KpsF is the arabinose-5-phosphate isomerase required for 3-deoxy-D-manno-octulosonic acid biosynthesis and for both lipooligosaccharide assembly and capsular polysaccharide expression in Neisseria meningitidis.
作者： Yih-Ling Tzeng , Anup Datta , Christy Strole , V. S. Kumar Kolli , Matthew R. Birck
关键词: Biology 、 Neisseria meningitidis 、 Lipid A 、 Biochemistry 、 Transferase 、 Isomerase 、 Microbiology 、 Biosynthesis 、 Wild type 、 Arabinose 、 Mutant
摘要: Next Section Abstract We have identified and defined the function ofkpsF of Neisseria meningitidis homologues kpsF in encapsulated K1 K5Escherichia coli. KpsF was shown to be arabinose-5-phosphate isomerase, an enzyme not previously prokaryotes, that mediates interconversion ribulose 5-phosphate arabinose 5-phosphate. is required for 3-deoxy-d-manno-octulosonic acid (Kdo) biosynthesis inN. meningitidis. Mutation or gene encoding CMP-Kdo synthetase (kpsU/kdsB) resulted expression a lipooligosaccharide (LOS) structure contained only lipid A reduced capsule five invasive disease-associated meningococcal serogroups (A, B, C, Y, W-135). The step linking LOS Kdo production as wild type transferase (kdtA) mutant. Thus, addition assembly, capsular polysaccharide expression. Furthermore, N. meningitidis, unlike enteric Gram-negative bacteria, can survive synthesize unglycosylated A.
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