high confidence, including the nucleoporin ELYS, lamin B1, and four proteins (emerin, MAN1, LAP1, and LBR) of the inner nuclear membrane, suggesting that SINC interacts with host proteins that control nuclear structure, signaling, chromatin organization, and gene silencing. GFP-SINC association with the native LEM-domain protein emerin, a conserved component of nuclear “lamina” structure, or with a complex containing emerin was confirmed by GFP pull down. Our findings identify SINC as a novel bacterial protein that targets the nuclear envelope with the capability of globally altering nuclear envelope functions in the infected host cell and neighboring uninfected cells. These properties may contribute to the aggressive virulence of C. psittaci.
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spelling pubmed-44368352015-07-30 SINC, a type III secreted protein of Chlamydia psittaci, targets the inner nuclear membrane of infected cells and uninfected neighbors Mojica, Sergio A. Hovis, Kelley M. Frieman, Matthew B. Tran, Bao Hsia, Ru-ching Ravel, Jacques Jenkins-Houk, Clifton Wilson, Katherine L. Bavoil, Patrik M. Mol Biol Cell Articles SINC, a new type III secreted protein of the avian and human pathogen Chlamydia psittaci, uniquely targets the nuclear envelope of C. psittaci–infected cells and uninfected neighboring cells. Digitonin-permeabilization studies of SINC-GFP–transfected HeLa cells indicate that SINC targets the inner nuclear membrane. SINC localization at the nuclear envelope was blocked by importazole, confirming SINC import into the nucleus. Candidate partners were identified by proximity to biotin ligase-fused SINC in HEK293 cells and mass spectrometry (BioID). This strategy identified 22 candidates with high confidence, including the nucleoporin ELYS, lamin B1, and four proteins (emerin, MAN1, LAP1, and LBR) of the inner nuclear membrane, suggesting that SINC interacts with host proteins that control nuclear structure, signaling, chromatin organization, and gene silencing. GFP-SINC association with the native LEM-domain protein emerin, a conserved component of nuclear “lamina” structure, or with a complex containing emerin was confirmed by GFP pull down. Our findings identify SINC as a novel bacterial protein that targets the nuclear envelope with the capability of globally altering nuclear envelope functions in the infected host cell and neighboring uninfected cells. These properties may contribute to the aggressive virulence of C. psittaci. The American Society for Cell Biology 2015-05-15 /pmc/articles/PMC4436835/ /pubmed/25788290 http://dx.doi.org/10.1091/mbc.E14-11-1530 Text en © 2015 Mojica et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.
spellingShingle Articles
Mojica, Sergio A.
Hovis, Kelley M.
Frieman, Matthew B.
Tran, Bao
Hsia, Ru-ching
Ravel, Jacques
Jenkins-Houk, Clifton
Wilson, Katherine L.
Bavoil, Patrik M.
SINC, a type III secreted protein of Chlamydia psittaci, targets the inner nuclear membrane of infected cells and uninfected neighbors
title SINC, a type III secreted protein of Chlamydia psittaci, targets the inner nuclear membrane of infected cells and uninfected neighbors
title_full SINC, a type III secreted protein of Chlamydia psittaci, targets the inner nuclear membrane of infected cells and uninfected neighbors
title_fullStr SINC, a type III secreted protein of Chlamydia psittaci, targets the inner nuclear membrane of infected cells and uninfected neighbors
title_full_unstemmed SINC, a type III secreted protein of Chlamydia psittaci, targets the inner nuclear membrane of infected cells and uninfected neighbors
title_short SINC, a type III secreted protein of Chlamydia psittaci, targets the inner nuclear membrane of infected cells and uninfected neighbors
title_sort sinc, a type iii secreted protein of chlamydia psittaci, targets the inner nuclear membrane of infected cells and uninfected neighbors
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4436835/
https://www.ncbi.nlm.nih.gov/pubmed/25788290
http://dx.doi.org/10.1091/mbc.E14-11-1530
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