How Stress and Antibiotic Exposure Affect Bacterial Intra- and Inter-species Competition

A special issue of Life (ISSN 2075-1729). This special issue belongs to the section "Microbiology".

Deadline for manuscript submissions: closed (30 April 2021) | Viewed by 3335

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Health Sciences Research Centre, University of Roehampton, London SW15 4JD, UK
Interests: targeted metabolomics; isotope labelling; microbial metabolomics; GC-MS; LC-MS; NMR
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Special Issue Information

Dear Colleagues,

This Special Issue will focus on the impact of stress and sub-MIC antibiotic exposure on bacterial competition.

To survive, bacteria have to be able to withstand abiotic stresses, such as changes in osmotic pressure, pH, and temperature, and biotic stresses, such as predators. However, bacteria rarely live in isolation. They share and compete for nutrients with other bacteria and also eukaryotic organisms, such as fungi. Even within a single species, the emergence of social cheaters from within a population has been described.

Microbial consortia are important in a variety of contexts, including human health and nutrient cycles. With interest in these consortia, such as the gut microbiota, increasing, our understanding of interactions and competition between consortia becomes more important. An interesting aspect of this is how the over-use of antibiotics, and the consequent selection of resistance mechanisms in exposed strains, affects cooperation and competition between bacteria.

We, therefore, invite you to submit an original research article or a review in the area of intra- and inter-species competition, with a particular focus on the influence of stress on these interactions. Topics of interest include, but are not limited to: gut microbial competition; the impact of exposure to sub-inhibitory levels of antibiotics on bacterial virulence; and the resistance to stress of environmental bacterial consortia.

Dr. Volker Behrends
Dr. Michal Letek
Guest Editors

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Keywords

  • bacterial virulence
  • gut microbiota
  • bacterial–fungal interaction
  • quorum sensing
  • bacterial communities

Published Papers (1 paper)

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Research

12 pages, 4400 KiB  
Article
Dual RNase and β-lactamase Activity of a Single Enzyme Encoded in Archaea
by Seydina M. Diene, Lucile Pinault, Nicholas Armstrong, Said Azza, Vivek Keshri, Saber Khelaifia, Eric Chabrière, Gustavo Caetano-Anolles, Jean-Marc Rolain, Pierre Pontarotti and Didier Raoult
Life 2020, 10(11), 280; https://doi.org/10.3390/life10110280 - 14 Nov 2020
Cited by 11 | Viewed by 2843
Abstract
β-lactam antibiotics have a well-known activity which disturbs the bacterial cell wall biosynthesis and may be cleaved by β-lactamases. However, these drugs are not active on archaea microorganisms, which are naturally resistant because of the lack of β-lactam target in their cell wall. [...] Read more.
β-lactam antibiotics have a well-known activity which disturbs the bacterial cell wall biosynthesis and may be cleaved by β-lactamases. However, these drugs are not active on archaea microorganisms, which are naturally resistant because of the lack of β-lactam target in their cell wall. Here, we describe that annotation of genes as β-lactamases in Archaea on the basis of homologous genes is a remnant of identification of the original activities of this group of enzymes, which in fact have multiple functions, including nuclease, ribonuclease, β-lactamase, or glyoxalase, which may specialized over time. We expressed class B β-lactamase enzyme from Methanosarcina barkeri that digest penicillin G. Moreover, while weak glyoxalase activity was detected, a significant ribonuclease activity on bacterial and synthetic RNAs was demonstrated. The β-lactamase activity was inhibited by β-lactamase inhibitor (sulbactam), but its RNAse activity was not. This gene appears to have been transferred to the Flavobacteriaceae group especially the Elizabethkingia genus, in which the expressed gene shows a more specialized activity on thienamycin, but no glyoxalase activity. The expressed class C-like β-lactamase gene, from Methanosarcina sp., also shows hydrolysis activity on nitrocefin and is more closely related to DD-peptidase enzymes. Our findings highlight the need to redefine the nomenclature of β-lactamase enzymes and the specification of multipotent enzymes in different ways in Archaea and bacteria over time. Full article
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