In:
PLOS Genetics, Public Library of Science (PLoS), Vol. 17, No. 10 ( 2021-10-21), p. e1009365-
Abstract:
Mycoplasmas are minute bacteria controlled by very small genomes ranging from 0.6 to 1.4 Mbp. They encompass several important medical and veterinary pathogens that are often associated with a wide range of chronic diseases. The long persistence of mycoplasma cells in their hosts can exacerbate the spread of antimicrobial resistance observed for many species. However, the nature of the virulence factors driving this phenomenon in mycoplasmas is still unclear. Toxin-antitoxin systems (TA systems) are genetic elements widespread in many bacteria that were historically associated with bacterial persistence. Their presence on mycoplasma genomes has never been carefully assessed, especially for pathogenic species. Here we investigated three candidate TA systems in M . mycoides subsp. capri encoding a (i) novel AAA-ATPase/subtilisin-like serine protease module, (ii) a putative AbiEii/AbiEi pair and (iii) a putative Fic/RelB pair. We sequence analyzed fourteen genomes of M . mycoides subsp. capri and confirmed the presence of at least one TA module in each of them. Interestingly, horizontal gene transfer signatures were also found in several genomic loci containing TA systems for several mycoplasma species. Transcriptomic and proteomic data confirmed differential expression profiles of these TA systems during mycoplasma growth in vitro . While the use of heterologous expression systems based on E . coli and B . subtilis showed clear limitations, the functionality and neutralization capacities of all three candidate TA systems were successfully confirmed using M . capricolum subsp. capricolum as a host. Additionally, M . capricolum subsp. capricolum was used to confirm the presence of functional TA system homologs in mycoplasmas of the Hominis and Pneumoniae phylogenetic groups. Finally, we showed that several of these M . mycoides subsp. capri toxins tested in this study, and particularly the subtilisin-like serine protease, could be used to establish a kill switch in mycoplasmas for industrial applications.
Type of Medium:
Online Resource
ISSN:
1553-7404
DOI:
10.1371/journal.pgen.1009365
DOI:
10.1371/journal.pgen.1009365.g001
DOI:
10.1371/journal.pgen.1009365.g002
DOI:
10.1371/journal.pgen.1009365.g003
DOI:
10.1371/journal.pgen.1009365.g004
DOI:
10.1371/journal.pgen.1009365.g005
DOI:
10.1371/journal.pgen.1009365.g006
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10.1371/journal.pgen.1009365.t001
DOI:
10.1371/journal.pgen.1009365.t002
DOI:
10.1371/journal.pgen.1009365.s001
DOI:
10.1371/journal.pgen.1009365.s002
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10.1371/journal.pgen.1009365.s003
DOI:
10.1371/journal.pgen.1009365.s004
DOI:
10.1371/journal.pgen.1009365.s005
DOI:
10.1371/journal.pgen.1009365.s006
DOI:
10.1371/journal.pgen.1009365.s007
DOI:
10.1371/journal.pgen.1009365.s008
DOI:
10.1371/journal.pgen.1009365.s009
DOI:
10.1371/journal.pgen.1009365.s010
DOI:
10.1371/journal.pgen.1009365.s011
DOI:
10.1371/journal.pgen.1009365.s012
DOI:
10.1371/journal.pgen.1009365.s013
DOI:
10.1371/journal.pgen.1009365.s014
DOI:
10.1371/journal.pgen.1009365.s015
Language:
English
Publisher:
Public Library of Science (PLoS)
Publication Date:
2021
detail.hit.zdb_id:
2186725-2
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