Envelope cell wall of gram-positive bacteria, macromolecular, exoskeleton organelles that are collected and submitted in prescribed areas. Cell wall also functions as a surface organelles that allows gram-positive pathogens to interact with the environment, particularly in the tissues of the infected host. All these functions require that surface proteins and enzymes, properly targeted to the cell wall envelope. Two major mechanisms of cell wall sorting and targeting, have been identified. Cell sorting and covalent joining surface proteins peptidoglycan through C-terminal sorting signal that contains a consensus LPXTG sequence. More than 100 proteins with cell wall sorting signals, including the M proteins of Streptococcus pyogenes, Staphylococcus aureus protein, and several internalins of Listeria, were found. Targeting cell wall involves attachment nekovalentnyh proteins on the cell surface via specialized binding domains. Some of these wall-binding domains appear to interact with secondary wall strattera price polymers that are associated with the peptidoglycan, for example teyhoevye acids and polysaccharides. Proteins targeted to the cell surface muralytic include enzymes such as autolysins, and phage lytic lizostafin enzymes. Other examples for targeted proteins surface S-layer proteins of bacteria and clostridia, as well as virulence factors required for pathogenesis monotsytohenes L. (Internalin B) and pneumococcus (PVNS) infection. In this review we examine the mechanisms for sorting proteins to the membrane attack gram-positive bacteria and review the functions of known surface proteins. .
