MOLECULAR CLONING, EXPRESSION AND PURIFICATION OF GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE (GAPDH-1) OF NEISSERIA MENINGITIDIS

S. A. TUNIO, N. J. OLDFIELD, K. G. WOOLDRIDGE, D. P. J. TURNER

Abstract


Glyceraldehyde  3-phosphate  dehydrogenases  (GAPDHs)  are  classical  cytoplasmic  glycolytic enzymes, which despite lacking predicted export signals, have also been shown to be expressed to the surface of a number of bacteria (some eukaryotic organisms), and shown to play additional roles in pathogesis of these organisms. N. meningitidis is an obligate human nasopharyngeal commensal which can cause life-threatening infections including septicaemia and meningitis. N. meningitidis genome possess two genes (GapA-1 and GapA-2) encoding GAPDH enzymes. This study was aimed to characterize GapA-1 of Neisseria meningitidis. Gene encoding GapA-1 was cloned, over-expressed, and purified to near homogeneity. In summary, GapA-1 was shown to be expressed and purified as a full-length protein


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