Published online ahead of print on 15 June 2009 as doi:10.1099/jmm.0.009936-0
Journal of Medical Microbiology 2009;58:1015.
J Med Microbiol (2009), DOI: 10.1099/jmm.0.009936-0
© 2009 Society for General Microbiology
Bacteroides fragilis signals through TLR2 and not TLR4
Mohammad Alhawi1,
John Stewart2,
Clett Erridge3,
Sheila Patrick4 and
Ian R Poxton2,5
1 King Abdulaziz University, Jeddah, Saudi Arabia;
2 University of Edinburgh;
3 Univesity of Leicester;
4 Queen's University Belfast
5 E-mail: i.r.poxton{at}ed.ac.uk
Received February 2, 2009
Accepted April 9, 2009
Although it is desirable to identify the interactions between endotoxin/ lipopolysaccharide (LPS) and the innate immune mechanism, it is often not possible to isolate these interactions from other cell wall related structures of protein or polysaccharide origin. There is no universally accepted method to extract different LPSs from different bacteria, and their natural state will be influenced by their interactions with the associated molecules in the bacterial outer membrane. It is now believed that toll-like receptor (TLR) 4 is the main signal transducer of classical LPS (i.e. Escherichia coli LPS), while TLR2 is used by certain non-classical LPSs. There are contradictory reports as to whether Bacteroides fragilis LPS, a non-classical LPS, signals primarily through TLR2 or TLR4. This study was designed to address this problem. Different non-purified and purified Bacteroides fragilis LPSs extracted by different methods together with different heat-killed, whole cell populations of B. fragilis were used to elucidate the TLR specificity. All of these B. fragilis preparations showed a significant signalling specificity for TLR2 but not TLR4. This indicates that changing the extraction methods, with or without applying a repurification procedure, and varying the cell populations do not alter the TLR specificity of B. fragilis LPS.
Copyright © 2009 Society for General Microbiology.