In silico analysis of Group A Streptococci virulence factor

The primary structure of the group A Streptococci virulence factor ‘M protein’ retrieved from SWISS-PROT’ was subjected to compositional, domain, fingerprint, secondary & tertiary structure analysis with the help of (basic) bioinformatics tools to establish its functions. The compositional analysis of the protein revealed that the Query protein was a stable one. The sequence was then subjected to Blast P & T blast n analysis to obtain similar sequences. The related sequences when subjected to multiple alignments revealed that the Gram positive anchor domain seems to be well conserved. Secondary structure analysis and transmembrane analysis revealed that this protein has helix predominant in the secondary structure. Homology modelling with similar sequences from SCOP database established the folded tertiary structure of the query protein. These analyses revealed that the query protein consists of conserved C-terminal hydrophobic hexa peptide region similar to other non-pathogenic Gram positive cocci & other sero types of these bacteria.