Selective inhibition of penicillin-binding proteins and its effects on growth and architecture of Staphylococcus aureus |
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| Institution: | 1. Universidad Nacional Autónoma de México, Facultad de Medicina, Departamento de Bioquímica, Circuito Escolar S/N, Ciudad Universitaria, CDMX, Mexico;2. Human Technopole, Palazzo Italia, Viale Rita Levi‑Montalcini, 1, 20157 Milan, Italy;3. MRC Laboratory of Molecular Biology, Structural Studies Division, Francis Crick Avenue, CB2 0QH Cambridge, England;1. The Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, 08826, Republic of Korea;2. Department of Pharmacy, College of Pharmacy and Institute of Pharmaceutical Sciences, CHA University, Pocheon-si, 11160, Gyeonggi-Do, Republic of Korea;1. Department of Crystallography and Structural Biology, Institute of Physical Chemistry “Rocasolano”, CSIC, 28006 Madrid, Spain;2. Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA;3. Structural Biology Programme, Spanish National Cancer Research Center (CNIO), 28029 Madrid, Spain |
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| Abstract: | We found that the three high molecular weight penicillin-binding proteins (PBP) 1, 2, and 3 of Staphylococcus aureus could be blocked by the β-lactam antibiotics imipenem, cefotaxime, and mecillinam, respectively. The inhibition of any of these PBPs was not sufficient for an antibacterial effect. Even the simultaneous blocking of PBPs 2 and 3, previously supposed to be the lethal targets of β-lactam antibiotics, did not induce bacteriolysis, nor did the combined saturation of PBPs 2, 3, and 4. Instead, PBP 1 seems to play a key role, because on one hand the combined inhibition of PBP 1 with any of the other high molecular weight PBPs led to bacteriolysis, on the other hand, only inhibition of PBP 1 led to a loss of the ‘splitting system’ of the staphylococcal cross wall, similar to that observed in penicillin G-treated cells earlier. |
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