| Modulation of microtubule dynamics by a TIR domain protein from the intracellular pathogen Brucella melitensis. | |
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MedLine Citation:
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PMID: 21692747 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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TIR (Toll/interleukin-1 receptor) domain-containing proteins play a crucial role in innate immunity in eukaryotes. Brucella is a highly infectious intracellular bacterium that encodes a TIR domain protein (TcpB) to subvert host innate immune responses to establish a beneficial niche for pathogenesis. TcpB inhibits NF-κB (nuclear factor κB) activation and pro-inflammatory cytokine secretions mediated by TLR (Toll-like receptor) 2 and TLR4. In the present study, we have demonstrated that TcpB modulates microtubule dynamics by acting as a stabilization factor. TcpB increased the rate of nucleation as well as the polymerization phases of microtubule formation in a similar manner to paclitaxel. TcpB could efficiently inhibit nocodazole- or cold-induced microtubule disassembly. Microtubule stabilization by TcpB is attributed to the BB-loop region of the TIR domain, and a point mutation affected the microtubule stabilization as well as the TLR-suppression properties of TcpB. |
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Authors:
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Girish K Radhakrishnan; Jerome S Harms; Gary A Splitter |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: The Biochemical journal Volume: 439 ISSN: 1470-8728 ISO Abbreviation: Biochem. J. Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-09-15 Completed Date: 2011-11-14 Revised Date: 2013-03-29 |
Medline Journal Info:
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Nlm Unique ID: 2984726R Medline TA: Biochem J Country: England |
Other Details:
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Languages: eng Pagination: 79-83 Citation Subset: IM |
Affiliation:
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Department of Pathobiological Sciences, University of Wisconsin-Madison, Madison, WI 53706, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Bacterial Proteins
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genetics,
metabolism* Brucella melitensis / genetics, metabolism* Microtubules / drug effects, metabolism* Nocodazole / pharmacology Protein Structure, Tertiary Receptors, Interleukin-1 / genetics, metabolism* Toll-Like Receptor 2 / genetics, metabolism Toll-Like Receptor 4 / genetics, metabolism |
| Grant Support | |
ID/Acronym/Agency:
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1R01AI073558/AI/NIAID NIH HHS; R01 AI073558/AI/NIAID NIH HHS; R21 AI088038/AI/NIAID NIH HHS; R21 AI088038/AI/NIAID NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Receptors, Interleukin-1; 0/Toll-Like Receptor 2; 0/Toll-Like Receptor 4; 31430-18-9/Nocodazole |
| Comments/Corrections | |
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