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The second messenger cyclic diguanylate monophosphate (c-di-GMP) has been proven to be a central regulator for physiological and metabolic processes including biofilm formation and sessile to motile transitioning (1,2). The synthesis and degradation of c-di-GMP are regulated by GGDEF- respectively EAL-domain proteins. Recently, c-di-GMP has been discovered in the Gram-positive Streptococcus genus including Streptococcus gallolyticus, which showed to have diguanylate cyclase activity (3). Characterisation of the c-di-GMP network in other Streptococcus is of relevance. Hence, the aim of this project was the assessment of the GGDEF- and EAL domains from the animal pathogenic Streptococcus uberis and Streptococcus henryi. In vivo recombination cloning was used for the analysis of the GGDEF, EAL and GGDEF-EAL domain proteins from S. uberis and S. henryi. The cloning was unsuccessful for most of the domain proteins, except, for EAL 2 of S. uberis. However, analysis of the sequencing results for the cloned EAL 2 presented mutations. Further studies testing alternative cloning methods should be applied. Research regarding probiotic streptococci is also of interest. Therefore, isolation of Streptococcus salivarius from human oral samples using Streptococcus Selection Agar was conducted. Isolation of S. salivarius from human saliva and tongue samples was successful using Streptococcus Selection Agar. Other Streptococcus spp., Lactobacillus, Staphylococcus, and additional bacterial species were also isolated. |
