Next Article in Journal
Ultrasound- and Molecular Sieves-Assisted Synthesis, Molecular Docking and Antifungal Evaluation of 5-(4-(Benzyloxy)-substituted phenyl)-3-((phenylamino)methyl)-1,3,4-oxadiazole-2(3H)-thiones
Next Article in Special Issue
Inhalable Antitubercular Therapy Mediated by Locust Bean Gum Microparticles
Previous Article in Journal
The Homocoupling Reaction of Aromatic Terminal Alkynes by a Highly Active Palladium(II)/AgNO3 Cocatalyst in Aqueous Media Under Aerobic Conditions
Previous Article in Special Issue
The Current Case of Quinolones: Synthetic Approaches and Antibacterial Activity
Article Menu
Issue 5 (May) cover image

Export Article

Open AccessReview
Molecules 2016, 21(5), 605; doi:10.3390/molecules21050605

Self-resistance in Streptomyces, with Special Reference to β-Lactam Antibiotics

1
HO Bio Institute, 33-9, Yushima-2, Bunkyo-ku, Tokyo 113-0034, Japan
2
Department of Biochemistry, Meiji Pharmaceutical University, 522-1, Noshio-2, Kiyose, Tokyo 204-8588, Japan
Academic Editor: Peter J. Rutledge
Received: 23 March 2016 / Revised: 26 April 2016 / Accepted: 29 April 2016 / Published: 10 May 2016
View Full-Text   |   Download PDF [7058 KB, uploaded 10 May 2016]   |  

Abstract

Antibiotic resistance is one of the most serious public health problems. Among bacterial resistance, β-lactam antibiotic resistance is the most prevailing and threatening area. Antibiotic resistance is thought to originate in antibiotic-producing bacteria such as Streptomyces. In this review, β-lactamases and penicillin-binding proteins (PBPs) in Streptomyces are explored mainly by phylogenetic analyses from the viewpoint of self-resistance. Although PBPs are more important than β-lactamases in self-resistance, phylogenetically diverse β-lactamases exist in Streptomyces. While class A β-lactamases are mostly detected in their enzyme activity, over two to five times more classes B and C β-lactamase genes are identified at the whole genomic level. These genes can subsequently be transferred to pathogenic bacteria. As for PBPs, two pairs of low affinity PBPs protect Streptomyces from the attack of self-producing and other environmental β-lactam antibiotics. PBPs with PASTA domains are detectable only in class A PBPs in Actinobacteria with the exception of Streptomyces. None of the Streptomyces has PBPs with PASTA domains. However, one of class B PBPs without PASTA domain and a serine/threonine protein kinase with four PASTA domains are located in adjacent positions in most Streptomyces. These class B type PBPs are involved in the spore wall synthesizing complex and probably in self-resistance. Lastly, this paper emphasizes that the resistance mechanisms in Streptomyces are very hard to deal with, despite great efforts in finding new antibiotics. View Full-Text
Keywords: β-lactam antibiotics; β-lactamase; penicillin-binding protein; self-resistance; antibiotic resistance; Streptomyces; Actinobacteria β-lactam antibiotics; β-lactamase; penicillin-binding protein; self-resistance; antibiotic resistance; Streptomyces; Actinobacteria
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Ogawara, H. Self-resistance in Streptomyces, with Special Reference to β-Lactam Antibiotics. Molecules 2016, 21, 605.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top