Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/105133
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Type: Journal article
Title: Mechanism of bacterial interference with TLR4 signaling by brucella toll/interleukin-1 receptor domain-containing protein TcpB
Author: Alaidarous, M.
Ve, T.
Casey, L.
Valkov, E.
Ericsson, D.
Ullah, M.
Schembri, M.
Mansell, A.
Sweet, M.
Kobe, B.
Citation: Journal of Biological Chemistry, 2014; 289(2):654-668
Publisher: American Society for Biochemistry and Molecular Biology Inc.
Issue Date: 2014
ISSN: 0021-9258
1083-351X
Statement of
Responsibility: 
Mohammed Alaidarous, Thomas Ve, Lachlan W. Casey, Eugene Valkov, Daniel J. Ericsson, M. Obayed Ullah, Mark A. Schembri, Ashley Mansell, Matthew J. Sweet, and Bostjan Kobe
Abstract: Background: TcpB is a TIR domain-containing protein form Brucella. Results: TcpB interacts with the host Toll-like receptor and adaptors, and its structure reveals a dimer essential for activity. Conclusion: TcpB forms a nonfunctional complex with host molecules, thus suppressing signaling. Significance: The work explains the structural and functional basis of immune suppression by the protein TcpB from a pathogenic bacterium.
Keywords: Toll-Like Receptor 4; Myeloid Differentiation Factor 88
Rights: © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
DOI: 10.1074/jbc.M113.523274
Grant ID: http://purl.org/au-research/grants/nhmrc/1003326
http://purl.org/au-research/grants/arc/FT100100662
http://purl.org/au-research/grants/arc/FT100100657
http://purl.org/au-research/grants/nhmrc/1003470
http://purl.org/au-research/grants/nhmrc/1003325
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