Chondroitinase AC: A host-associated genetic feature of Helicobacter bizzozeronii

Namburi, Ramesh Babu; Berteau, Olivier; Spillmann, Dorothe; Rossi, Mirko

doi:10.1016/j.vetmic.2016.02.013

Cited by 4 publications

(3 citation statements)

References 33 publications

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“…Another example of the acquisition of a genetic feature associated with adaptation to a specific niche is the unique presence of chondroitinase AC in H. bizzozeronnii . Chondroitinase AC binds to chondroitin‐4‐sulfate, which is secreted in the fundus mucosa and is unique for the canine stomach . A system for the incorporation of selenocysteine is found in all Helicobacter sp., except for H. pylori and H. acinonychis, indicating a loss in the common ancestor .…”

Section: Pathogenesis Of Infections With Nhphmentioning

confidence: 99%

“…Chondroitinase AC binds to chondroitin-4-sulfate, which is secreted in the fundus mucosa and is unique for the canine stomach. 28 A system for the incorporation of selenocysteine is found in all Helicobacter sp., cancer were also more expressed (S100A3). These upregulations were regulated through an activation of the NF-κB signaling pathway.…”

Section: Pathogenesis Of Infections With Nhphmentioning

confidence: 99%

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Other Helicobacters and gastric microbiota

et al. 2016

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This article aimed to review the literature from 2015 dealing with gastric and enterohepatic non-Helicobacter pylori Helicobacter species (NHPH). A summary of the gastric microbiota interactions with H. pylori is also presented. An extensive number of studies were published during the last year and have led to a better understanding of the pathogenesis of infections with NHPH. These infections are increasingly reported in human patients, including infections with H. cinaedi, mainly characterized by severe bacteremia. Whole-genome sequencing appears to be the most reliable technique for identification of NHPH at species level. Presence of NHPH in laboratory animals may influence the outcome of experiments, making screening and eradication desirable. Vaccination based on UreB proteins or bacterial lysate with CCR4 antagonists as well as oral glutathione supplementation may be promising strategies to dampen the pathogenic effects associated with gastric NHPH infections. Several virulent factors such as outer membrane proteins, phospholipase C-gamma 2, Bak protein, and nickel-binding proteins are associated with colonization of the gastric mucosae and development of gastritis. The development of high-throughput sequencing has led to new insights in the gastric microbiota composition and its interaction with H. pylori. Alterations in the gastric microbiota caused by the pH-increasing effect of a H. pylori infection may increase the risk for gastric cancer.

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Section: Pathogenesis Of Infections With Nhphmentioning

confidence: 99%

Section: Pathogenesis Of Infections With Nhphmentioning

confidence: 99%

Other Helicobacters and gastric microbiota

et al. 2016

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“…MAT3885 can degrade Chn, CS and HA (Kale et al, 2015). Namburi et al found a CSase AC from Helicobacter bizzozeronii in canine stomach, and this enzyme exhibited specific endolytic activity on HA and various CSs with different sulfation patterns at an optimum low pH between pH 4.0 and pH 5.5 and might represent one of several factors involved in the development of gastritis in dogs (Namburi et al, 2016). The CSase AsChnAC identified from Arthrobacter sp.…”

Section: Newly Identified Cs/ds Lyasesmentioning

confidence: 99%

Research and Application of Chondroitin Sulfate/Dermatan Sulfate-Degrading Enzymes

Wang

Shi

Qin

et al. 2020

Front. Cell Dev. Biol.

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Chondroitin sulfate (CS) and dermatan sulfate (DS) are widely distributed on the cell surface and in the extracellular matrix in the form of proteoglycan, where they participate in various biological processes. The diverse functions of CS/DS can be mainly attributed to their high structural variability. However, their structural complexity creates a big challenge for structural and functional studies of CS/DS. CS/DS-degrading enzymes with different specific activities are irreplaceable tools that could be used to solve this problem. Depending on the site of action, CS/DS-degrading enzymes can be classified as glycosidic bond-cleaving enzymes and sulfatases from animals and microorganisms. As discussed in this review, a few of the identified enzymes, particularly those from bacteria, have wildly applied to the basic studies and applications of CS/DS, such as disaccharide composition analysis, the preparation of bioactive oligosaccharides, oligosaccharide sequencing, and potential medical application, but these do not fulfill all of the needs in terms of the structural complexity of CS/DS.

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