In silico study of the structure and function of Streptococcus mutans plasmidic proteins

The Gram-positive bacterium Streptococcus mutans is the principal causative agent of human tooth decay, an oral disease that affects the majority of the world’s population. Although the complete S. mutans genome is known, approximately 700 proteins are still annotated as hypothetical proteins, as no threedimensional structure or homology with known proteins exists for them. Thus, the significant portion of genomic sequences coding for unknown-function proteins makes the knowledge of pathogenicity and survival mechanisms of S. mutans still incomplete. Plasmids are found in virtually every species of Streptococcus, and some of these mediate resistance to antibiotics and pathogenesis. However, there are strains of S. mutans that contain plasmids, such as LM7 and UA140, to which no function has been assigned yet. In this work, we describe an in silico study of the structure and function of all the S. mutans proteins encoded by pLM7 and pUA140 plasmids to gain insight into their biological function. A combination of different structural bioinformatics methodologies led to the identification of plasmidic proteins potentially required for the bacterial survival and pathogenicity. The structural information obtained on these proteins can be used to select novel targets for the design of innovative therapeutic agents towards S. mutans.