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L-Fucose Utilization Provides Campylobacter Jejuni with a Competitive Advantage

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L-Fucose Utilization Provides Campylobacter Jejuni with a Competitive Advantage L-Fucose utilization provides Campylobacter jejuni with a competitive advantage Martin Stahla, Lorna M. Friisb,1, Harald Nothaftb,1, Xin Liuc, Jianjun Lic, Christine M. Szymanskib,2, and Alain Stintzia,2 aOttawa Institute of Systems Biology, Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Ottawa, ON, Canada K1H 8M5; bAlberta Ingenuity Centre for Carbohydrate Science, Department of Biological Sciences, University of Alberta, Edmonton, AB, Canada T6G 2E9; and cInstitute for Biological Sciences, National Research Council, Ottawa, ON, Canada K1A 0R6 Edited* by Pascale Cossart, Institut Pasteur, Paris, France, and approved March 18, 2011 (received for review September 23, 2010) Campylobacter jejuni is a prevalent gastrointestinal pathogen in typically located in terminal positions on the extensively modi- humans and a common commensal of poultry. When colonizing fied mucin glycoproteins (13, 15). These fucosylated glycans coating its hosts, C. jejuni comes into contact with intestinal carbohydrates, the mucins are known to act as adherence targets for many in- including L-fucose, released from mucin glycoproteins. Several testinal bacteria [including C. jejuni (16)], potentially contributing strains of C. jejuni possess a genomic island (cj0480c–cj0490) that to the function of mucin as a barrier to intestinal pathogens (17). is up-regulated in the presence of both L-fucose and mucin and Fucose monomers and fucosylated glycans can serve as a chemo- allows for the utilization of L-fucose as a substrate for growth. attractant (18) and carbon source for many species within the gut. Strains possessing this genomic island show increased growth in Being so common within the intestine, fucose is an integral part of the presence of L-fucose and mutation of cj0481, cj0486, and the intestinal ecology. For example, the presence of the ubiqui- cj0487 results in the loss of the ability to grow on this substrate. tous commensal Bacteroides thetaiotaomicron in the gut triggers Furthermore, mutants in the putative fucose permease (cj0486)are an increase in the production of fucosylated mucins by the in- deficient in fucose uptake and demonstrate a competitive disadvan- testinal epithelium, which is important for gut maturation (19). tage when colonizing the piglet model of human disease, which is These bacteria then secrete fucosidases to release fucose residues not paralleled in the colonization of poultry. This identifies a previ- from the oligosaccharides and transport the sugar into the cell ously unrecorded metabolic pathway in select strains of C. jejuni for metabolism and surface presentation (12, 20). Even bacteria associated with a virulent lifestyle. such as Escherichia coli, which do not express fucosidases, use this same pathway for fucose transport (21) and colonization of the pathogenesis | metabolism | gut | mucus bovine rectum (22). Despite the lack of an annotated fucose metabolic pathway, he most common cause of gastroenteritis in the developed fucose has long been described as influencing the behavior of C. Tworld, Campylobacter jejuni is a frequent cause of pediatric jejuni. In 1988, Hugdahl et al. reported C. jejuni chemotaxis to- diarrheal episodes within developing countries that can last from ward L-fucose, as well as toward intact mucins, which would have a few days to several weeks (1). The symptoms vary from mild, included fucosylated glycans (18). In addition, fucosylated milk watery diarrhea to bloody diarrhea with fever and severe abdom- oligosaccharides were used in an elegant experiment to com- inal pain (2). The disease usually resolves itself relatively quickly, petitively inhibit the specific attachment of C. jejuni to intestinal but autoimmune reactions to the infection can lead to post- H-antigens (23). More recently, Korolik and colleagues have infectious sequelae, such as Guillain-Barré syndrome and reactive made use of glycan microarrays to demonstrate increased C. arthritis (2). jejuni adherence to fucosylated glycans, such as those found on When colonizing its host (whether commensally in poultry and mucin and cell surfaces (16), structures that were suggested to be other animals, or pathogenically in humans), C. jejuni must es- significant factors in the ability of C. jejuni to closely adhere to tablish itself within the mucus layer of the intestinal epithelium (3, the cell surface and invade intestinal epithelial cells. 4). Byrne et al. (5) recently showed that the mucus layer originating This study is unique in demonstrating the uptake and utilization from humans or chickens influences the virulence of C. jejuni and of L-fucose by certain strains of C. jejuni via a previously unde- might differentially control the virulence versus commensalism scribed pathway not found in other enteric bacteria. We further equilibrium. However, it remains unknown which specific com- demonstrate how L-fucose transport provides a distinct competi- ponents of the mucus layer contribute to this change in phenotype. tive advantage in the pathogenesis model that is not found during C. jejuni lacks many of the pathways for nutrient metabolism commensal growth. used by other pathogens and the normal intestinal microbiota. Results For example, several key enzymes within the glycolytic pathway, the Entner-Doudoroff pathway, and the pentose phosphate Fucose Up-Regulates Expression of Genes Linked to Fucose Use. pathway are absent (6, 7), and it has generally been assumed that Microarray experiments were used to assemble a transcriptomic fi C. jejuni α C. jejuni is unable to use any form of carbohydrate as a substrate pro le of NCTC 11168 during growth in MEM medium for growth. Instead, C. jejuni relies on the use of amino acids and citric acid cycle intermediates as carbon sources (8). The amino acid metabolic pathways that allow C. jejuni to use serine (9), Author contributions: M.S., L.M.F., H.N., J.L., C.M.S., and A.S. designed research; M.S., L.M.F., H.N., X.L., and J.L. performed research; M.S., L.M.F., H.N., X.L., J.L., C.M.S., and A.S. analyzed aspartate, glutamate (10), and proline (11) have all been studied data; and M.S., L.M.F., H.N., C.M.S., and A.S. wrote the paper. C. jejuni – in depth. Additionally, some strains, including 81 176, The authors declare no conflict of interest. can metabolize glutamine and asparagine (8). However, and in *This Direct Submission article had a prearranged editor. contrast to the generally accepted paradigm, we demonstrate in C. jejuni Data deposition: The microarray data have been deposited in the National Center for this study that certain strains of contain a unique path- Biotechnology Information Geo Omnibus database. way for the uptake and metabolism of the sugar L-fucose, which is 1L.M.F. and H.N. contributed equally to this work. obtained from the host during colonization of the intestine. 2To whom correspondence may be addressed. E-mail: [email protected] or cszymans@ The importance of fucose to the intestinal microflora is well ualberta.ca. – established (12 14). Fucosylated glycans are common within the This article contains supporting information online at www.pnas.org/lookup/suppl/doi:10. digestive tract, where they are found on cell surfaces and are 1073/pnas.1014125108/-/DCSupplemental. 7194–7199 | PNAS | April 26, 2011 | vol. 108 | no. 17 www.pnas.org/cgi/doi/10.1073/pnas.1014125108 Downloaded by guest on September 28, 2021 supplemented with 25 mM L-fucose. This process led to the tator superfamily (MFS) transporter, but does not contain these identification of 74 up-regulated genes, and 52 down-regulated conserved residues or a significant degree of sequence similarity, genes (Table S1). The most notable change from the list of up- suggesting it does not serve as a second L-fucose transporter. 3 regulated genes was an operon between cj0481 and cj0490, which Active transport of L-fucose by C. jejuni was confirmed in H-L- exhibited six- to -ninefold up-regulation (Table S1). The putative fucose uptake experiments. In wild-type cells grown in the absence regulator cj0480c did not show any significant change in expres- of L-fucose, the initial uptake was approximately threefold lower sion. Similarly, a microarray study of C. jejuni grown in MEMα than in cells grown in the presence of L-fucose (Fig. 2A), consistent medium supplemented with 2 mg/mL porcine gastric mucin also with E. coli (Fig. 2B), indicating that [3H]-fucose transport is in- revealed significant up-regulation (two- to fourfold) of the genes ducible by its substrate. Insertion mutants were subsequently cj0481 to cj0490 (Table S2). constructed into C. jejuni genes cj0481, cj0483, cj0486,andcj0487. The Δcj0486 mutant (Fig. 2) showed no significant fucose transport fi Identi cation of a Genomic Island Required for Fucose Utilization. (< 0.2 pmols·min·109 cfu), demonstrating that Cj0486 is an es- cj0480c cj0490 fi None of the genes to have any con rmed func- sential component of the active L-fucose assimilation pathway in C. tion, but cj0486 bears homology to the fucose permease gene jejuni cj0481 cj0483 cj0487 fucP fi . The mutants , , and all transport L-fu- ( ) of other bacteria (21). This operon has been identi ed cose at levels of the uniduced wild-type strain independent of the previously in RM1221 and NCTC 11168 as a genomic island presence of fucose in the growth medium. This finding indicates spanning from cj0480c to cj0490 (24) and nestled in between the rpoC fusA that fucose transport is still occurring but not inducible in these genes and (Fig. S1) of some strains. Notably, this re- strains (Fig. 2A). Complementation of cj0486 and cj0487 showed gion is absent in strain 81–176. Although this region is not uni- partial, but significant, restoration of L-fucose uptake. Quantitative versally conserved within strains of C. jejuni, it has been linked to RT-PCR analysis demonstrated that cj0486 and cj0487 are ex- C. jejuni hyper-invasiveness (25, 26).
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