Aspartate chemosensory receptor signalling in<i>Campylobacter jejuni</i>

Korolik, Victoria

doi:10.4161/viru.1.5.12735

Cited by 9 publications

(10 citation statements)

References 27 publications

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“…Transducer like proteins (Tlps) are the key components involved in sensing environmental signals through chemotaxis or energy taxis in C. jejuni . ( Marchant et al, 2002 ; Vegge et al, 2009 ; Korolik, 2010 ; Tareen et al, 2010 ; Reuter and van Vliet, 2013 ; Rahman et al, 2014 ). Amino acids (aspartate, glutamate and serine), organic acid salts (succinate, isocitrate, and formate), bile and mucin are chemoattractants for C. jejuni ( Hugdahl et al, 1988 ; Hartley-Tassell et al, 2010 ; Tareen et al, 2010 ).…”

Section: Introductionmentioning

confidence: 99%

Transducer-Like Protein in Campylobacter jejuni With a Role in Mediating Chemotaxis to Iron and Phosphate

et al. 2018

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Chemotaxis-mediated motility enables Campylobacter jejuni to navigate through complex environmental gradients and colonize diverse niches. C. jejuni is known to possess several methyl accepting chemotaxis proteins (MCPs), also called transducer-like proteins (Tlps). While the role of some of the Tlps in chemotaxis has been identified, their regulation and role in virulence is still not very clear. Here, we investigated the contribution of Tlp2 to C. jejuni chemotaxis, stress survival and colonization of the chicken gastrointestinal tract. The Δtlp2 deletion mutant showed decreased chemotaxis toward aspartate, pyruvate, inorganic phosphate (Pi), and iron (FeSO4). Transcriptional analysis of tlp2 with a promoter fusion reporter assay revealed that the tlp2 promoter (Ptlp2) was induced by Pi and iron, both in the ferrous (Fe2+) and ferric form (Fe3+). RT-PCR analysis using overlapping primers indicated that the phoX gene, located immediately downstream of tlp2, is co-transcribed with tlp2. A transcription start site was identified at 53 bp upstream of the tlp2 start codon. The Δtlp2 mutant showed decreased colonization of the chicken gastrointestinal tract. Collectively, our findings revealed that the tlp2 plays a role in C. jejuni pathogenesis and colonization in the chicken host and its expression is regulated by iron.

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Section: Introductionmentioning

confidence: 99%

Transducer-Like Protein in Campylobacter jejuni With a Role in Mediating Chemotaxis to Iron and Phosphate

et al. 2018

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“…Based on this information and previous reports, a functional Tlp3 seems to be absent in the C. jejuni 81-176. 67,69 A recent study on the expression of tlp genes in different C. jejuni strains also pointed out that tlp3 expression was absent in the C. jejuni 81-176 strain. 64 It might be important to note that a functional Tlp3 and its role in aspartate chemotaxis might explain why tlp1 mutants resulted in different colonization phenotypes in different strains.…”

Section: Tlp3mentioning

confidence: 99%

Campylobacter jejunitransducer like proteins: Chemotaxis and beyond

2017

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Chemotaxis, a process that mediates directional motility toward or away from chemical stimuli (chemoeffectors/ligands that can be attractants or repellents) in the environment, plays an important role in the adaptation of Campylobacter jejuni to disparate niches. The chemotaxis system consists of core signal transduction proteins and methyl-accepting-domain-containing Transducer like proteins (Tlps). Ligands binding to Tlps relay a signal to chemotaxis proteins in the cytoplasm which initiate a signal transduction cascade, culminating into a directional flagellar movement. Tlps facilitate substrate-specific chemotaxis in C. jejuni, which plays an important role in the pathogen's adaptation, pathobiology and colonization of the chicken gastrointestinal tract. However, the role of Tlps in C. jejuni's host tissue specific colonization, physiology and virulence remains not completely understood. Based on recent studies, it can be predicted that Tlps might be important targets for developing strategies to control C. jejuni via vaccines and antimicrobials.

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“…The varying binding strength of CheV and CheW to different chemoreceptor signalling domains suggests that both proteins may out-compete each other depending on the specific receptor and the protein concentration [33,66]. Thus, CheW preferentially binds Tlp4, whereas CheV demonstrates a high affinity to Tlp1, Tlp4, Tlp6 as well as Tlp8 [65,66].…”

Section: Different Mechanisms Of Sensory Adaptationmentioning

confidence: 99%

“…It is possible that this competition is part of a kind of sensory adaptation. It could also be that alternative pathways are controlled by either protein [33].…”

Section: Different Mechanisms Of Sensory Adaptationmentioning

confidence: 99%