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Vitali, L. A.

Publications and source records attributed to Vitali, L. A..

2 recordsLinked to original sources
bioRxiv2017

High degree of virulence gene diversity in Streptococcus pyogenes isolated in Central Italy

Globally, Streptococcus pyogenes poses a continuous burden on human health, causing both self-limiting and life-threatening diseases. Therefore, studying the profile of virulence genes and their combinations is essential to monitor the epidemiology and pathogenetic potential of this important species. Thus, the aim of this study was to analyze some genetic features of clinical strains collected in Italy in 2012.\n\nWe conducted fibronectin-collagen-T antigen (FCT) region typing and emm typing in 122 S. pyogenes strains. Furthermore, several additional virulence genes were screened by polymerase chain reaction.\n\nWe found correlations between emm types and FCT region profiles. emm1 strains were mainly associated with FCT2 and FCT6, while emm89 and emm12 strains were associated with FCT4. FCT5 was mainly represented in emm4, emm6, and emm75 strains. Noteworthy, we defined subtypes for each FCT type based on the differences in single and multiple loci compared to the reference scheme used for the classification of the FCT region. In addition, new FCT types were identified. Cluster analysis based on virulence gene profiling showed a non-random distribution within each emm type.\n\nThis study showed the high variability of S. pyogenes strains and the great diversification that this pathogen has undergone during its evolution in the human host.

microbiology↗
bioRxiv2017

Antidiabetic drugs “gliptin” affect biofilm formation by the cariogenic bacterium Streptococcus mutans through inhibition of the bacterial DPP IV-like enzyme

Streptococcus mutans, a dental caries causing odontopathogen, produces X-prolyl dipeptidyl peptidase (Sm-XPDAP, encoded by pepX), a serine protease known to have a nutritional role. Considering the potential of proteases as therapeutic targets in pathogens, this study was primarily aimed at investigating the role of Sm-XPDAP in contributing to virulence-related traits. Dipeptidyl peptidase (DPP IV), an XPDAP analogous enzyme found in mammalian tissues, is a well known therapeutic target in Type II diabetes. Based on the hypothesis that gliptins, commonly used as anti-human-DPP IV drugs, may affect bacterial growth upon inhibition of Sm-XPDAP, we have determined their ex vivo antimicrobial and anti-biofilm activity towards S. mutans. All three DPP IV drugs tested reduced biofilm formation as determined by crystal violet staining. To link the observed biofilm inhibition to the human-DPP IV analogue present in S. mutans UA159, a pepX isogenic mutant was generated. In addition to reduced biofilm formation, CLSM studies of the biofilm formed by the pepX isogenic mutant showed these were comparable to those formed in the presence of saxagliptin, suggesting a probable role of this enzyme in biofilm formation by S. mutans UA159. The effects of both pepX deletion and DPP IV drugs on the proteome were studied using LC-MS/MS. Overall, this study highlights the potential of Sm-XPDAP as a novel anti-biofilm target and suggests a template molecule to synthesize lead compounds effective against this enzyme.

microbiology↗