Capnocytophaga canimorsus sp. nov. (formerly CDC group DF-2), a cause of septicemia following dog bite, and C. cynodegmi sp. nov., a cause of localized wound infection following dog bite

Brenner, Don J.; Hollis, D G; Fanning, G R; Weaver, Robert E.

doi:10.1128/jcm.27.2.231-235.1989

Cited by 238 publications

(111 citation statements)

References 15 publications

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“…It includes a variety of commensals found in the oral flora of mammals. C. canimorsus are found in dogs and cats while Capnocytophaga gingivalis, Capnocytophaga ochracea and Capnocytophaga sputigena are found in human mouth (Brenner et al, 1989;Frandsen et al, 2008). Human infections by C. canimorsus occur after dog bites, scratches or simply licks.…”

Section: Introductionmentioning

confidence: 99%

The genome and surface proteome of Capnocytophaga canimorsus reveal a key role of glycan foraging systems in host glycoproteins deglycosylation

Manfredi

Renzi

Mally

et al. 2011

Molecular Microbiology

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SummaryCapnocytophaga canimorsus are commensal Gramnegative bacteria from dog's mouth that cause rare but dramatic septicaemia in humans. C. canimorsus have the unusual property to feed on cultured mammalian cells, including phagocytes, by harvesting the glycan moiety of cellular glycoproteins. To understand the mechanism behind this unusual property, the genome of strain Cc5 was sequenced and analysed. In addition, Cc5 bacteria were cultivated onto HEK 293 cells and the surface proteome was determined. The genome was found to encode many lipoproteins encoded within 13 polysaccharide utilization loci (PULs) typical of the FlavobacteriaBacteroides group. PULs encode surface exposed feeding complexes resembling the archetypal starch utilization system (Sus). The products of at least nine PULs were detected among the surface proteome and eight of them represented more than half of the total peptides detected from the surface proteome. Systematic deletions of the 13 PULs revealed that half of these Sus-like complexes contributed to growth on animal cells. The complex encoded by PUL5, one of the most abundant ones, was involved in foraging glycans from glycoproteins. It was essential for growth on cells and contributed to survival in mice. It thus represents a fitness factor during infection.

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Section: Introductionmentioning

confidence: 99%

The genome and surface proteome of Capnocytophaga canimorsus reveal a key role of glycan foraging systems in host glycoproteins deglycosylation

Manfredi

Renzi

Mally

et al. 2011

Molecular Microbiology

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“…are difficult to culture in vitro, and their growth rates are often relatively slow . These bacteria have specific nutrient requirements for optimal growth, including iron and CO 2 supplementation, and some media must be incubated for prolonged periods prior to bacterial colonies becoming detectable . The fastidious and slow‐growing nature of Capnocytophaga spp.…”

Section: Discussionmentioning

confidence: 99%

Capnocytophaga keratitis in dogs: clinical, histopathologic, and microbiologic features of seven cases

Ledbetter

Franklin‐Guild

Edelmann

2018

Veterinary Ophthalmology

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“…Local inhibition of coagulation by agglomerates of adhering bacteria in tissues, organs or blood vessels releasing CcDPP7 seems to be more probable. Brenner et al mentioned a C. canimorsus isolate derived from a petechial lesion [1], pointing to the presence of C. canimorsus in the skin, which is interesting with respect to the skin hemorrhage observed in patients. It is tempting to speculate that C. canimorsus could directly induce skin manifestations, like Neisseria meningitidis [40,41], or that it could reduce the inflammatory response and clearance, like Y. pestis [12], by locally blocking hemostasis.…”

Section: Discussionmentioning

confidence: 99%

Inactivation of human coagulation factor X by a protease of the pathogen Capnocytophaga canimorsus

Hack

Renzi

Hess

et al. 2017

Journal of Thrombosis and Haemostasis

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Background Capnocytophaga canimorsus is a Gram-negative bacterium that is present in the oral flora of dogs and causes fulminant sepsis in humans who have been bitten, licked, or scratched. In patients, bleeding abnormalities, such as petechiae, purpura fulminans, or disseminated intravascular coagulation (DIC), occur frequently. Objective To investigate whether C. canimorsus could actively contribute to these bleeding abnormalities. Methods Calibrated automated thrombogram and clotting time assays were performed to assess the anticoagulant activity of C. canimorsus 5 (Cc5), a strain isolated from a fatal human infection. Clotting factor activities were measured with factor-deficient plasma. Factor X cleavage was monitored with the radiolabeled zymogen and western blotting. Mutagenesis of Cc5 genes encoding putative serine proteases was performed to identify the protease that cleaves FX. Protein purification was performed with affinity chromatography. Edman degradation allowed the detection of N-terminal cleavage of FX. Tail bleeding times were measured in mice. Results We found that Cc5 inhibited thrombin generation and increased the prothrombin time and the activated partial thromboplastin time of human plasma via FX cleavage. A mutant that was unable to synthesize a type 7 dipeptidyl peptidase (DPP7) of the S46 serine protease family failed to proteolyse FX. The purified protease (CcDPP7) cleaved FX heavy and light chains from the N-terminus, and was active in vivo after intravenous injection. Conclusions This is, to our knowledge, the first study demonstrating a detailed mechanism for FX inactivation by a bacterial protease, and it is the first functional study associating DPP7 proteases with a potentially pathogenic outcome.

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Capnocytophaga canimorsus sp. nov. (formerly CDC group DF-2), a cause of septicemia following dog bite, and C. cynodegmi sp. nov., a cause of localized wound infection following dog bite

Abstract: Capnocytophaga canimorsus sp. nov. (Formerly CDC Group DF-2), a Cause of Septicemia following Dog Bite, and C. cynodegmi sp. nov., a Cause of Localized Wound Infection following Dog Bite

Cited by 238 publications

References 15 publications

The genome and surface proteome of Capnocytophaga canimorsus reveal a key role of glycan foraging systems in host glycoproteins deglycosylation

The genome and surface proteome of Capnocytophaga canimorsus reveal a key role of glycan foraging systems in host glycoproteins deglycosylation

Capnocytophaga keratitis in dogs: clinical, histopathologic, and microbiologic features of seven cases

Inactivation of human coagulation factor X by a protease of the pathogen Capnocytophaga canimorsus

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