Characterization of two putative mechanosensitive channel proteins of Campylobacter jejuni involved in protection against osmotic downshock

Kakuda, Tsutomu; Koide, Yuuki; Sakamoto, Aya; Takaı̈, Shinji

doi:10.1016/j.vetmic.2012.04.044

Cited by 17 publications

(24 citation statements)

References 24 publications

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“…B) clearly showed expression of the gene in our NCTC 11168 strain. Interestingly, we noted from the genome sequence that canB ( cj0237 ) is translationally coupled to cj0238 , encoding MscS, a small mechanosensitive ion channel (Kakuda et al ., ), and we confirmed by RT‐PCR that these genes are co‐transcribed (Fig. B).…”

Section: Resultssupporting

confidence: 70%

“…) strongly suggests a functional interaction of the gene products. mscS encodes a mechanosensitive ion channel that is known to be required in C. jejuni for cell survival following osmotic downshock (Kakuda et al ., ). Intriguingly, in higher organisms, binding of CA to aquaporins has been shown to enhance channel activity (Vilas et al ., ), which may point to the possibility of modulation of MscS activity by CanB.…”

Section: Discussionmentioning

confidence: 97%

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Major contribution of the type II beta carbonic anhydrase CanB (Cj0237) to the capnophilic growth phenotype of Campylobacter jejuni

Al-Haideri

White

Kelly

2015

Environmental Microbiology

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Campylobacter jejuni, the leading cause of human bacterial gastroenteritis, requires low environmental oxygen and high carbon dioxide for optimum growth, but the molecular basis for the carbon dioxide requirement is unclear. One factor may be inefficient conversion of gaseous CO2 to bicarbonate, the required substrate of various carboxylases. Two putative carbonic anhydrases (CAs) are encoded in the genome of C. jejuni strain NCTC 11168 (Cj0229 and Cj0237). Here, we show that the deletion of the cj0237 (canB) gene alone prevents growth in complex media at low (1% v/v) CO2 and significantly reduces the growth rate at high (5% v/v) CO2. In minimal media incubated under high CO2, the canB mutant grew on L-aspartate but not on the key C3 compounds L-serine, pyruvate and L-lactate, showing that CanB is crucial in bicarbonate provision for pyruvate carboxylase-mediated oxaloacetate synthesis. Nevertheless, purified CanB (a dimeric, anion and acetazolamide sensitive, zinc-containing type II beta-class enzyme) hydrates CO2 actively only above pH 8 and with a high Km (∼ 34 mM). At typical cytoplasmic pH values and low CO2, these kinetic properties might limit intracellular bicarbonate availability. Taken together, our data suggest CanB is a major contributor to the capnophilic growth phenotype of C. jejuni.

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Section: Resultssupporting

confidence: 70%

Section: Discussionmentioning

confidence: 97%

Major contribution of the type II beta carbonic anhydrase CanB (Cj0237) to the capnophilic growth phenotype of Campylobacter jejuni

Al-Haideri

White

Kelly

2015

Environmental Microbiology

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“…Removal of the N-linked glycans from Cj1496c, a protein involved in epithelial cell invasion and chicken colonization, and ZnuA, which is important for survival in low-zinc environments, showed no significant influence on the function of these proteins (42,45). Similarly, the N-glycan on the surface-associated lipoprotein JlpA, an adhesin required for chicken colonization, was not required for protein antigenicity (47,48), and N-glycosylation of two mechanosensitive channel proteins had no major effect on their function and stability (49). However, N-glycosylation at one site of VirB10, a periplasmic component of the type IV secretion system, was shown to be important for DNA uptake and stability of the complex (44).…”

Section: Biological Significancementioning

confidence: 96%

Bacterial Protein N-Glycosylation: New Perspectives and Applications

Nothaft

Szymanski

2013

Journal of Biological Chemistry

144

123

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Protein glycosylation is widespread throughout all three domains of life. Bacterial protein N-glycosylation and its application to engineering recombinant glycoproteins continue to be actively studied. Here, we focus on advances made in the last 2 years, including the characterization of novel bacterial N-glycosylation pathways, examination of pathway enzymes and evolution, biological roles of protein modification in the native host, and exploitation of the N-glycosylation pathways to create novel vaccines and diagnostics.

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“…Two MscS homologs from the food-borne pathogen Campylobacter jejuni, Cjj0263 and Cjj1025 , were recently found to be required for colonization of the digestive tract of chicks 136 , and a Pseudomonas aeruginosa MscK ortholog has been associated with virulence 137 . PamA, a MscS homolog from the photosynthetic cyanobacterium Synechocystis sp.PCC6803 was reported to interact in vitro and in vivo with PII, a highly conserved carbon/nitrogen sensor 138, 139 .…”

Section: Mscs and Mscs-like Channels: Conservation And Diversitymentioning

confidence: 99%

MscS-like Mechanosensitive Channels in Plants and Microbes

2013

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The challenge of osmotic stress is something all living organisms must face as a result of environmental dynamics. Over the past three decades, innovative research and cooperation across disciplines has irrefutably established that cells utilize mechanically gated ion channels to release osmolytes and prevent cell lysis during hypoosmotic stress. Early electrophysiological analysis of the inner membrane of Escherichia coli identified the presence of three distinct mechanosensitive activities. The subsequent discoveries of the genes responsible for two of these activities, the mechanosensitive channels of large (MscL) and small (MscS) conductance, led to the identification of two diverse families of mechanosensitive channels. The latter of these two families, the MscS family, is made up of members from bacteria, archaea, fungi, and plants. Genetic and electrophysiological analysis of these family members has provided insight into how organisms use mechanosensitive channels for osmotic regulation in response to changing environmental and developmental circumstances. Furthermore, solving the crystal structure of E. coli MscS and several homologs in several conformational states has contributed to the understanding of the gating mechanisms of these channels. Here we summarize our current knowledge of MscS homologs from all three domains of life, and address their structure, proposed physiological functions, electrophysiological behaviors, and topological diversity.

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Characterization of two putative mechanosensitive channel proteins of Campylobacter jejuni involved in protection against osmotic downshock

Cited by 17 publications

References 24 publications

Major contribution of the type II beta carbonic anhydrase CanB (Cj0237) to the capnophilic growth phenotype of Campylobacter jejuni

Major contribution of the type II beta carbonic anhydrase CanB (Cj0237) to the capnophilic growth phenotype of Campylobacter jejuni

Bacterial Protein N-Glycosylation: New Perspectives and Applications

MscS-like Mechanosensitive Channels in Plants and Microbes

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