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- 1. β-ラクタム系抗生物質：作用機序、耐性および有害作用 beta lactam antibiotics mechanisms of action and resistance and adverse effects
- 2. メチシリン耐性黄色ブドウ球菌の微生物学 microbiology of methicillin resistant staphylococcus aureus
- 3. コアグラーゼ陰性ブドウ球菌による感染症の治療 treatment of infections due to coagulase negative staphylococci
- 4. 腸球菌における抗菌薬耐性の機構 mechanisms of antibiotic resistance in enterococci
- 5. 連鎖球菌毒素性ショック症候群の治療 treatment of streptococcal toxic shock syndrome
- A highly unstable transcript makes expression of the CwlO D,L-endopeptidase responsive to growth conditions in Bacillus subtilis.
- Noone D, Salzberg LI, Botella E, Bäsell K, Becher D, Antelmann H, Devine KM.SourceSmurfit Institute of Genetics, Trinity College Dublin, Dublin 2 Ireland.
- Journal of bacteriology.J Bacteriol.2013 Oct 25. [Epub ahead of print]
- The B. subtilis cell wall is a dynamic structure, composed of peptidoglycan and teichoic acid that is continually remodeled during growth. Remodelling is effected by the combined activities of penicillin binding proteins and autolysins that participate in the synthesis and turnover peptidoglycan res
- PMID 24163346
- Label-free Quantitative Proteomics Analysis of Antibiotic Response in Staphylococcus aureus to Oxacillin.
- Liu X, Hu Y, Pai PJ, Chen D, Lam H.AbstractMethicillin-resistant Staphylococcus aureus (MRSA) is the leading cause of fatal bacterial infections in hospitals and has become a global health threat. Although the resistance mechanisms of β-lactam antibiotics have been studied for decades, there are few attempts at systems-wide investigations into how the bacteria respond to antibiotic stress. In this paper, spectral counting-based label-free quantitative proteomics has been applied to study global responses in MRSA and methicillin-susceptible S. aureus (MSSA) treated with sub-inhibitory doses of oxacillin, a model beta-lactam antibiotic. We developed a simple and easily repeated sample preparation procedure that is effective for extracting surface-associated proteins. On average, 1025 and 1013 proteins were identified at a false discovery rate threshold of 0.01, for the untreated group of MRSA and MSSA. Upon treatment with oxacillin, 81 proteins (65 up-regulated, 16 down-regulated) were shown differentially expressed in MRSA (p<0.05). In comparison, 225 proteins (162 up-regulated, 63 down-regulated) were shown differentially expressed in oxacillin-treated MSSA. Beta-lactamase and penicillin-binding protein 2a were observed up-regulated uniquely in oxacillin-treated MRSA, which is consistent with the known beta-lactam resistance mechanisms of S. aureus. More interestingly, the peptidoglycan biosynthesis pathway and the pantothenate and CoA biosynthesis pathway were found up-regulated in both oxacillin-treated MRSA and MSSA, and a series of energy metabolism pathways were up-regulated uniquely in oxacillin-treated MSSA. These new data offer a more complete view of the proteome changes in bacteria in response to the antibiotic. This report is first in using label-free quantitative proteomics to study beta-lactam antibiotic responses in S. aureus.
- Journal of proteome research.J Proteome Res.2013 Oct 24. [Epub ahead of print]
- Methicillin-resistant Staphylococcus aureus (MRSA) is the leading cause of fatal bacterial infections in hospitals and has become a global health threat. Although the resistance mechanisms of β-lactam antibiotics have been studied for decades, there are few attempts at systems-wide investigations i
- PMID 24156611
- Binding of (5S)-Penicilloic Acid to Penicillin Binding Protein 3.
- van Berkel SS, Nettleship JE, Leung IK, Brem J, Choi H, Stuart DI, Claridge TD, McDonough MA, Owens RJ, Ren J, Schofield CJ.SourceChemistry Research Laboratory, University of Oxford , 12 Mansfield Road, Oxford OX1 3TA, U.K.
- ACS chemical biology.ACS Chem Biol.2013 Oct 18;8(10):2112-6. doi: 10.1021/cb400200h. Epub 2013 Aug 15.
- β-Lactam antibiotics react with penicillin binding proteins (PBPs) to form relatively stable acyl-enzyme complexes. We describe structures derived from the reaction of piperacillin with PBP3 (Pseudomonas aeruginosa) including not only the anticipated acyl-enzyme complex but also an unprecedented co
- PMID 23899657
- Synthetic Lethality of the lytE cwlO Genotype in Bacillus subtilis Is Caused by Lack of D,L-Endopeptidase Activity at the Lateral Cell Wall
- Hashimoto Masayuki,Ooiwa Seika,Sekiguchi Junichi
- JOURNAL OF BACTERIOLOGY 194(4), 796-803, 2012-02
- … Although peptidoglycan biosynthesis by penicillin-binding proteins is well studied, few studies have described peptidoglycan disassembly, which is necessary for a dynamic structure that allows cell growth. … Only the chimeric proteins that were enzymatically active and localized to the sidewall were able to suppress the synthetic lethality, suggesting that the lack of D,L-endopeptidase activity at the cylindrical part of the cell leads to a growth defect. …
- NAID 80022308460
- Correlation of the antimicrobial activity of ME1036 with its binding affinities to the penicillin-binding proteins from Streptococcus pneumoniae strains
- HIRAI Yoko,TAKAHATA Sho,YAMADA Keiko,IDA Takashi,MAEBASHI Kazunori
- Journal of antibiotics 64(11), 741-746, 2011-11-25
- NAID 10030640729
- Identification of the Catalytic Residues of Carboxylesterase from Arthrobacter globiformis by Diisopropyl Fluorophosphate-Labeling and Site-Directed Mutagenesis
- Nishizawa Masako,Yabusaki Yoshiyasu,Kanaoka Masaharu
- Bioscience, biotechnology, and biochemistry 75(1), 89-94, 2011-01-23
- … The further comparison of endopeptidase-digested fragments between native and DFP-labeled esterase by fast atom bombardment mass spectrometric (FAB-MS) analysis as well as site-directed mutagenesis indicated that Ser59 in the consensus sequence Ser-X-X-Lys, which is conserved exclusively in penicillin-binding proteins and some esterases, served as a catalytic nucleophile. …
- NAID 10027896792
- Exploring the Structure The PDB entry 1hvb shows a penicillin-binding protein in action. The enzyme is a D-alanyl-D-alanine carboxypeptidase/transpeptidase that creates a crosslink between two chains in the peptidoglycan ...
- 細菌の破壊 低濃度でペニシリンが投与された時、細菌の細胞は形が変化し長い繊維を伸ばす。投与量が増加するにつれ、細胞表面は完全性を失い、ふくれて膨張し最終的には破裂する。ペニシリンは酵素に対して攻撃するが、その酵素 ...
- Penicillin-binding proteins