Only a subset of C. canimorsus strains is dangerous for humans

Capnocytophaga canimorsus are gram-negative bacteria living as commensals in the mouth of dogs and cats. C. canimorsus cause rare but life-threatening generalized infections in humans that have been in contact with a dog or a cat. Over the last years we collected 105 C. canimorsus strains from different geographical origins and from severe human infections or healthy dogs. All these strains were analyzed by 16S rDNA sequencing and a phylogenetic tree revealed two main groups of bacteria instead of one with no relation to the geographical origin. This branching was confirmed by the whole-genome sequencing of 10 strains, supporting the evidence of a new Capnocytophaga species in dogs. Interestingly, 19 out of 19 C. canimorsus strains isolated from human infections belonged to the same species. Furthermore, most strains from this species could grow in heat-inactivated human serum (HIHS) (40/46 tested), deglycosylate IgM (48/66) and were cytochrome-oxidase positive (60/66) while most strains from the other species could not grow in HIHS (22/23 tested), could not deglycosylate IgM (33/34) and were cytochrome-oxidase negative (33/34). Here, we propose to call Capnocytophaga canis (Latin: dog) the novel, presumably less virulent dog-hosted Capnocytophaga species and to keep the name C. canimorsus for the species including human pathogens

Studying the regulation of the operon ftsW-psr-pbp5 in Enterococcus hirae

GENESI

Modélisation de la β-lactamase BlaP chez Bacillus licheniformis

In bacteria, the production of a β-lactamase, an hydrolase specific to β-lactam antibiotics, may be constitutive or inducible. In Bacillus licheniformis 749/I the presence of a β-lactam in the external media is detected by a protein relay producing an intracellular signal which leads to the induction of BlaP β-lactamase expression. The blaP gene is included in a divergeon along with blaI, coding for a cytoplasmic repressor, and blaR1, coding for a penicillin membrane receptor. Both, the acylation of the extracellular domain of BlaR1 by a β-lactam together with cellular stress due to the presence of the antibiotic outside the cell generate a dipeptide (coactivator) resulting from the peptidoglycan turnover that destabilizes BlaI repressor-DNA complex, leading to the expression of β-lactam resistance.Etude de l'induction de la β-lactamase BlaP chez Bacillus licheniformi