Figures & data
Table 1 Demographic Data of Patients Included in This Study
Table 2 Summary of MIC Results Among the 22 M. odoratimimus Isolates
Table 3 Primers for the Carbapenemase Gene Sequencing Analysis
Figure 1 PFGE image of the M. odoratimimus strains. The 22 isolates belonged to six distant PFGE groups (types A–F) by using a cut-off of 80% similarity (Δurology department, □biliary and pancreatic surgery department).
![Figure 1 PFGE image of the M. odoratimimus strains. The 22 isolates belonged to six distant PFGE groups (types A–F) by using a cut-off of 80% similarity (Δurology department, □biliary and pancreatic surgery department).](/cms/asset/19ed3018-2b94-435a-b5ff-6bc0770ef57f/didr_a_251626_f0001_b.jpg)
Figure 2 MALDI-TOF MS dendrograms for 22 isolates. Using PCA cluster analysis to construct a dendrogram, MALDI-TOF MS generated four clusters (types I, II, III, and IV) with a cut-off value of 3.
![Figure 2 MALDI-TOF MS dendrograms for 22 isolates. Using PCA cluster analysis to construct a dendrogram, MALDI-TOF MS generated four clusters (types I, II, III, and IV) with a cut-off value of 3.](/cms/asset/107c4c82-46fb-42e5-897c-b35cefc62a4d/didr_a_251626_f0002_c.jpg)
Figure 3 The level of resistance to meropenem between the clinical isolates of MUS-1 from the biliary and pancreatic surgery ward and MUS-3 from the urology ward (P < 0.05).
![Figure 3 The level of resistance to meropenem between the clinical isolates of MUS-1 from the biliary and pancreatic surgery ward and MUS-3 from the urology ward (P < 0.05).](/cms/asset/289c0063-8ddf-40a3-8a64-301c69cf21a9/didr_a_251626_f0003_c.jpg)
Figure 4 The secondary and tertiary structure prediction of MUS-1 wild-type and V60A-mutant proteins using bioinformatics tools. (A) Secondary structure prediction of the MUS wild-type protein by PSIPRED. (B) Secondary structure prediction of the MUS-3 (V60A) mutant protein by PSIPRED. A beta-strand is predicted to form at the mutation position (red triangle). (C) Tertiary structure prediction of the MUS protein by RaptorX, with the mutation marked inside (black oval).
![Figure 4 The secondary and tertiary structure prediction of MUS-1 wild-type and V60A-mutant proteins using bioinformatics tools. (A) Secondary structure prediction of the MUS wild-type protein by PSIPRED. (B) Secondary structure prediction of the MUS-3 (V60A) mutant protein by PSIPRED. A beta-strand is predicted to form at the mutation position (red triangle). (C) Tertiary structure prediction of the MUS protein by RaptorX, with the mutation marked inside (black oval).](/cms/asset/11606032-1742-4b52-852a-884d8f09cb28/didr_a_251626_f0004_c.jpg)