Microbial Physiology · 2016 · 15 citations · 45 references
Gluconate KinaseMetabolic PathwaysBiosynthesisN. MeningitidisBiochemistryNeisseria Meningitidis StrainGlycobiologyPolysaccharideMicrobiologyMetabolismMedicineNeisseria MeningitidisCarbohydrate-protein InteractionProtein BiosynthesisGlycosylation
We identified the genes encoding the proteins for the transport of glucose and maltose in Neisseria meningitidis strain 2C4-3. A mutant deleted for NMV_1892(glcP) no longer grew on glucose and deletion of NMV_0424(malY) prevented the utilization of maltose. We also purified and characterized glucokinase and α-phosphoglucomutase, which catalyze early catabolic steps of the two carbohydrates. N. meningitidis catabolizes the two carbohydrates either via the Entner-Doudoroff (ED) pathway or the pentose phosphate pathway, thereby forming glyceraldehyde-3-P and either pyruvate or fructose-6-P, respectively. We purified and characterized several key enzymes of the two pathways. The genes required for the transformation of glucose into gluconate-6-P and its further catabolism via the ED pathway are organized in two adjacent operons. N. meningitidis also contains genes encoding proteins which exhibit similarity to the gluconate transporter (NMV_2230) and gluconate kinase (NMV_2231) of Enterobacteriaceae and Firmicutes. However, gluconate might not be the real substrate of NMV_2230 because N. meningitidis was not able to grow on gluconate as the sole carbon source. Surprisingly, deletion of NMV_2230 stimulated growth in minimal medium in the presence and absence of glucose and drastically slowed the clearance of N. meningitidis cells from transgenic mice after intraperitoneal challenge.
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<i>NEISSERIA GONORRHOEAE</i> I
Douglas S. Kellogg, William L. Peacock, W. E. Deacon et al. · Journal of Bacteriology · 1963 · 1.2K citations · Full text
Functional genomics of Neisseria meningitidis pathogenesis
Yaohui Sun, Sharmila Bakshi, Ronald Chalmers et al. · Nature Medicine · 2000 · 199 citations · Full text