Relationships of capsular polysaccharides belonging to Campylobacter jejuni HS1 serotype complex

Monteiro, Mário A.; Chen, Yuhan; Ma, Zuchao; Ewing, Cheryl P.; Nor, Nooraisyah Mohamad; Omari, Eman; Song, Ellen; Gabryelski, Pawel; Guerry, Patricia; Poly, Frédéric

doi:10.1371/journal.pone.0247305

Cited by 4 publications

(4 citation statements)

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“…An important virulence factor for C. jejuni infections is the capsular polysaccharide (CPS), which coats the exterior cell surface and mediates the interactions of the bacterium with its host . The CPSs vary in sugar composition and linkage within the various strains of the bacterium.…”

Section: Introductionmentioning

confidence: 99%

“…At least 12 CPS structures from various strains of C. jejuni have been reported, and nine of them contain heptose moieties with at least 13 different structural variations. − Bioinformatic analyses and other experimental data suggest that all of the known heptose variations in C. jejuni likely originate from GDP- d -glycero-α- d -manno-heptose ( 3 ) .…”

Section: Introductionmentioning

confidence: 99%

“…8 An important virulence factor for C. jejuni infections is the capsular polysaccharide (CPS), which coats the exterior cell surface and mediates the interactions of the bacterium with its host. 9 The CPSs vary in sugar composition and linkage within the various strains of the bacterium. The repeating structures of the CPSs in C. jejuni NCTC 11168 (serotype HS:2) and C. jejuni 81-176 (serotype HS:23/36) are presented in Figure 1.…”

Section: ■ Introductionmentioning

confidence: 99%

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Reaction Mechanism and Three-Dimensional Structure of GDP-d-glycero-α-d-manno-heptose 4,6-Dehydratase from Campylobacter jejuni

et al. 2022

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Campylobacter jejuni is a human pathogen and a leading cause of food poisoning in the United States and Europe. Surrounding the outside of the bacterium is a carbohydrate coat known as the capsular polysaccharide. Various strains of C. jejuni have different sequences of unusual sugars and an assortment of decorations. Many of the serotypes have heptoses with differing stereochemical arrangements at C2 through C6. One of the many common modifications is a 6-deoxy-heptose that is formed by dehydration of GDP-d-glycero-α-d-manno-heptose to GDP-6-deoxy-4-keto-d-lyxo-heptose via the action of the enzyme GDP-d-glycero-α-d-manno-heptose 4,6-dehydratase. Herein, we report the biochemical and structural characterization of this enzyme from C. jejuni 81-176 (serotype HS:23/36). The enzyme was purified to homogeneity, and its three-dimensional structure was determined to a resolution of 2.1 Å. Kinetic analyses suggest that the reaction mechanism proceeds through the formation of a 4-keto intermediate followed by the loss of water from C5/C6. Based on the three-dimensional structure, it is proposed that oxidation of C4 is assisted by proton transfer from the hydroxyl group to the phenolate of Tyr-159 and hydride transfer to the tightly bound NAD+ in the active site. Elimination of water at C5/C6 is most likely assisted by abstraction of the proton at C5 by Glu-136 and subsequent proton transfer to the hydroxyl at C6 via Ser-134 and Tyr-159. A bioinformatic analysis identified 19 additional 4,6-dehydratases from serotyped strains of C. jejuni that are 89–98% identical in the amino acid sequence, indicating that each of these strains should contain a 6-deoxy-heptose within their capsular polysaccharides.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: ■ Introductionmentioning

confidence: 99%

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Reaction Mechanism and Three-Dimensional Structure of GDP-d-glycero-α-d-manno-heptose 4,6-Dehydratase from Campylobacter jejuni

et al. 2022

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“…The capsular polysaccharide (CPS) of C. jejuni forms an external layer on the cell surface, that contributes to C. jejuni virulence and immune evasion [ 71 ]. Indeed, an isogenic mutation in the kpsM gene, encoding a component of an ABC transporter involved in capsule biosynthesis, resulted in reduced adhesion to and invasion of human intestinal epithelial cells, reduced diarrhoea in a ferret model of disease [ 72 ], and impaired colonisation in a mouse model of infection [ 73 ].…”

Section: Introductionmentioning

confidence: 99%

Campylobacter jejuni virulence factors: update on emerging issues and trends

Tikhomirova,

McNabb,

Petterlin

et al. 2024

J Biomed Sci

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Campylobacter jejuni is a very common cause of gastroenteritis, and is frequently transmitted to humans through contaminated food products or water. Importantly, C. jejuni infections have a range of short- and long-term sequelae such as irritable bowel syndrome and Guillain Barre syndrome. C. jejuni triggers disease by employing a range of molecular strategies which enable it to colonise the gut, invade the epithelium, persist intracellularly and avoid detection by the host immune response. The objective of this review is to explore and summarise recent advances in the understanding of the C. jejuni molecular factors involved in colonisation, invasion of cells, collective quorum sensing-mediated behaviours and persistence. Understanding the mechanisms that underpin the pathogenicity of C. jejuni will enable future development of effective preventative approaches and vaccines against this pathogen.

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Consortium of Lactobacillus crispatus 2029 and Ligilactobacillus salivarius 7247 Strains Shows In Vitro Bactericidal Effect on Campylobacter jejuni and, in Combination with Prebiotic, Protects Against Intestinal Barrier Dysfunction

Abramov,

Kosarev,

Machulin

et al. 2024

Antibiotics

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Background/Objectives: Campylobacter jejuni (CJ) is the etiological agent of the world’s most common intestinal infectious food-borne disease, ranging from mild symptoms to fatal outcomes. The development of innovative synbiotics that inhibit the adhesion and reproduction of multidrug-resistant (MDR) CJ in animals and humans, thereby preserving intestinal homeostasis, is relevant. We have created a synbiotic based on the consortium of Lactobacillus crispatus 2029 (LC2029), Ligilactobacillus salivarius 7247 (LS7247), and a mannan-rich prebiotic (Actigen®). The purpose of this work was to study the in vitro anti-adhesive and antagonistic activities of the created synbiotic against MDR CJ strains, along with its role in preventing intestinal barrier dysfunction, which disrupts intestinal homeostasis. Methods: A complex of microbiological, immunological, and molecular biological methods was used. The ability of the LC2029 and LS7247 consortium to promote intestinal homeostasis in vitro was assessed by the effectiveness of controlling CJ-induced TLR4 activation, secretion of pro-inflammatory cytokines, development of intestinal barrier dysfunction, and production of intestinal alkaline phosphatase (IAP). Results: All MDR CJ strains showed marked adhesion to human Caco-2, pig IPEC-J2, chicken CPCE, and bovine BPCE enterocytes. For the first time, we found that the prebiotic and cell-free culture supernatant (CFS) from the consortium of LC2029 and LS7247 strains exhibit an additive effect in inhibiting the adhesion of MDR strains of CJ to human and animal enterocytes. CFS from the LC2029 and LS7247 consortium increased the permeability of the outer and inner membranes of CJ cells, which led to extracellular leakage of ATP and provided access to the peptidoglycan of the pathogen for the peptidoglycan-degrading bacteriocins nisin and enterolysin A produced by LS7247. The LC2029 and LS7247 consortium showed a bactericidal effect on CJ strains. Co-cultivation of the consortium with CJ strains resulted in a decrease in the viability of the pathogen by 6 log. CFS from the LC2029 and LS7247 consortium prevented the growth of CJ-induced TLR4 mRNA expression in enterocytes. The LC2029 and LS7247 consortium inhibited a CJ-induced increase in IL-8 and TNF-α production in enterocytes, prevented CJ-induced intestinal barrier dysfunction, maintained the transepithelial electrical resistance of the enterocyte monolayers, and prevented an increase in intestinal paracellular permeability and zonulin secretion. CFS from the consortium stimulated IAP mRNA expression in enterocytes. The LC2029 and LS7247 consortium and the prebiotic Actigen represent a new synergistic synbiotic with anti-CJ properties that prevents intestinal barrier dysfunction and preserves intestinal homeostasis. Conclusions: These data highlight the potential of using a synergistic synbiotic as a preventive strategy for creating feed additives and functional nutrition products based on it to combat the prevalence of campylobacteriosis caused by MDR strains in animals and humans.

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Relationships of capsular polysaccharides belonging to Campylobacter jejuni HS1 serotype complex

Cited by 4 publications

References 34 publications

Reaction Mechanism and Three-Dimensional Structure of GDP-d-glycero-α-d-manno-heptose 4,6-Dehydratase from Campylobacter jejuni

Reaction Mechanism and Three-Dimensional Structure of GDP-d-glycero-α-d-manno-heptose 4,6-Dehydratase from Campylobacter jejuni

Campylobacter jejuni virulence factors: update on emerging issues and trends

Consortium of Lactobacillus crispatus 2029 and Ligilactobacillus salivarius 7247 Strains Shows In Vitro Bactericidal Effect on Campylobacter jejuni and, in Combination with Prebiotic, Protects Against Intestinal Barrier Dysfunction

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