UDP-galactofuranose Precursor Required for Formation of the Lipopolysaccharide O Antigen of Klebsiella pneumoniae Serotype O1 Is Synthesized by the Product of the rfbDKPO1 Gene

Koplin, R; Brisson, Jean‐Robert; Whitfield, Chris

doi:10.1074/jbc.272.7.4121

Cited by 123 publications

(113 citation statements)

References 71 publications

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“…From the 1 H spectrum J P␤, H1 was found to be 7.6 Hz, and J P␤, H2 was 2.8 Hz. The 1 H, 13 C chemical shifts for the UDP moiety were similar to those previously reported (19). These results provided the evidence that the structure of the WbpA enzyme-substrate reaction product is UDP-D-GlcNAcA.…”

Section: Resultssupporting

confidence: 78%

Biochemical Characterization of WbpA, a UDP-N-acetyl-d-glucosamine 6-Dehydrogenase Involved in O-antigen Biosynthesis in Pseudomonas aeruginosa PAO1

Miller

Wenzel

Daniels

et al. 2004

Journal of Biological Chemistry

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Section: Resultssupporting

confidence: 78%

Biochemical Characterization of WbpA, a UDP-N-acetyl-d-glucosamine 6-Dehydrogenase Involved in O-antigen Biosynthesis in Pseudomonas aeruginosa PAO1

Miller

Wenzel

Daniels

et al. 2004

Journal of Biological Chemistry

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“…A BLAST analysis of these SNPs against the Virulence Factors Database revealed three genes of particular interest: (i) fliK, coding for a flagellar hook-length control protein (41), (ii) sthD, a gene coding for a fimbrial outer membrane usher protein (42), and (iii) rfbD, coding for a UDP-galactopyranose mutase precursor involved in the synthesis of the O antigen of the lipopolysaccharide (LPS). All three proteins are virulence determinants in Salmonella (43)(44)(45)(46). WGS has already proved its usefulness for elucidating the evolutionary diversity of large populations of bacterial isolates (11,47,48).…”

Section: Discussionmentioning

confidence: 99%

Differential Single Nucleotide Polymorphism-Based Analysis of an Outbreak Caused by Salmonella enterica Serovar Manhattan Reveals Epidemiological Details Missed by Standard Pulsed-Field Gel Electrophoresis

et al. 2015

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We retrospectively analyzed a rare Salmonella enterica serovar Manhattan outbreak that occurred in Italy in 2009 to evaluate the potential of new genomic tools based on differential single nucleotide polymorphism (SNP) analysis in comparison with the gold standard genotyping method, pulsed-field gel electrophoresis. A total of 39 isolates were analyzed from patients (n ‫؍‬ 15) and food, feed, animal, and environmental sources (n ‫؍‬ 24), resulting in five different pulsed-field gel electrophoresis (PFGE) profiles. Isolates epidemiologically related to the outbreak clustered within the same pulsotype, SXB_BS.0003, without any further differentiation. Thirty-three isolates were considered for genomic analysis based on different sets of SNPs, core, synonymous, nonsynonymous, as well as SNPs in different codon positions, by Bayesian and maximum likelihood algorithms. Trees generated from core and nonsynonymous SNPs, as well as SNPs at the second and first plus second codon positions detailed four distinct groups of isolates within the outbreak pulsotype, discriminating outbreak-related isolates of human and food origins. Conversely, the trees derived from synonymous and third-codon-position SNPs clustered food and human isolates together, indicating that all outbreak-related isolates constituted a single clone, which was in line with the epidemiological evidence. Further experiments are in place to extend this approach within our regional enteropathogen surveillance system. Salmonellosis is a major food-borne disease worldwide, with an estimated 93.8 million cases occurring each year, resulting in 155,000 deaths (1). The European Union summary report on trends and sources of zoonoses, zoonotic agents and food-borne outbreaks (2) indicated that nontyphoid salmonellosis was the second most reported food-borne zoonosis in Europe in 2012, trailing only behind Campylobacter jejuni infection. The 2012 overall notification rate for human salmonellosis in the European Union (EU) was 22.2 episodes per 100,000 population, for a total of 91,034 confirmed cases, with hospitalization and mortality rates of 45.1% and 0.14%, respectively. The highest proportions of Salmonella-positive foodstuff samples were reported for fresh turkey, poultry, and pork at 4.4%, 4.1%, and 0.7%, respectively (2). In order to manage this food-borne infection and to limit its health and economic burdens, surveillance programs have developed and implemented DNA-based subtyping methods to identify outbreaks in a timely manner and to trace infections back to their food sources. Over the past decades, the two most intensively used protocols for Salmonella subtyping have been pulsed-field gel electrophoresis (PFGE) and multilocus variable-number tandemrepeat analysis (MLVA) (3). Unfortunately, these methods rely on just few features of the entire bacterial genome (rare restriction sites for PFGE or few polymorphic loci for MLVA) to assess the relatedness of different isolates. During epidemiological investigations of food-borne outbreaks, this limitation mi...

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“…O-PSs isolated from these strains contain a mixture of molecules carrying only D-galactan I and others comprising short chains of D-galactan I capped by the additional antigen (73,74). The activated precursors for D-galactan I biosynthesis are UDPgalactopyranose and UDP-galactofuranose (75). Synthesis proceeds on a Und-PP-GlcNAc acceptor formed by WecA (28,52,163), and it requires three dedicated galactosyltransferases (WbbM, WbbN, and WbbO), whose precise contributions are only partially resolved.…”

Section: O-ps Export Using Group C and D Nbds Lacking An Extended C Tmentioning

confidence: 99%

ABC Transporters Involved in Export of Cell Surface Glycoconjugates

Cuthbertson

Kos

Whitfield

2010

Microbiol Mol Biol Rev

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SUMMARY Complex glycoconjugates play critical roles in the biology of microorganisms. Despite the remarkable diversity in glycan structures and the bacteria that produce them, conserved themes are evident in the biosynthesis-export pathways. One of the primary pathways involves representatives of the ATP-binding cassette (ABC) transporter superfamily. These proteins are responsible for the export of a wide variety of cell surface oligo- and polysaccharides in both Gram-positive and Gram-negative bacteria. Recent investigations of the structure and function of ABC transporters involved in the export of lipopolysaccharide O antigens have revealed two fundamentally different strategies for coupling glycan polymerization to export. These mechanisms are distinguished by the presence (or absence) of characteristic nonreducing terminal modifications on the export substrates, which serve as chain termination and/or export signals, and by the presence (or absence) of a discrete substrate-binding domain in the nucleotide-binding domain polypeptide of the ABC transporter. A bioinformatic survey examining ABC exporters from known oligo- and polysaccharide biosynthesis loci identifies conserved nucleotide-binding domain protein families that correlate well with themes in the structures and assembly of glycans. The familial relationships among the ABC exporters generate hypotheses concerning the biosynthesis of structurally diverse oligo- and polysaccharides, which play important roles in the biology of bacteria with different lifestyles.

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UDP-galactofuranose Precursor Required for Formation of the Lipopolysaccharide O Antigen of Klebsiella pneumoniae Serotype O1 Is Synthesized by the Product of the rfbDKPO1 Gene

Cited by 123 publications

References 71 publications

Biochemical Characterization of WbpA, a UDP-N-acetyl-d-glucosamine 6-Dehydrogenase Involved in O-antigen Biosynthesis in Pseudomonas aeruginosa PAO1

Biochemical Characterization of WbpA, a UDP-N-acetyl-d-glucosamine 6-Dehydrogenase Involved in O-antigen Biosynthesis in Pseudomonas aeruginosa PAO1

Differential Single Nucleotide Polymorphism-Based Analysis of an Outbreak Caused by Salmonella enterica Serovar Manhattan Reveals Epidemiological Details Missed by Standard Pulsed-Field Gel Electrophoresis

ABC Transporters Involved in Export of Cell Surface Glycoconjugates

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