Homology modeling of putative cell envelope proteinase in Streptococcus pyogenes

Streptococcus pyogenes is a species of bacteria. Like most other streptococci, it is clinically important in human illness. It is an infrequent, but usually pathogenic, part of the skin flora. It is the sole species of Lancefield group A and is often called group A streptococcus (GAS), because it displays streptococcal group A antigen on its cell wall. Bacterial surface proteins play a fundamental role in the interaction between the bacterial cell and its environment. They are involved in adhesion to and invasion of host cells, in sensing the chemical and physical conditions of the external milieu and sending appropriate signals to the cytoplasmic compartment, in mounting defenses against host responses and in toxicity. Hence, surface proteins are potential targets of drugs aimed at preventing bacterial infections and diseases. Spy0416 is a putative cell envelope proteinase carrying a typical cell wall–anchoring LPXTG motif, whose protective activity. Despite the biological relevance of bacterial surface proteins, their characterization is still incomplete. This is mostly owing to difficulties in defining the protein composition and topology on the bacterial surface. In this paper we predict putative cell envelope proteinase structure as a vaccine candidate in Streptococcus pyogenes via Homology modeling.

کلیدواژه ها:

Streptococcus pyogenes ، Homology modeling ، Spy0416