Altered Linkage of Hydroxyacyl Chains in Lipid A of Campylobacter jejuni Reduces TLR4 Activation and Antimicrobial Resistance

Mourik, Andries van; Steeghs, Liana; Laar, Jacoline van; Meiring, Hugo D.; Hamstra, Hendrik-Jan; Putten, Jos P. M. van; Wösten, Marc M. S. M.

doi:10.1074/jbc.m110.102061

Cited by 51 publications

(52 citation statements)

References 45 publications

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“…Whereas PmrA-dependent LPS modifications can reduce the risk of Salmonella detection by the Toll-like receptor-4 in a mammalian host (15,45), its role in ssrB repression may reduce expression of Spi/Ssa-secreted effectors that dampen the host immune response (46,47).…”

Section: Discussionmentioning

confidence: 99%

The lipopolysaccharide modification regulator PmrA limitsSalmonellavirulence by repressing the type three-secretion system Spi/Ssa

Choi

Groisman

2013

Proc. Natl. Acad. Sci. U.S.A.

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The regulatory protein PmrA controls expression of lipopolysaccharide (LPS) modification genes in Salmonella enterica serovar Typhimurium, the etiologic agent of human gastroenteritis and murine typhoid fever. PmrA-dependent LPS modifications confer resistance to serum, Fe 3+ , and several antimicrobial peptides, suggesting that the pmrA gene is required for Salmonella virulence. We now report that, surprisingly, a pmrA null mutant is actually hypervirulent when inoculated i.p. into C3H/HeN mice. We establish that the PmrA protein binds to the promoter and represses transcription of ssrB , a virulence regulatory gene required for expression of the Spi/Ssa type three-secretion system inside macrophages. The pmrA mutant displayed heightened expression of SsrB-dependent genes and faster Spi/Ssa-dependent macrophage killing than wild-type Salmonella . A mutation in the ssrB promoter that abolished repression by the PmrA protein rendered Salmonella as hypervirulent as the pmrA null mutant. The antivirulence function of the PmrA protein may limit the acute phase of Salmonella infection, thereby enhancing pathogen persistence in host tissues.

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Section: Discussionmentioning

confidence: 99%

The lipopolysaccharide modification regulator PmrA limitsSalmonellavirulence by repressing the type three-secretion system Spi/Ssa

Choi

Groisman

2013

Proc. Natl. Acad. Sci. U.S.A.

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“…C. jejuni can adapt to its host by modification of its LOS, flagella and capsule for instance [49]. Hereby, C. jejuni is able to impact TLR-4 activation and enhance antimicrobial resistance [50].…”

Section: Discussionmentioning

confidence: 99%

Campylobacter jejuniinduces extra-intestinal immune responses via toll-like-receptor-4 signaling in conventional IL-10 deficient mice with chronic colitis

Otto¹,

Haag²,

Fischer³

et al. 2012

European Journal of Microbiology and Immunology

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“…61 Inactivation of the genes responsible for forming this amide linkage rendered the mutant C. jejuni more susceptible to polymyxins B and E as well as to the chicken host defense peptide cathelicidin-1. 61 Similarly, masking the anionic phosphate moieties of lipid A with phosphoethanolamine reduces sensitivity to polymyxin B. 62 Taking advantage of this resistance, polymyxin-supplemented media have often been used for the selective isolation of C. jejuni.…”

Section: Polymyxinmentioning

confidence: 99%

“…36 However, certain strains of C. jejuni are relatively insensitive to polymyxins due to modifications of the lipooligosaccharide structure. 61 The hydroxylipid chains of the lipid A in resistant strains are attached to the sugar moiety through an amide linkage instead of the more common ester linkage. 61 Inactivation of the genes responsible for forming this amide linkage rendered the mutant C. jejuni more susceptible to polymyxins B and E as well as to the chicken host defense peptide cathelicidin-1.…”

Section: Polymyxinmentioning

confidence: 99%

“…61 The hydroxylipid chains of the lipid A in resistant strains are attached to the sugar moiety through an amide linkage instead of the more common ester linkage. 61 Inactivation of the genes responsible for forming this amide linkage rendered the mutant C. jejuni more susceptible to polymyxins B and E as well as to the chicken host defense peptide cathelicidin-1. 61 Similarly, masking the anionic phosphate moieties of lipid A with phosphoethanolamine reduces sensitivity to polymyxin B.…”

Section: Polymyxinmentioning

confidence: 99%

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Characterization of bacterial antimicrobial peptides active against Campylobacter jejuni

Lohans

Belkum

et al. 2015

Can. J. Chem.

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Abstract:Campylobacter jejuni is one of the major causes of food poisoning, often resulting from the consumption of improperly cooked poultry products. The emergence of C. jejuni strains resistant to conventional antibiotics necessitates the evaluation of other possible treatments or preventative measures to minimize the impact and prevalence of infections. Antimicrobial peptides produced by bacteria have begun to emerge as a potential means of decreasing the levels of C. jejuni in poultry, thereby limiting Campylobacter contamination in associated food products. A number of bacteriocins produced by Gram-positive bacteria have unexpectedly been described as having antimicrobial activity against the Gram-negative C. jejuni. Additionally, some nonribosomal lipopeptides produced by Bacillus and Paenibacillus spp. show efficacy against this pathogen. This review will describe the bacterial antimicrobial peptides reported to be active against C. jejuni, with an emphasis on the characterization of their primary structures. However, for many of these peptides, little is known about their amino acid sequences and structures. Furthermore, there are unusual inconsistencies associated with the reported amino acid sequences for several of the more well-studied bacteriocins. Clarifying the chemical nature of these promising antimicrobial peptides is necessary before their potential utility for livestock protection from C. jejuni can be fully explored. Once these peptides are better characterized, they may prove to be strong candidates for minimizing the impact of Campylobacter on human health.Key words: Campylobacter, bacteriocin, antimicrobial, lipopeptide, tridecaptin. Résumé :Campylobacter jejuni est l'un des agents les plus importants à l'origine de l'empoisonnement alimentaire, souvent dû à la consommation de produits de volaille cuits de manière inadéquate. L'émergence de souches de C. jejuni résistantes aux antibiotiques habituels exige d'évaluer les autres possibilités de traitements ou mesures préventives afin de réduire la préva-lence et les conséquences des infections. La possibilité d'utiliser les peptides antimicrobiens d'origine bactérienne pour diminuer les taux de C. jejuni dans la volaille et limiter ainsi la contamination des produits alimentaires dérivés par le Campylobacter est apparue récemment. De façon inattendue, un certain nombre de bactériocines produites par des bactéries à Gram positif ont été décrites comme ayant une activité antimicrobienne contre la bactérie à Gram négatif C. jejuni. De plus, certains lipopeptides d'origine non ribosomique produits par des espèces de Bacillus et Paenibacillus montrent une efficacité contre cet agent pathogène. Cet exposé de synthèse décrira les peptides antimicrobiens d'origine bactérienne dont l'activité contre C. jejuni est connue, et mettra l'accent sur la caractérisation de leur structure primaire. Cependant, on sait peu de choses de la séquence d'acides aminés et de la structure de plusieurs de ces peptides. En outre, les séquences d'acides aminés de plusi...

show abstract

Altered Linkage of Hydroxyacyl Chains in Lipid A of Campylobacter jejuni Reduces TLR4 Activation and Antimicrobial Resistance

Cited by 51 publications

References 45 publications

The lipopolysaccharide modification regulator PmrA limitsSalmonellavirulence by repressing the type three-secretion system Spi/Ssa

The lipopolysaccharide modification regulator PmrA limitsSalmonellavirulence by repressing the type three-secretion system Spi/Ssa

Campylobacter jejuniinduces extra-intestinal immune responses via toll-like-receptor-4 signaling in conventional IL-10 deficient mice with chronic colitis

Characterization of bacterial antimicrobial peptides active against Campylobacter jejuni

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