Publications
288 results found
ZHANG QY, JONES DM, NIETO JAS, et al., 1990, GENETIC DIVERSITY OF PENICILLIN-BINDING PROTEIN-2 GENES OF PENICILLIN-RESISTANT STRAINS OF NEISSERIA-MENINGITIDIS REVEALED BY FINGERPRINTING OF AMPLIFIED DNA, ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, Vol: 34, Pages: 1523-1528, ISSN: 0066-4804
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- Citations: 57
BRANNIGAN JA, TIRODIMOS IA, ZHANG QY, et al., 1990, INSERTION OF AN EXTRA AMINO-ACID IS THE MAIN CAUSE OF THE LOW AFFINITY OF PENICILLIN-BINDING PROTEIN-2 IN PENICILLIN-RESISTANT STRAINS OF NEISSERIA-GONORRHOEAE, MOLECULAR MICROBIOLOGY, Vol: 4, Pages: 913-919, ISSN: 0950-382X
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- Citations: 82
BROOMESMITH JK, BOWLER LD, SPRATT BG, 1989, A SIMPLE METHOD FOR MAXIMIZING THE YIELDS OF MEMBRANE AND EXPORTED PROTEINS EXPRESSED IN ESCHERICHIA-COLI, MOLECULAR MICROBIOLOGY, Vol: 3, Pages: 1813-1817, ISSN: 0950-382X
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- Citations: 5
DOWSON CG, HUTCHISON A, BRANNIGAN JA, et al., 1989, Horizontal transfer of penicillin-binding protein genes in penicillin-resistant clinical isolates of Streptococcus pneumoniae, Proceedings of the National Academy of Sciences of the United States of America, Vol: 86, Pages: 8842-8846, ISSN: 1091-6490
Resistance to penicillin in clinical isolates ofStreptococcus pneumoniae has occurred by the development ofaltered penicillin-binding proteins (PBPs) that have greatlydecreased affinity for the antibiotic. We have investigated theorigins of penicillin-resistant strains by comparing the sequencesof the transpeptidase domain of PBP2B from 6 penicillin-sensitiveand 14 penicillin-resistant strains. In additionwe have sequenced part of the amylomaltase gene from 2 of thesensitive and 6 of the resistant strains. The sequences of theamylomaltase gene of all of the strains and of the PBP2B geneof the penicillin-sensitive strains show that S. pneumoniae isgenetically very uniform. In contrast the PBP2B genes of thepenicillin-resistant strains show -14% sequence divergencefrom those of the penicillin-sensitive strains and the developmentof penicillin resistance has involved the replacement,presumably by transformation, of the original PBP2B gene bya homologous gene from an unknown source. This genetic eventhas occurred on at least two occasions, involving differentsources, to produce the two classes of altered PBP2B genesfound in penicillin-resistant strains of S. pneumoniae. There isconsiderable variation among the PBP2B genes of the resistantstrains that may have arisen by secondary transformationevents accompanied by nismatch repair subsequent to theiroriginal introductions into S. pneumoniae.
SPRATT BG, ZHANG QY, JONES DM, et al., 1989, Recruitment of a penicillin-binding protein gene from Neisseria flavescens during the emergence of penicillin resistance in Neisseria meningitidis, Proceedings of the National Academy of Sciences of the United States of America, Vol: 86, Pages: 8988-8992, ISSN: 1091-6490
Non-f8-lactamase-producing, penicillin-resistantstrains of Neisseria meningildis produce altered forms ofpenicillin-binding protein 2 that have decreased affinity forpenicillin. The sequence of the penicillin-binding protein 2 gene(penA) from a penicillin-resistant strain of N. meningitidis wascompared to the sequence of the same gene from penicillinsensitivestrains and from penicillin-sensitive and penicillinresistantstrains of Neisseria gonorrhoeae. The penA genes frompenicillin-sensitive strains ofN. gonorrhoeae and N. meningitdiswere 98% identical. The gene from the penicillin-resistant strainof N. meningitis consisted of regions that were almost identicalto the corresponding regions in the penicillin-sensitive strains(<0.2% divergence) and two regions that were very differentfrom them (-22% divergence). The two blocks of alteredsequence have arisen by the replacement of meningococcalsequences with the corresponding regions from the penA gene ofNeisseria flavescens and result in an altered form of penicillinbindingprotein 2 that contains 44 amino acid substitutions and1 amino acid insertion compared to penicillin-binding protein 2of penicillin-sensitive strains of N. meningitddis. A similar introductionof part of the penA gene of N. flavescens, or a verysimilar commensal Neisseria species, appears to have occurredindependently during the development of altered penA genes innon-,B-lactamase-producing penicillin-resistant strains of N.gonorrhoeae.
DOWSON CG, HUTCHISON A, SPRATT BG, 1989, NUCLEOTIDE-SEQUENCE OF THE PENICILLIN-BINDING PROTEIN-2B GENE OF STREPTOCOCCUS-PNEUMONIAE STRAIN-R6, NUCLEIC ACIDS RESEARCH, Vol: 17, Pages: 7518-7518, ISSN: 0305-1048
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- Citations: 45
Dowson CG, Hutchison A, Spratt BG, 1989, Nucleotide sequence of the penicillin-binding protein 2B gene of Streptococcus pneumoniae strain R6., Nucleic Acids Res, Vol: 17, ISSN: 0305-1048
BOWLER LD, SPRATT BG, 1989, MEMBRANE TOPOLOGY OF PENICILLIN-BINDING PROTEIN-3 OF ESCHERICHIA-COLI, MOLECULAR MICROBIOLOGY, Vol: 3, Pages: 1277-1286, ISSN: 0950-382X
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- Citations: 56
ZHANG QY, SPRATT BG, 1989, NUCLEOTIDE-SEQUENCE OF THE PENICILLIN-BINDING PROTEIN-2 GENE OF NEISSERIA-MENINGITIDIS, NUCLEIC ACIDS RESEARCH, Vol: 17, Pages: 5383-5383, ISSN: 0305-1048
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- Citations: 11
DENBLAAUWEN T, WIENTJES FB, KOLK AHJ, et al., 1989, PREPARATION AND CHARACTERIZATION OF MONOCLONAL-ANTIBODIES AGAINST NATIVE MEMBRANE-BOUND PENICILLIN-BINDING PROTEIN-1B OF ESCHERICHIA-COLI, JOURNAL OF BACTERIOLOGY, Vol: 171, Pages: 1394-1401, ISSN: 0021-9193
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- Citations: 13
DOWSON CG, JEPHCOTT AE, GOUGH KR, et al., 1989, PENICILLIN-BINDING PROTEIN 2 GENES OF NON-BETA-LACTAMASE-PRODUCING, PENICILLIN-RESISTANT STRAINS OF NEISSERIA-GONORRHOEAE, MOLECULAR MICROBIOLOGY, Vol: 3, Pages: 35-41, ISSN: 0950-382X
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- Citations: 52
DOWSON CG, HUTCHISON A, SPRATT BG, 1989, EXTENSIVE REMODELING OF THE TRANSPEPTIDASE DOMAIN OF PENICILLIN-BINDING PROTEIN-2B OF A PENICILLIN-RESISTANT SOUTH-AFRICAN ISOLATE OF STREPTOCOCCUS-PNEUMONIAE, MOLECULAR MICROBIOLOGY, Vol: 3, Pages: 95-102, ISSN: 0950-382X
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- Citations: 143
TASCHNER PEM, YPENBURG N, SPRATT BG, et al., 1988, AN AMINO-ACID SUBSTITUTION IN PENICILLIN-BINDING PROTEIN-3 CREATES POINTED POLAR CAPS IN ESCHERICHIA-COLI, JOURNAL OF BACTERIOLOGY, Vol: 170, Pages: 4828-4837, ISSN: 0021-9193
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- Citations: 21
SPRATT BG, CROMIE KD, 1988, PENICILLIN-BINDING PROTEINS OF GRAM-NEGATIVE BACTERIA, REVIEWS OF INFECTIOUS DISEASES, Vol: 10, Pages: 699-711, ISSN: 0162-0886
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- Citations: 170
SPRATT BG, 1988, HYBRID PENICILLIN-BINDING PROTEINS IN PENICILLIN-RESISTANT STRAINS OF NEISSERIA-GONORRHOEAE, NATURE, Vol: 332, Pages: 173-176, ISSN: 0028-0836
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- Citations: 184
Broome-Smith JK, Ioannidis I, Edelman A, et al., 1988, Nucleotide sequences of the penicillin-binding protein 5 and 6 genes of Escherichia coli., Nucleic Acids Res, Vol: 16, ISSN: 0305-1048
BROOMESMITH JK, IOANNIDIS I, EDELMAN A, et al., 1988, NUCLEOTIDE-SEQUENCES OF THE PENICILLIN-BINDING PROTEIN 5 AND 6 GENES OF ESCHERICHIA-COLI, NUCLEIC ACIDS RESEARCH, Vol: 16, Pages: 1617-1617, ISSN: 0305-1048
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- Citations: 58
Spratt BG, 1988, Genetics and control of β-lactamase expression, Clinical Infectious Diseases, Vol: 10, Pages: 780-781, ISSN: 1058-4838
EDELMAN A, BOWLER L, BROOMESMITH JK, et al., 1987, USE OF A BETA-LACTAMASE FUSION VECTOR TO INVESTIGATE THE ORGANIZATION OF PENICILLIN-BINDING PROTEIN 1B IN THE CYTOPLASMIC MEMBRANE OF ESCHERICHIA-COLI, MOLECULAR MICROBIOLOGY, Vol: 1, Pages: 101-106, ISSN: 0950-382X
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- Citations: 45
BEGG KJ, SPRATT BG, DONACHIE WD, 1986, INTERACTION BETWEEN MEMBRANE-PROTEINS PBP3 AND RODA IS REQUIRED FOR NORMAL-CELL SHAPE AND DIVISION IN ESCHERICHIA-COLI, JOURNAL OF BACTERIOLOGY, Vol: 167, Pages: 1004-1008, ISSN: 0021-9193
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- Citations: 47
Ishino F, Park W, Tomioka S, et al., 1986, Peptidoglycan synthetic activities in membranes of Escherichia coli caused by overproduction of penicillin-binding protein 2 and rodA protein., J Biol Chem, Vol: 261, Pages: 7024-7031, ISSN: 0021-9258
Penicillin-binding protein (PBP)-2 and the RodA protein are known to function in determining the rod shape of Escherichia coli cells. Peptidoglycan biosynthetic reactions that required these two proteins were demonstrated in the membrane fraction prepared from an E. coli strain that overproduced both of these two proteins and which lacked PBP-1B activity (the major peptidoglycan synthetase activity in the normal E. coli membranes). The cross-linked peptidoglycan was synthesized from UDP-N-acetylmuramylpentapeptide and UDP-N-acetylglucosamine in the presence of a high concentration of cefmetazole that inhibited all of PBPs except PBP-2. The peptidoglycan was synthesized via a lipid intermediate and showed up to 30% cross-linking. The cross-linking reaction was strongly inhibited by the amidinopenicillin, mecillinam, and by other beta-lactam antibiotics that have a high affinity for PBP-2, but not by beta-lactams that had very low affinity for PBP-2. The formation of peptidoglycan required the presence of high levels of both PBP-2 and the RodA protein in the membranes, but it is unclear which of the two proteins was primarily responsible for the extension of the glycan chains (transglycosylation). However, the sensitivity of the cross-linking reaction to specific beta-lactam antibiotics strongly suggested that it was catalyzed by PBP-2. The transglycosylase activity of the membranes was sensitive to enramycin and vancomycin and was unusual in being stimulated greatly by a high concentration of a chelating agent.
ISHINO F, PARK W, TOMIOKA S, et al., 1986, THE FUNCTIONAL BIOSYNTHESIS OF BACTERIAL-CELL WALL PEPTIDOGLYCAN .2. PEPTIDOGLYCAN SYNTHETIC ACTIVITIES IN MEMBRANES OF ESCHERICHIA-COLI CAUSED BY OVERPRODUCTION OF PENICILLIN-BINDING PROTEIN-2 AND RODA PROTEIN, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 261, Pages: 7024-7031, ISSN: 0021-9258
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- Citations: 121
SPRATT BG, HEDGE PJ, HEESEN ST, et al., 1986, KANAMYCIN-RESISTANT VECTORS THAT ARE ANALOGS OF PLASMIDS PUC8, PUC9, PEMBL8 AND PEMBL9, GENE, Vol: 41, Pages: 337-342, ISSN: 0378-1119
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- Citations: 429
BROOMESMITH JK, SPRATT BG, 1986, A VECTOR FOR THE CONSTRUCTION OF TRANSLATIONAL FUSIONS TO TEM BETA-LACTAMASE AND THE ANALYSIS OF PROTEIN EXPORT SIGNALS AND MEMBRANE-PROTEIN TOPOLOGY, GENE, Vol: 49, Pages: 341-349, ISSN: 0378-1119
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- Citations: 131
KECK W, GLAUNER B, SCHWARZ U, et al., 1985, Sequences of the active-site peptides of three of the high-Mr penicillin-binding proteins of Escherichia coli K-12, Proceedings of the National Academy of Sciences of the United States of America, Vol: 82, Pages: 1999-2003, ISSN: 1091-6490
The amino acid compositions of the radioactivepeptides obtained from trypsin digestion of ['4C]benzylpenicillin-labeledpenicillin-binding proteins (PBPs) 1A, 1B,and 3 of Escherichia coli have been obtained. Complete digestionof these peptides with a combination of aminopeptidase Mand carboxypeptidase Y showed that benzylpenicillin wasbound to a serine residue in each of these proteins. Comparisonof the compositions of the penicillin-labeled peptides withthe complete amino acid sequences of PBPs 1A, 1B, and 3showed that the acylated serine occurs near the middle of eachof the proteins, within the conserved sequence Gly-Ser-XaaXaa-Lys-Pro.The sequence around the acylated serine of thesehigh Mr PBPs shows little similarity to that around the acylatedserine of the low-Mr PBPs (D-alanine carboxypeptidases) orof the class A or class C 3-lactamases, except that in all ofthese enzymes which interact with penicillin the acylated serineresidue occurs within the sequence Ser-Xaa-Xaa-Lys.
BROOMESMITH JK, EDELMAN A, YOUSIF S, et al., 1985, THE NUCLEOTIDE-SEQUENCES OF THE PONA AND PONB GENES ENCODING PENICILLIN-BINDING PROTEINS 1A AND 1B OF ESCHERICHIA-COLI-K12, EUROPEAN JOURNAL OF BIOCHEMISTRY, Vol: 147, Pages: 437-446, ISSN: 0014-2956
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- Citations: 93
BROOMESMITH JK, HEDGE PJ, SPRATT BG, 1985, PRODUCTION OF THIOL-PENICILLIN-BINDING PROTEIN-3 OF ESCHERICHIA-COLI USING A 2 PRIMER METHOD OF SITE-DIRECTED MUTAGENESIS, EMBO JOURNAL, Vol: 4, Pages: 231-235, ISSN: 0261-4189
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- Citations: 33
YOUSIF SY, BROOMESMITH JK, SPRATT BG, 1985, LYSIS OF ESCHERICHIA-COLI BY BETA-LACTAM ANTIBIOTICS - DELETION ANALYSIS OF THE ROLE OF PENICILLIN-BINDING PROTEIN-1A AND PROTEIN-1B, JOURNAL OF GENERAL MICROBIOLOGY, Vol: 131, Pages: 2839-2845, ISSN: 0022-1287
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- Citations: 144
HEDGE PJ, SPRATT BG, 1985, AMINO-ACID SUBSTITUTIONS THAT REDUCE THE AFFINITY OF PENICILLIN-BINDING PROTEIN-3 OF ESCHERICHIA-COLI FOR CEPHALEXIN, EUROPEAN JOURNAL OF BIOCHEMISTRY, Vol: 151, Pages: 111-121, ISSN: 0014-2956
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- Citations: 46
HEDGE PJ, SPRATT BG, 1985, RESISTANCE TO BETA-LACTAM ANTIBIOTICS BY RE-MODELLING THE ACTIVE-SITE OF AN ESCHERICHIA-COLI PENICILLIN-BINDING PROTEIN, NATURE, Vol: 318, Pages: 478-480, ISSN: 0028-0836
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- Citations: 47
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