The <i>Campylobacter jejuni</i> PEB1a adhesin is an aspartate/glutamate‐binding protein of an ABC transporter essential for microaerobic growth on dicarboxylic amino acids

Leon-Kempis, Maria del Rocio; Guccione, Edward; Mulholland, Francis; Williamson, Michael P.; Kelly, David J.

doi:10.1111/j.1365-2958.2006.05168.x

Cited by 108 publications

(70 citation statements)

References 36 publications

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“…The latter has been first described as surface-bound antigen of C. jejuni with homology to amino acid-binding proteins like GlnH and HisJ (Pei and Blaser, 1993). Further studies characterized Peb1A as a glutamate- and aspartate-binding protein (Leon-Kempis Mdel et al, 2006; Müller et al, 2007), and an isogenic C. jejuni peb1A mutant showed impaired growth with aspartate or glutamate as sole carbon sources (Leon-Kempis Mdel et al, 2006). This phenotype correlated with an abolished glutamate uptake.…”

Section: Finding a Nutritional Niche: The Low-carb High-protein Dietmentioning

confidence: 99%

“…This is reflected by the identification of two chemoreceptors, Tlp1 (Hartley-Tassell et al, 2010) and CcmL (Tlp3) (Rahman et al, 2014), that interact with aspartate. The uptake of aspartate is convoluted and involves various transporters: While the periplasmic binding protein Peb1A interacts with aspartate and participates in its uptake, the peb1A mutant still possesses capacity to import aspartate although with a 20-fold reduction (Leon-Kempis Mdel et al, 2006). The direct involvement of the other Peb ABC transporter components like the two Peb permeases and the Peb ATP-binding protein has not been experimentally proven yet.…”

Section: Finding a Nutritional Niche: The Low-carb High-protein Dietmentioning

confidence: 99%

“…Such a modified AnsB enzyme (AnsB s ) is translocated to the periplasm where it catalyzes the deamination of asparagine to aspartate. Consequently, the growth of ansB s - and ggt -positive C. jejuni isolates with asparagine and glutamine relies on the conversion of both amino acids to aspartate and glutamate in the periplasm and the subsequent uptake of the deaminated amino acids (Hofreuter et al, 2008) through the DcuAB, DctA and Peb transporters (Leon-Kempis Mdel et al, 2006; Guccione et al, 2008). Interestingly, many ggt -positive C. jejuni strains encode also for a secreted asparaginase but lack the fucP -gene cluster, while C. jejuni isolates without the GGT- and AnsB s -mediated expanded amino acid catabolism harbor the genes required for fucose utilization (Gripp et al, 2011; Zautner et al, 2011; de Haan et al, 2012).…”

Section: Finding a Nutritional Niche: The Low-carb High-protein Dietmentioning

confidence: 99%

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Defining the metabolic requirements for the growth and colonization capacity of Campylobacter jejuni

Hofreuter

2014

Front. Cell. Infect. Microbiol.

118

114

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During the last decade Campylobacter jejuni has been recognized as the leading cause of bacterial gastroenteritis worldwide. This facultative intracellular pathogen is a member of the Epsilonproteobacteria and requires microaerobic atmosphere and nutrient rich media for efficient proliferation in vitro. Its catabolic capacity is highly restricted in contrast to Salmonella Typhimurium and other enteropathogenic bacteria because several common pathways for carbohydrate utilization are either missing or incomplete. Despite these metabolic limitations, C. jejuni efficiently colonizes various animal hosts as a commensal intestinal inhabitant. Moreover, C. jejuni is tremendously successful in competing with the human intestinal microbiota; an infectious dose of few hundreds bacteria is sufficient to overcome the colonization resistance of humans and can lead to campylobacteriosis. Besides the importance and clear clinical manifestation of this disease, the pathogenesis mechanisms of C. jejuni infections are still poorly understood. In recent years comparative genome sequence, transcriptome and metabolome analyses as well as mutagenesis studies combined with animal infection models have provided a new understanding of how the specific metabolic capacity of C. jejuni drives its persistence in the intestinal habitat of various hosts. Furthermore, new insights into the metabolic requirements that support the intracellular survival of C. jejuni were obtained. Because C. jejuni harbors distinct properties in establishing an infection in comparison to pathogenic Enterobacteriaceae, it represents an excellent organism for elucidating new aspects of the dynamic interaction and metabolic cross talk between a bacterial pathogen, the microbiota and the host.

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Section: Finding a Nutritional Niche: The Low-carb High-protein Dietmentioning

confidence: 99%

Section: Finding a Nutritional Niche: The Low-carb High-protein Dietmentioning

confidence: 99%

Section: Finding a Nutritional Niche: The Low-carb High-protein Dietmentioning

confidence: 99%

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Defining the metabolic requirements for the growth and colonization capacity of Campylobacter jejuni

Hofreuter

2014

Front. Cell. Infect. Microbiol.

118

114

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“…Citric acid cycle intermediates such as pyruvate, fumarate, oxaloacetate and 2-oxoglutarate, succinate, fumarate and malate have been reported as energy sources for C. jejuni [6,10,16]. In addition, C. jejuni has been reported to metabolise short-chain fatty acids (SCFA) [9,13].…”

Section: Introductionmentioning

confidence: 99%

Differences in carbon source utilisation distinguish Campylobacter jejuni from Campylobacter coli

et al. 2014

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BackgroundCampylobacter jejuni and C. coli are human intestinal pathogens that are the most frequent causes of bacterial foodborne gastroenteritis in humans in the UK. In this study, we aimed to characterise the metabolic diversity of both C. jejuni and C. coli using a diverse panel of clinical strains isolated from the UK, Pakistan and Thailand, thereby representing both the developed and developing world. Our aim was to apply multi genome analysis and Biolog phenotyping to determine differences in carbon source utilisation by C. jejuni and C. coli strains.ResultsWe have identified a core set of carbon sources (utilised by all strains tested) and a set that are differentially utilised for a diverse panel of thirteen C. jejuni and two C. coli strains. This study used multi genome analysis to show that propionic acid is utilised only by C. coli strains tested. A broader PCR screen of 16 C. coli strains and 42 C. jejuni confirmed the absence of the genes needed for propanoate metabolism.ConclusionsFrom our analysis we have identified a phenotypic method and two genotypic methods based on propionic utilisation that might be applicable for distinguishing between C. jejuni and C. coli.Electronic supplementary materialThe online version of this article (doi:10.1186/s12866-014-0262-y) contains supplementary material, which is available to authorized users.

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“…Very few such solute specific binding proteins of glutamate ABC- transporter system in different bacterial species have been experimentally characterized. Three such proteins from E. coli K 12, Pseudomonas putida KT2440 and Campylobacter jejuni NCTC 11168 are GltI, AatJ (PP1071) and PEB1a (CJ0921c) respectively [11– 13]. The aligned consensus of these three sequences revealed putative gene/ORF for periplasmic glutamate binding protein in C. perfringens Type-A strains Table 2 (see supplementary material).…”

Section: Resultsmentioning

confidence: 99%

Identification of glutamate ABC-Transporter component in Clostridium perfringens as a putative drug target

et al. 2014

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Clostridium perfringens is an anaerobic pathogen known to cause vast number of diseases in mammals and birds. Various toxins and hydrolysing enzymes released by the organism are responsible for the necrosis of soft tissues. Due to serious safety issues associated with current vaccines against C. perfringens, there is a need for new drug or vaccine targets. C. perfringens is extremely dependent on its host for nutrition which can be targeted for vaccine development or drug design. Therefore, it is of interest to identify the unique transport systems used by C. perfringens involved in uptake of essential amino acids that are synthesized by the host, so that therapeutic agents can be designed to target the specific transport systems. Use of bioinformatics tools resulted in the identification of a protein component of the glutamate transport system that is not present in the host. Analysis of the conservation profile of the protein domain indicated it to be a glutamate binding protein which also stimulates the ATPase activity of ATP Binding Cassettes (ABC) transporters. Homology modelling of the protein showed two distinct lobes, which is a characteristic of substrate binding proteins. This suggests that the carboxylates of glutamate might be stabilized by electrostatic interactions with basic residues as is observed with other binding proteins. Hence, the homology model of this potential drug target can be employed for in silico docking studies by suitable inhibitors.

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The Campylobacter jejuni PEB1a adhesin is an aspartate/glutamate‐binding protein of an ABC transporter essential for microaerobic growth on dicarboxylic amino acids

Cited by 108 publications

References 36 publications

Defining the metabolic requirements for the growth and colonization capacity of Campylobacter jejuni

Defining the metabolic requirements for the growth and colonization capacity of Campylobacter jejuni

Differences in carbon source utilisation distinguish Campylobacter jejuni from Campylobacter coli

Identification of glutamate ABC-Transporter component in Clostridium perfringens as a putative drug target

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