Production, stability and degradation of Trichoderma gliotoxin in growth medium, irrigation water and agricultural soil.

Gliotoxin produced by Trichoderma virens is inhibitory against various phytopathogenic fungi and bacteria. However, its stability in soil-ecosystem has not yet been well-defined. This study aimed to decipher its persistence and behaviour in growth media, irrigation water and soil ecosystems. Gliotoxin production was noticed at logarithmic growth phase and converted into bis-thiomethyl gliotoxin at late stationary growth phase of T. virens in acidic growth medium. But, no gliotoxin production was observed in neutral and alkaline growth medium. Gliotoxin was stable for several days in acidic water but degraded in alkaline water. Degradation of gliotoxin was more in unsterile soil than sterile soil and also that was higher under wet soil than dry soil. Degradation of gliotoxin was hastened by alkaline pH in wet soil but not in dry soil. Under unsterile soil conditions, high soil moisture increased the degradation of gliotoxin and the degradation of gliotoxin occurred quickly in alkaline soil (in 5 days) compared to acidic soil (in 10 days). Under sterile soil conditions, high soil moisture also enhanced the degradation of gliotoxin but level of degradation was less compared to unsterile conditions. Thus, gliotoxin stability is influenced mainly by the soil wetness, soil microbial community and pH conditions.

Active sulfite oxidase domain of Salmonella enterica pathogenic protein small intestine invasive factor E (SiiE): a potential diagnostic target.

Serovars of Salmonella enterica are common food-borne bacterial pathogens. Salmonella typhi, which causes typhoid, is the most dangerous of them. Though detailed molecular pathogenesis studies reveal many virulence factors, inability to identify their biochemical functions hampers the development of diagnostic methods and therapeutic leads. Lack of quicker diagnosis is an impediment in starting early antibiotic treatment to reduce the severe morbidity and mortality in typhoid. In this study, employing bioinformatic prediction, biochemical analysis, and recombinantly cloning the active region, we show that extracellularly secreted virulence-associated protein, small intestinal invasion factor E (SiiE), possesses a sulfite oxidase (SO) domain that catalyzes the conversion of sodium sulfite to sodium sulfate using tungsten as the cofactor. This activity common to Salmonella enterica serovars seems to be specific to them from bioinformatic analysis of available bacterial genomes. Along with the ability of this large non-fimbrial adhesin of 600 kDa binding to sialic acid on the host cells, this activity could aid in subverting the host defense mechanism by destroying sulfites released by the immune cells and colonize the host gastrointestinal epithelium. Being an extracellular enzyme, it could be an ideal candidate for developing diagnostics of S. enterica, particularly S. typhi.