Coordinated Transcriptional Increases in Cell Wall Synthesis Genes in Neisseria gonorrhoeae Lacking the Lytic Transglycosylase, ltgA.

ABSTRACT: Lytic transglycosylase A in Neisseria gonorrhoeae cleaves the β-1,4-glycosidic bond between peptidoglycan (PG) monomers to liberate 1,6-anhydro-PG fragments that are either recycled or released as cytotoxic fragments. To gain further insight into the effect of LtgA on cellular processes in Neisseria gonorrhoeae, we performed a proteomic analysis comparing wild-type and an isogenic ltgA null mutant strain. Proteins were separated by two-dimensional gel electrophoresis and identified by MALDI-TOF mass spectrometry, which revealed several proteins that were increased in their level of expression upon loss of LtgA. The most notable changes corresponded to enzymes related to aminosugar and pyrimidine metabolism. Quantitative real-time RT-PCR of mRNA from a ltgA null strain confirmed increased t

SUBMITTER: Broadie CO 

PROVIDER: S-EPMC12055626 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature