The vitamin riboflavin and its derivative lumichrome activate the LasR bacterial quorum-sensing receptor.
The vitamin riboflavin and its derivative lumichrome activate the LasR bacterial quorum-sensing receptor.
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DOI:
10.1094/mpmi-21-9-1184
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发表时间:
2008-09
期刊:
影响因子:
--
通讯作者:
Phillips DA
中科院分区:
文献类型:
--
作者:
Rajamani S;Bauer WD;Robinson JB;Farrow JM 3rd;Pesci EC;Teplitski M;Gao M;Sayre RT;Phillips DA
Many bacteria use quorum sensing (QS) as an intercellular signaling mechanism to regulate gene expression in local populations. Plant and algal hosts, in turn, secrete compounds that mimic bacterial QS signals, allowing these hosts to manipulate QS-regulated gene expression in bacteria. Lumichrome, a derivative of the vitamin riboflavin, was purified and chemically identified from culture filtrates of the alga Chlamydomonas as a QS signal-mimic compound capable of stimulating the Pseudomonas aeruginosa LasR QS receptor. LasR normally recognizes the N-acyl homoserine lactone (AHL) signal, N-3-oxo-dodecanoyl homoserine lactone (3-oxo-C12-HSL). Authentic lumichrome and riboflavin stimulated the LasR receptor in bioassays, and lumichrome activated LasR in gel shift experiments. Amino acid substitutions in LasR residues required for AHL binding altered responses to both AHLs and lumichrome/riboflavin. These results and docking studies indicate that the AHL binding pocket of LasR recognizes both AHLs and the structurally dissimilar lumichrome/riboflavin. Bacteria, plants and algae commonly secrete riboflavin and/or lumichrome, raising the possibility that these compounds could serve as either QS signals or as interkingdom signal-mimics capable of manipulating QS in bacteria with a LasR-like receptor.