Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Jennings, G.T. et al.

Jennings, Savino, Marchetti, Aricò, Kast, Baldi, Ursinus, Höltje, Nicholas, Rappuoli, Grandi,

GNA33 from Neisseria meningitidis serogroup B encodes a membrane-bound lytic transglycosylase (MltA).

In a previous study, we used the genome of serogroup B Meningococcus to identify novel vaccine candidates. One of these molecules, GNA33, is well conserved among Meningococcus B strains, other Meningococcus serogroups and Gonococcus and induces bactericidal antibodies as a result of being a mimetic antigen of the PorA epitope P1. 2. GNA33 encodes a 48-kDa lipoprotein that is 34.5% identical with membrane- bound lytic transglycosylase A (MltA) from Escherichia coli. In this study, we expressed GNA33, i.e. Meningococcus MltA, as a lipoprotein in E. coli. The lipoprotein nature of recombinant MltA was demonstrated by incorporation of [3H]palmitate. MltA lipoprotein was purified to homogeneity from E. coli membranes by cation-exchange chromatography. Muramidase activity was confirmed when MltA was shown to degrade insoluble murein sacculi and unsubstituted glycan strands. HPLC analysis demonstrated the formation of 1,6-anhydrodisaccharide tripeptide and tetrapeptide reaction products, confirming that the protein is a lytic transglycosylase. Optimal muramidase activity was observed at pH 5.5 and 37 degrees C and enhanced by Mg2+, Mn2+ and Ca2+. The addition of Ni2+ and EDTA had no significant effect on activity, whereas Zn2+ inhibited activity. Triton X-100 stimulated activity 5.1-fold. Affinity chromatography indicated that MltA interacts with penicillin-binding protein 2 from Meningococcus B, and, like MltA from E. coli, may form part of a multienzyme complex.[1]

References

GNA33 from Neisseria meningitidis serogroup B encodes a membrane-bound lytic transglycosylase (MltA). Jennings, G.T., Savino, S., Marchetti, E., Aricò, B., Kast, T., Baldi, L., Ursinus, A., Höltje, J.V., Nicholas, R.A., Rappuoli, R., Grandi, G. Eur. J. Biochem. (2002) [Pubmed]

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