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Article

Effects of two novel amino acid substitutions on the penicillin binding properties of the PBP5 C‑terminal from Enterococcus faecium

  • Authors:
    • Chengjiang Zhou
    • Haiying Niu
    • Hui Yu
    • Lishe Zhou
    • Zhanli Wang
  • View Affiliations / Copyright

    Affiliations: Department of Medical and Cell Biology, Baotou Medical College, Baotou 014010, P.R. China, Clinical Laboratory, The First Affiliated Hospital, Baotou Medical College, Baotou 014010, P.R. China, Clinical Laboratory, The Second Affiliated Hospital, Baotou Medical College, Baotou 014010, P.R. China
  • Pages: 5281-5285
    |
    Published online on: July 8, 2015
       https://doi.org/10.3892/mmr.2015.4057
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Abstract

The low‑affinity penicillin‑binding protein (PBP)5 is responsible for resistance to β‑lactam antibiotics in Enterococcus faecium. (E. faecium). In order to evaluate more fully the potential of this species for the development of resistance to β-lactam antibiotics, the present study aimed to examine the extent of penicillin-binding protein (PBP) variations in a collection of clinical E. faecium isolates. In the present study, the C‑terminal domain of PBP5 (PBP5‑CD) of 13 penicillin‑resistant clinical isolates of E. faecium were sequenced and the correlation between penicillin resistance and particular amino acid changes were analyzed. The present study identified for the first time, to the best of our knowledge, two novel substitutions (Tyr460Phe and Ala462Thr or Val462Thr) of E. faecium PBP5‑CD. The covalent interaction between penicillin and PBP5‑CD was also investigated using homology modeling and molecular docking methods. The theoretical calculation revealed that Phe460 and Thr462 were involved in penicillin binding, suggesting that substitutions at these positions exert effects on the affinity for penicillin, and this increased affinity translates into lower resistance in vitro.
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Copy and paste a formatted citation
Spandidos Publications style
Zhou C, Niu H, Yu H, Zhou L and Wang Z: Effects of two novel amino acid substitutions on the penicillin binding properties of the PBP5 C‑terminal from Enterococcus faecium. Mol Med Rep 12: 5281-5285, 2015.
APA
Zhou, C., Niu, H., Yu, H., Zhou, L., & Wang, Z. (2015). Effects of two novel amino acid substitutions on the penicillin binding properties of the PBP5 C‑terminal from Enterococcus faecium. Molecular Medicine Reports, 12, 5281-5285. https://doi.org/10.3892/mmr.2015.4057
MLA
Zhou, C., Niu, H., Yu, H., Zhou, L., Wang, Z."Effects of two novel amino acid substitutions on the penicillin binding properties of the PBP5 C‑terminal from Enterococcus faecium". Molecular Medicine Reports 12.4 (2015): 5281-5285.
Chicago
Zhou, C., Niu, H., Yu, H., Zhou, L., Wang, Z."Effects of two novel amino acid substitutions on the penicillin binding properties of the PBP5 C‑terminal from Enterococcus faecium". Molecular Medicine Reports 12, no. 4 (2015): 5281-5285. https://doi.org/10.3892/mmr.2015.4057
Copy and paste a formatted citation
x
Spandidos Publications style
Zhou C, Niu H, Yu H, Zhou L and Wang Z: Effects of two novel amino acid substitutions on the penicillin binding properties of the PBP5 C‑terminal from Enterococcus faecium. Mol Med Rep 12: 5281-5285, 2015.
APA
Zhou, C., Niu, H., Yu, H., Zhou, L., & Wang, Z. (2015). Effects of two novel amino acid substitutions on the penicillin binding properties of the PBP5 C‑terminal from Enterococcus faecium. Molecular Medicine Reports, 12, 5281-5285. https://doi.org/10.3892/mmr.2015.4057
MLA
Zhou, C., Niu, H., Yu, H., Zhou, L., Wang, Z."Effects of two novel amino acid substitutions on the penicillin binding properties of the PBP5 C‑terminal from Enterococcus faecium". Molecular Medicine Reports 12.4 (2015): 5281-5285.
Chicago
Zhou, C., Niu, H., Yu, H., Zhou, L., Wang, Z."Effects of two novel amino acid substitutions on the penicillin binding properties of the PBP5 C‑terminal from Enterococcus faecium". Molecular Medicine Reports 12, no. 4 (2015): 5281-5285. https://doi.org/10.3892/mmr.2015.4057
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