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Yersinia pestis YrbH is a multifunctional protein required for both 3‐deoxy‐ d ‐ manno ‐oct‐2‐ulosonic acid biosynthesis and biofilm formation
Author(s) -
Tan Li,
Darby Creg
Publication year - 2006
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2006.05265.x
Subject(s) - biofilm , yersinia pestis , biology , biosynthesis , caenorhabditis elegans , isomerase , microbiology and biotechnology , arabinose , biochemistry , bacteria , fermentation , virulence , enzyme , gene , genetics , xylose
Summary Bubonic plague is transmitted by fleas whose feeding is blocked by a Yersinia pestis biofilm in the digestive tract. Y. pestis also block feeding of Caenorhabditis elegans by forming a biofilm on the nematode head, making the nematode an experimentally tractable surrogate for fleas to study plague transmission. Arabinose 5‐phosphate isomerase (API), encoded by Y. pestis yrbH, catalyses the conversion of ribulose 5‐phosphate into arabinose 5‐phosphate (A5P), the first committed step in the 3‐deoxy‐ d ‐ manno ‐oct‐2‐ulosonic acid (Kdo) biosynthesis pathway. Here we show that Y. pestis YrbH is a multifunctional protein required for both Kdo biosynthesis and biofilm formation on C. elegans. The YrbH protein contains four functional components: biofilm‐related region 1 (B1), a sugar isomerase domain (SIS), biofilm‐related region 2 (B2) and a cystathionine β‐synthase domain pair (CBS). B1, SIS and B2 are all required for API function, but any of the three is sufficient for a biofilm‐related function. The CBS domain appears to negatively regulate the biofilm‐related function.