Nucleotide sequence of the penicillin-binding protein 2 gene of<i>Neisseria meningitidis</i>

Zhang, Qian-yun; Spratt, Brian G.

doi:10.1093/nar/17.13.5383

Cited by 13 publications

(6 citation statements)

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“…To date, four PBPs have been identified in Meningococcus B: PBP1, PBP2, PBP3 and PBP4. These proteins have predicted molecular masses of 88.9 kDa, 63.6 kDa 50.5 kDa and 34.1 kDa, respectively [25,26]. Hence we reasoned that the 62‐kDa PBP specifically retained during affinity chromatography is PBP2.…”

Section: Resultsmentioning

confidence: 99%

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

Jennings

Savino

Marchetti³

et al. 2002

European Journal of Biochemistry

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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 °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.

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Section: Resultsmentioning

confidence: 99%

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

Jennings

Savino

Marchetti³

et al. 2002

European Journal of Biochemistry

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“…The Gram-negative Neisseria gonorrhoeae has only four PBPs. PBP1 is analogous to Escherichia coli PBP1a (Ropp et al, 2002) and PBP2 is homologous to Escherichia coli PBP3 (Spratt & Cromie, 1988;Dowson et al, 1989;Zhang & Spratt, 1989). Neisseria gonorrhoeae incorporates new peptidoglycan through its divisome complex (Giesbrecht et al, 1976).…”

Section: Classification and Overview Of The Content In Pbps Of Selectmentioning

confidence: 99%

The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis

et al. 2008

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Penicillin-binding proteins (PBPs) have been scrutinized for over 40 years. Recent structural information on PBPs together with the ongoing long-term biochemical experimental investigations, and results from more recent techniques such as protein localization by green fluorescent protein-fusion immunofluorescence or double-hybrid assay, have brought our understanding of the last stages of the peptidoglycan biosynthesis to an outstanding level that allows a broad outlook on the properties of these enzymes. Details are emerging regarding the interaction between the peptidoglycan-synthesizing PBPs and the peptidoglycan, their mesh net-like product that surrounds and protects bacteria. This review focuses on the detailed structure of PBPs and their implication in peptidoglycan synthesis, maturation and recycling. An overview of the content in PBPs of some bacteria is provided with an emphasis on comparing the biochemical properties of homologous PBPs (orthologues) belonging to different bacteria.

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“…PBP fusions of subclass B2, however, are dispensable in some gram-negative bacteria. Neisseria meningitidis possesses a single PBP fusion of class B that belongs to subclass B3 (255). This PBP fusion may fulfil functions comparable to those of Eco2 and Eco3 in E. coli (14).…”

Section: Class B Pbp Fusions: Morphogenetic Apparatusmentioning

confidence: 99%

Biochemistry and Comparative Genomics of SxxK Superfamily Acyltransferases Offer a Clue to the Mycobacterial Paradox: Presence of Penicillin-Susceptible Target Proteins versus Lack of Efficiency of Penicillin as Therapeutic Agent

Goffin

Ghuysen

2002

Microbiol Mol Biol Rev

179

213

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The bacterial acyltransferases of the SxxK superfamily vary enormously in sequence and function, with conservation of particular amino acid groups and all-α and α/β folds. They occur as independent entities (free-standing polypeptides) and as modules linked to other polypeptides (protein fusions). They can be classified into three groups. The group I SxxK d,d-acyltransferases are ubiquitous in the bacterial world. They invariably bear the motifs SxxK, SxN(D), and KT(S)G. Anchored in the plasma membrane with the bulk of the polypeptide chain exposed on the outer face of it, they are implicated in the synthesis of wall peptidoglycans of the most frequently encountered (4→3) type. They are inactivated by penicillin and other β-lactam antibiotics acting as suicide carbonyl donors in the form of penicillin-binding proteins (PBPs). They are components of a morphogenetic apparatus which, as a whole, controls multiple parameters such as shape and size and allows the bacterial cells to enlarge and duplicate their particular pattern. Class A PBP fusions comprise a glycosyltransferase module fused to an SxxK acyltransferase of class A. Class B PBP fusions comprise a linker, i.e., protein recognition, module fused to an SxxK acyltransferase of class B. They ensure the remodeling of the (4→3) peptidoglycans in a cell cycle-dependent manner. The free-standing PBPs hydrolyze d,d peptide bonds. The group II SxxK acyltransferases frequently have a partially modified bar code, but the SxxK motif is invariant. They react with penicillin in various ways and illustrate the great plasticity of the catalytic centers. The secreted free-standing PBPs, the serine β-lactamases, and the penicillin sensors of several penicillin sensory transducers help the d,d-acyltransferases of group I escape penicillin action. The group III SxxK acyltransferases are indistinguishable from the PBP fusion proteins of group I in motifs and membrane topology, but they resist penicillin. They are referred to as Penr protein fusions. Plausible hypotheses are put forward on the roles that the Penr protein fusions, acting as l,d-acyltransferases, may play in the (3→3) peptidoglycan-synthesizing molecular machines. Shifting the wall peptidoglycan from the (4→3) type to the (3→3) type could help Mycobacterium tuberculosis and Mycobacterium leprae survive by making them penicillin resistant

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Nucleotide sequence of the penicillin-binding protein 2 gene ofNeisseria meningitidis

Cited by 13 publications

References 0 publications

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

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

The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis

Biochemistry and Comparative Genomics of SxxK Superfamily Acyltransferases Offer a Clue to the Mycobacterial Paradox: Presence of Penicillin-Susceptible Target Proteins versus Lack of Efficiency of Penicillin as Therapeutic Agent

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