Characterization of Clostridioides difficile ribotypes in domestic dogs in Rio de Janeiro, Brazil.

Clostridioides difficile is the major etiologic agent of nosocomial bacterial diarrhoea and pseudomembranous colitis. The pathogenesis of C. difficile infection (CDI)involves two cytotoxic enzymes (TcdA, TcdB) that cause colonic epithelial damage, fluid accumulation and enteritis. CDI has been demonstrated in a variety of animal species and some reports have recently raised the importance of wild animals as a reservoir of this pathogen and possible transmission to humans and domestic animals. The aim of this study was to characterize C. difficile isolates obtained from pet dogs in Rio de Janeiro, Brazil. A total of 50 faecal samples were obtained from healthy and diarrheic dogs. Five of fifty samples (10%) grew C. difficile. Of those, three belonged to the PCR ribotype 106 (ST 42) and were toxigenic (A+B+). The other two strains belonged to the PCR ribotype 010 (ST 15) and were not toxin producers (A-B-). None of the isolates tested positive for the binary toxin genes. Considering the antimicrobial resistance patterns of all isolates using EUCAST breakpoints, all strains were sensitive to metronidazole and vancomycin. However, two strains (ribotype 106 and ribotype 010), were resistant to clindamycin (≤256 µg/mL). All strains were strong biofilm producers. Our study provides evidence that dogs can act as reservoirs for C. difficile epidemic ribotypes.

Proteome data set of human gingival crevicular fluid from healthy periodontium sites by multidimensional protein separation and mass spectrometry.

BACKGROUND AND OBJECTIVE: Gingival crevicular fluid has been of major interest for many decades as a valuable body fluid that may serve as a source of biomarkers for both periodontal and systemic diseases. Owing to its very small sample size, submicroliter volumes, identification of its protein composition by classical biochemical methods has been limited. The advent of highly sensitive mass spectrometric technology has permitted large-scale identification of protein components of many biological samples. This technology has been employed to identify the protein composition of gingival crevicular fluid from inflamed and periodontal sites. In this report, we present a proteome data set of gingival crevicular fluid from healthy periodontium sites. MATERIAL AND METHODS: A combination of a periopaper collection method with application of multidimensional protein separation and mass spectrometric technology led to a large-scale documentation of the proteome of gingival crevicular fluid from healthy periodontium sites. RESULTS: The approaches used have culminated in identification of 199 proteins in gingival crevicular fluid of periodontally healthy sites. The present gingival crevicular fluid proteome from healthy sites was compared and contrasted with those proteomes of gingival crevicular fluid from inflamed and periodontal sites, as well as serum. The cross-correlation of the gingival crevicular fluid and plasma proteomes permitted dissociation of the 199 identified gingival crevicular fluid proteins into 105 proteins (57%) that can be identified in plasma and 94 proteins (43%) that are distinct and unique to the gingival crevicular fluid microenvironment. Such analysis also revealed distinctions in protein functional categories between serum proteins and those specific to the gingival crevicular fluid microenvironment. CONCLUSION: Firstly, the data presented herein provide the proteome of gingival crevicular fluid from periodontally healthy sites through establishment of innovative analytical approaches for effective analysis of gingival crevicular fluid from periopapers both at the level of complete elusion and with removal of abundant albumin, which restricts identification of low-abundant proteins. Secondly, it adds significantly to the knowledge of gingival crevicular fluid composition and highlights new groups of proteins specific to the gingival crevicular fluid microenvironment.