Mutation of a single lytic transglycosylase causes aberrant septation and inhibits cell separation of Neisseria gonorrhoeae.
نویسندگان
چکیده
The function of lytic peptidoglycan transglycosylases is poorly understood. Single lytic transglycosylase mutants of Escherichia coli have no growth phenotype. By contrast, mutation of Neisseria gonorrhoeae ltgC inhibited cell separation without affecting peptidoglycan monomer production. Thus, LtgC has a dedicated function in gonococcal cell division.
منابع مشابه
Neisseria gonorrhoeae uses two lytic transglycosylases to produce cytotoxic peptidoglycan monomers.
Peptidoglycan fragments released by Neisseria gonorrhoeae contribute to the inflammation and ciliated cell death associated with gonorrhea and pelvic inflammatory disease. However, little is known about the production and release of these fragments during bacterial growth. Previous studies demonstrated that one lytic transglycosylase, LtgA, was responsible for the production of approximately ha...
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Neisseria gonorrhoeae releases soluble fragments of peptidoglycan during growth. These molecules are implicated in the pathogenesis of various forms of gonococcal infection. A major peptidoglycan fragment released by gonococci is identical to the tracheal cytotoxin of Bordetella pertussis and has been shown to kill ciliated fallopian tube cells in organ culture. Previous studies indicated that ...
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متن کاملBulgecin A: The Key to a Broad-Spectrum Inhibitor That Targets Lytic Transglycosylases
Lytic transglycosylases (Lts) are involved in recycling, cell division, and metabolism of the peptidoglycan. They have been understudied for their usefulness as potential antibacterial targets due to their high redundancy in Gram-negative bacteria. Bulgecin A is an O-sulphonated glycopeptide that targets primarily soluble lytic tranglycosylases (Slt). It has been shown that bulgecin A increases...
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ورودعنوان ژورنال:
- Journal of bacteriology
دوره 186 22 شماره
صفحات -
تاریخ انتشار 2004