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Microbial virulence is the ability of pathogen to penetrate, replicate, multiplícate and, as a consequence, damage the cells of the infected organism. In recent years, rapid progress in bacterial genome sequencing has led to the discovery and characterization of many new virulence factors. One of the many mechanisms of bacterial virulence is the activity of bacterial kinases and phosphatases. These enzymes phosphorylate and dephosphorylate various amino acid residues in proteins, most commonly serine, tyrosine and threonine. Reversible phosphorylation and dephosphorylation can control the activity of target proteins, either directly, by inducing conformational changes in proteins, or indirectly, by regulating protein-protein interactions. Due to the increasing antibiotic resistance, new substances that could be used to treat diseases caused by resistant bacterial strains are sought. One of the possibilities seems to be the inhibition of bacterial tyrosine phosphatases. Phosphorylation of proteins containing tyrosine residues is a key post-translational modification that controls the numerous cellular functions in bacteria. So far, many tyrosine phosphatases have been found to be responsible for the virulence of various bacterial strains. Many bacterial species use protein tyrosine phosphatases activity in host-pathogen interaction, by affecting signalling pathways and subsequent induction of the infection process. Many studies are devoted to the search for tyrosine phosphatases inhibitors in the context of possible support of the current antibacterial treatment. This article presents a review of reports on bacterial virulence factors-protein tyrosine phosphatases as potential therapeutic targets.
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