Abstract

by Parastoo
(Malaysia)

Original Text: Abstract

Melioidosis is caused by the Gram negative and antibiotic resistant saprophytic bacterium Burkholderia pseudomallei, which is endemic to Southeast Asia and Northern Australia. This disease is difficult to treat and it depend on β lactam antibiotics to perturb the cell wall biosynthetic machinery by targeting penicillin binding proteins (PBPs) which catalyze the last steps in the synthesis of the peptidoglycan. Cephalosporin resistant strains have now emerged which have greatly reduced the efficacy of these antibiotics in the treatment of B. pseudomallei infections. At least nine type PBPs have been identified in B. pseudomallei. Compared to other PBPs, limited studies have been done on PBP1C which is a bifunctional transglycosylase/transpeptidase protein and belong to high molecular weight PBPs that are essential for bacterial growth. The transglycosylase domain is of particular interest because it may harbor a yet uncharacterized fold and thus could be a novel potential antibacterial development target and in the other hand, the transpeptidase is responsible for the final stages of cell wall synthesis in bacteria and the molecular target for β-lactam antibiotics. Although these antibiotics have been practically considered ineffective against melioidosis. Thus, PBP1C remain potential target and is therefore important to study. In order to delineate the role of PBP1C in chromosomally mediated resistant to cephalosporins, we have cloned, expressed, , purified and studied kinetic assay of transglycosylase and transpeptidase domains of PBP1C from Burkholderia pseudomallei R15 strain, a cephalosporin resistant clinical isolates from Malaysia as the first report of a PBP from this important pathogen bacteria.

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Revised Text:

Melioidosis is caused by the Gram negative and antibiotic resistant saprophytic bacterium, Burkholderia pseudomallei, which is endemic to Southeast Asia and Northern Australia. This disease is difficult to treat. It depends on β lactam antibiotics to perturb the cell wall biosynthetic machinery by targeting penicillin binding proteins (PBPs), which catalyzes the last steps in the synthesis of the peptidoglycan.

Cephalosporin resistant strains have now emerged, which has greatly reduced the efficacy of these antibiotics in the treatment of B. pseudomallei infections. At least nine types of PBPs have been identified in B. pseudomallei. Compared to other PBPs, limited studies have been done on PBP1C, which is a bifunctional transglycosylase/transpeptidase protein, and belongs to high molecular weight PBPs that are essential for bacterial growth.

The transglycosylase domain is of particular interest because it may harbor a yet uncharacterized fold, and thus could be a novel potential antibacterial development target. On the other hand, the transpeptidase is responsible for the final stages of cell wall synthesis in bacteria and is the molecular target for β-lactam antibiotics, although these antibiotics have been practically considered ineffective against melioidosis.

Thus, PBP1C remains a potential target, and is therefore important to study. In order to delineate the role of PBP1C in chromosomally mediated resistant to cephalosporins, we have cloned, expressed, purified and studied the kinetic assay of transglycosylase and transpeptidase domains of PBP1C from the Burkholderia pseudomallei R15 strain, a cephalosporin resistant clinical isolates from Malaysia, for the first report of a PBP from this important pathogen bacteria.

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