scholarly journals glmM Operon and Methicillin-ResistantglmM Suppressor Mutants in Staphylococcus aureus

1999 ◽  
Vol 43 (2) ◽  
pp. 240-245 ◽  
Author(s):  
Philipp Glanzmann ◽  
John Gustafson ◽  
Hithoshi Komatsuzawa ◽  
Kouji Ohta ◽  
Brigitte Berger-Bächi
Keyword(s):  
Staphylococcus Aureus ◽  
Binding Proteins ◽  
Methicillin Resistance ◽  
Alternative Pathway ◽  
Suppressor Mutation ◽  
Methicillin Resistant ◽  
Penicillin Binding Proteins ◽  
Suppressor Mutants ◽  
Selection For ◽  
Monocistronic Transcript

ABSTRACT The Staphylococcus aureus phosphoglucosamine mutase gene glmM was shown to be the last gene of a three-cistron operon, orf1-orf2-glmM. One transcriptional start was identified upstream of orf1, and a second start producing a monocistronic transcript was identified upstream of glmM. Disruption of glmM abolished GlmM production, decreased methicillin resistance, and resulted in teicoplanin hypersusceptibility without affecting the production of the endogenous penicillin-binding proteins and PBP 2′. Complementation of the glmM mutation by the complete glmMoperon restored both methicillin resistance and normal teicoplanin susceptibility. In contrast, a highly methicillin-resistant suppressor mutant obtained by selection for growth in the presence of methicillin remained GlmM deficient and teicoplanin hypersusceptible. The suppressor mutation was not linked to the glmM operon but was correlated with decreased autolysis and increased production of a 49-kDa protein, suggesting that there is an alternative pathway for glucosamine-1-phosphate synthesis in S. aureus.

scholarly journals Susceptibility of Methicillin-Resistant Staphylococcus aureus to Five Quinazolinone Antibacterials

2019 ◽  
Vol 64 (1) ◽  
Author(s):  
Sara Ceballos ◽  
Choon Kim ◽  
Yuanyuan Qian ◽  
Shahriar Mobashery ◽  
Mayland Chang ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Binding Proteins ◽  
Methicillin Resistant Staphylococcus Aureus ◽  
Methicillin Resistant ◽  
Content Type ◽  
Penicillin Binding Proteins

ABSTRACT The in vitro activities of five quinazolinone antibacterials, compounds Q1 to Q5, were tested against 210 strains of methicillin-resistant Staphylococcus aureus (MRSA). The MIC50/MIC90 values (in μg/ml) were as follows: Q1, 0.5/2; Q2, 1/4; Q3, 2/4; Q4, 0.06/0.25; and Q5, 0.125/0.5. Several strains with high MIC values (from 8 to >32 μg/ml) for some of these compounds exhibited amino acid changes in the penicillin-binding proteins, which are targeted by these antibacterials.

Cloning and characterization of the fmt gene which affects the methicillin resistance level and autolysis in the presence of triton X-100 in methicillin-resistant Staphylococcus aureus.

1997 ◽  
Vol 41 (11) ◽  
pp. 2355-2361 ◽  
Author(s):  
H Komatsuzawa ◽  
M Sugai ◽  
K Ohta ◽  
T Fujiwara ◽  
S Nakashima ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Binding Proteins ◽  
Methicillin Resistant Staphylococcus Aureus ◽  
Insertion Mutant ◽  
Resistance Level ◽  
Methicillin Resistant ◽  
Penicillin Binding Proteins ◽  
Oxacillin Resistance ◽  
Mrsa Strains ◽  
Triton X

In methicillin-resistant Staphylococcus aureus (MRSA) strains, Triton X-100 reduced the oxacillin resistance level, although the degree of reduction varied from strain to strain. To study the responses of MRSA strains to Triton X-100, we isolated a Tn551 insertion mutant of the COL strain that became more susceptible to oxacillin in the presence of 0.02% Triton X-100. The Tn551 insertion of the mutant was transduced back to the parent strain, other MRSA strains (strains KSA8 and NCTC 10443), and methicillin-susceptible strain RN450. All transductants of MRSA strains had reduced levels of resistance to oxacillin in the presence of 0.02% Triton X-100, while those of RN450 did not. Tn551 mutants of KSA8 and NCTC 10443 also had reduced levels of resistance in the absence of 0.02% Triton X-100. The autolysis rates of the transductants in the presence of 0.02% Triton X-100 were significantly increased. Amino acid analysis of peptidoglycan and testing of heat-inactivated cells for their susceptibilities to several bacteriolytic enzymes showed that there were no significant differences between the parents and the respective Tn551 mutants. The Tn551 insertion site mapped at a location different from the previously identified fem and llm sites. Cloning and sequencing showed that Tn551 had inserted at the C-terminal region of a novel gene designated fmt. The putative Fmt protein showed a hydropathy pattern similar to that of S. aureus penicillin-binding proteins and contained two of the three conserved motifs shared by penicillin-binding proteins and beta-lactamases, suggesting that fmt may be involved in cell wall synthesis.

Prevalence and Molecular Characterization of Methicillin-Resistant Staphylococcus aureus in Foods of Animal Origin, Turkey

2016 ◽  
Vol 79 (11) ◽  
pp. 1990-1994 ◽  
Author(s):  
BELGİN SİIRİKEN ◽  
TUBA YILDIRIM ◽  
AKİF KORAY GÜNEY ◽  
İRFAN EROL ◽  
BELMA DURUPINAR
Keyword(s):  
Staphylococcus Aureus ◽  
Methicillin Resistant Staphylococcus Aureus ◽  
Methicillin Resistance ◽  
Meca Gene ◽  
Raw Milk ◽  
Animal Origin ◽  
Methicillin Resistant ◽  
Selection For

ABSTRACT In the present study, 175 coagulase-positive Staphylococcus (CPS) isolates recovered from samples of beef (n = 110), raw milk n = 56), and fish (n = 9) were analyzed for methicillin resistance using MIC and PCR assays. Methicillin-resistant (MR) Staphylococcus aureus (SA) isolates were then characterized using pulsed-field gel electrophoresis (PFGE). According to findings, 62 (35.4%) of the isolates (44 from beef, 9 from milk, and 9 from fish) were identified as S. aureus based on the presence of the nuc gene. MRCPS was detected in 18 (10.3%) of 175 CPS isolates based on the presence of the mecA gene. Among these isolates, 15 (24.2%) were MRSA: 4 (26.7%) from beef, 2 (13.3%) from milk, and 9 (60%) from fish. However, based on the MIC assay, 21 (12.0%) of the CPS isolates (1 from beef, 15 from milk, and 5 from fish) were MRCPS, indicating a discrepancy between the results of these two methods. The PFGE results indicated genetic heterogeneity of the isolates; six PFGE clusters were found. These results confirm that MRSA is present in foods of animal origin, which is a concern to human health, and indicate the importance of method selection for determination of methicillin resistance. The identity of MR isolates should be verified by PCR to obtain more reliable results.

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