Abstract:
: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.
journal_name
Mol Biol Celljournal_title
Molecular biology of the cellauthors
Mojica SA,Hovis KM,Frieman MB,Tran B,Hsia RC,Ravel J,Jenkins-Houk C,Wilson KL,Bavoil PMdoi
10.1091/mbc.E14-11-1530subject
Has Abstractpub_date
2015-05-15 00:00:00pages
1918-34issue
10eissn
1059-1524issn
1939-4586pii
mbc.E14-11-1530journal_volume
26pub_type
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