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Genetic and biochemical analyses of the Pseudomonas aeruginosa Psl exopolysaccharide reveal overlapping roles for polysaccharide synthesis enzymes in Psl and LPS production
Author(s) -
Byrd Matthew S.,
Sadovskaya Irina,
Vinogradov Evgueny,
Lu Haiping,
Sprinkle April B.,
Richardson Stephen H.,
Ma Luyan,
Ralston Brad,
Parsek Matthew R.,
Anderson Erin M.,
Lam Joseph S.,
Wozniak Daniel J.
Publication year - 2009
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.1365-2958.2009.06795.x
Subject(s) - psl , biology , rhamnose , complementation , polysaccharide , mannose , biofilm , mutant , gene , microbiology and biotechnology , biochemistry , genetics , bacteria , geometry , mathematics
Summary Exopolysaccharides contribute significantly to attachment and biofilm formation in the opportunisitc pathogen Pseudomonas aeruginosa . The Psl polysaccharide, which is synthesized by the p olysaccharide s ynthesis l ocus ( psl ), is required for biofilm formation in non‐mucoid strains that do not rely on alginate as the principal biofilm polysaccharide. In‐frame deletion and complementation studies of individual psl genes revealed that 11 psl genes, pslACDEFGHIJKL , are required for Psl production and surface attachment. We also present the first structural analysis of the psl ‐dependent polysaccharide, which consists of a repeating pentasaccharide containing d ‐mannose, d ‐glucose and l ‐rhamnose:In addition, we identified the sugar nucleotide precursors involved in Psl generation and demonstrated the requirement for GDP‐ d ‐mannose, UDP‐ d ‐glucose and dTDP‐ l ‐rhamnose in Psl production and surface attachment. Finally, genetic analyses revealed that wbpW restored Psl production in a pslB mutant and pslB promoted A‐band LPS synthesis in a wbpW mutant, indicating functional redundancy and overlapping roles for these two enzymes. The structural and genetic data presented here provide a basis for further investigation of the Psl proteins and potential roles for Psl in the biology and pathogenesis of P. aeruginosa .