![]() Meanwhile, the mutagenesis experiments, including D124A, C208A, K211A and K211E, which displayed down-regulation on meropenem catalysis, proved the accuracy of our model.Īt present, there are no effective antibiotics against NDM-1 positive pathogen. We found that NDM-1 enzyme was highly potent to degrade carbapenem antibiotics, while mostly susceptible to tigecycline, which had the ability to slow down the hydrolysis velocity of meropenem by NDM-1. Furthermore, through biological experiments, we revealed the molecular basis for antibiotics catalysis of NDM-1 on the enzymatic level. ![]() In addition, the detailed analysis indicates that the more flexible and hydrophobic loop1, together with the evolution of more positive-charged loop2 leads to NDM-1 positive strain more potent and extensive in antibiotics resistance compared with other MBLs. It revealed that the hydrolytic mechanisms are highly conserved. In this study, we performed modeling studies to obtain its 3D structure and NDM-1/antibiotics complex. These can no longer be relied on to treat infections and therefore, NDM-1 now becomes potentially a major global health threat. A recent study reported that Klebsiella pneumonia NDM-1 positive strain or Escherichia coli NDM-1 positive strain was highly resistant to all antibiotics tested except tigecycline and colistin. ![]() The New Delhi Metallo-β-lactamase (NDM-1) was first reported in 2009 in a Swedish patient. ![]()
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