Insight of Genus Corynebacterium: Ascertaining the Role of Pathogenic and Non-pathogenic Species

Oliveira, Alberto de; Oliveira, Lívia Costa de; Aburjaile, Flávia Figueira; Benevides, Leandro de Jesus; Tiwari, Sandeep; Jamal, Syed Babar; Silva, Arthur; Figueiredo, Henrique César Pereira; Ghosh, Preetam; Portela, Ricardo Wagner; Azevedo, Vasco; Wattam, Alice R.

doi:10.3389/fmicb.2017.01937

Cited by 84 publications

(57 citation statements)

References 207 publications

(195 reference statements)

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“…An initial BLASTP study revealed that many corynebacteria, in contrast to the highly conserved rel and relS genes, contain no ORF with a significant similarity to the amino acid sequence of RelH Cg besides the hydrolase domain of the respective rel gene. Based on this observation we assessed the presence of this gene in the whole genus of which more than 110 species were described ( Oliveira et al, 2017 ). These species were isolated from the environment but also from humans and animals, where in some cases, a pathogenic potential has been documented.…”

Section: Resultsmentioning

confidence: 99%

Functional Characterization of a Small Alarmone Hydrolase in Corynebacterium glutamicum

et al. 2018

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The (pp)pGpp metabolism is an important component of bacterial physiology as it is involved in various stress responses and mechanisms of cell homeostasis, e.g., the regulation of growth. However, in order to better understand the (pp)pGpp associated regulation, it is crucial to study the molecular mechanisms of (pp)pGpp metabolism. In recent years, bioinformatic analyses of the RelA/SpoT homolog (RSH) superfamily have led to the discovery of small monofunctional RSH derivatives in addition to the well-known bifunctional Rel proteins. These are also referred to as small alarmone synthetases (SASs) or small alarmone hydrolases (SAHs). In this study, the ORF cg1485 from C. glutamicum was identified as a putative SAH encoding gene, based on a high similarity of the corresponding amino acid sequence with the (pp)pGpp hydrolysis domain. The characterization of its gene product, designated as RelHCg, represents the first functional investigation of a bacterial representative of the SAH subfamily. The predicted pyrophosphohydrolase activity was demonstrated in vivo by expression in two E. coli strains, characterized by different alarmone basal levels, as well as by in vitro analysis of the purified protein. During the assay-based analysis of hydrolysis activity in relation to the three known alarmone species, both RelHCg and the bifunctional RSH enzyme RelCg were found to exhibit a pronounced substrate inhibition for alarmone concentrations of more than 0.75 mM. This characteristic of (pp)pGpp hydrolases could be an important mechanism for realizing the bistable character of the (pp)pGpp metabolism between a (pp)pGpp basal level and stress-associated alarmone production. The deletion of relHCg caused only a minor effect on growth behavior in both wild-type background and deletion mutants with deletion of (pp)pGpp synthetases. Based on this observation, the protein is probably only present or active under specific environmental conditions. The independent loss of the corresponding gene in numerous representatives of the genus Corynebacterium, which was found by bioinformatic analyses, also supports this hypothesis. Furthermore, growth analysis of all possible deletion combinations of the three active C. glutamicum RSH genes revealed interesting functional relationships which will have to be investigated in more detail in the future.

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Section: Resultsmentioning

confidence: 99%

Functional Characterization of a Small Alarmone Hydrolase in Corynebacterium glutamicum

et al. 2018

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“…2 ), isolated from cases of endocarditis in Rio de Janeiro, Brazil, with high nucleotide similarity between our C. striatum isolate and C. diphtheriae HC01 and HC02 isolates. However, the SpaA pili proposed as an essential factor in C. diphtheriae to adherence to pharyngeal epithelial cells 21 was absent in our C. striatum isolate analysed.…”

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confidence: 64%

Genome sequence of a multidrug-resistant Corynebacterium striatum isolated from bloodstream infection from a nosocomial outbreak in Rio de Janeiro, Brazil

Ramos

Rodrigues

Baio

et al. 2018

Mem. Inst. Oswaldo Cruz

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Multidrug-resistant (MDR) Corynebacterium striatum has been cited with increased frequency as pathogen of nosocomial infections. In this study, we report the draft genome of a C. striatum isolated from a patient with bloodstream infection in a hospital of Rio de Janeiro, Brazil. The isolate presented susceptibility only to tetracycline, vancomycin and linezolid. The detection of various antibiotic resistance genes is fully consistent with previously observed multidrug-resistant pattern in Corynebacterium spp. A large part of the pTP10 plasmid of MDR C. striatum M82B is present in the genome of our isolate. A SpaDEF cluster and seven arrays of CRISPR-Cas were found.

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“…To study the relation of species distance and recombineering efficiency, we first identified the PRFUs in the genus Corynebacterium , a taxonomic group with highly diversified species that are of medical, veterinary, or biotechnological relevance (12). Previous studies relating to PRFUs used either reference genomes or nonredundant protein databases for bioinformatics analysis (13–15).…”

Section: Resultsmentioning

confidence: 99%

The efficiency for recombineering is dependent on the source of the phage recombinase function unit

Chang¹,

Wang

Su³

et al. 2019

Preprint

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21Phage recombinase function units (PRFUs) such as lambda-Red or Rac RecET have been proven 22 to be powerful genetic tools in the recombineering of Escherichia coli. Studies have focused on 23 developing such systems in other bacteria as it is believed that these PRFUs have limited efficiency 24 in distant species. However, how the species evolution distance relates to the efficiency of 25 recombineering remains unclear. Here, we present a thorough study of PRFUs to find features that 26 might be related to the efficiency of PRFUs for recombineering. We first identified 59 unique sets 27 of PRFUs in the genus Corynebacterium and classified them based on their sequence as well as 28 secondary structure similarities. Then both PRFUs from this genus and other bacteria were chosen 29 for experiment based on sequential and secondary structure similarity as well as species distance. 30These PRFUs were compared for their ability in mediating recombineering with oligo or double-31 stranded DNA substrates in Corynebacterium glutamicum. We demonstrate that the source of the 32 PRFU is more critical than species distance for the efficiency of recombineering. Our work will 33 provide new ideas for efficient recombineering using PRFUs. 34 35 Importance 36 Recombineering using phage recombinase function units (PRFUs) such as lambda-Red or Rac 37RecET has gained success in Escherichia coli, while efforts applying these systems in other 38 bacteria were limited by the efficiency. It is believed that the species distance may be a major 39 reason for the low efficiency. In this study, however, we showed that it is the source of PRFU 40 rather than the species distance that matters for the recombineering in Corynebacterium 41 glutamicum. Besides, we also showed that the lower transformation efficiency in other bacteria 42 compared to that of E. coli could be a major reason for the low performance of heterogeneously 43 expressed RecET. These findings will be helpful for the recombineering using PRFUs. 44 Keywords: phage recombinase function unit, RecET, recombineering, efficiency 45 46 Recombineering using a phage recombinase function unit (PRFU), which usually contains one 48 single-stranded annealing protein (SSAP) and one 5'-3' exonuclease (EXO), is powerful in certain 49 bacteria (1-5). Expression of the SSAP alone can mediate recombineering with single-stranded 50 DNA (ssDNA) substrates, while expression of the whole system can use double-stranded DNA 51 (dsDNA) as substrates for genome fragment editing (1, 2).52 Well-known PRFUs such as lambda-Red or Rac RecET have been used for successful 53 recombineering in Escherichia coli. The Red system is phage lambda derived, while the RecET 54 system is from the defective prophage Rac of E. coli (1). Lambda-Red contains three adjacent 55 genes gam, bet, and exo, which encode a host nuclease inhibiting the protein Gam, an SSAP Beta, 56 and an EXO, respectively (6). In E. coli, it is possible to mediate recombineering using a dsDNA 57 fragment with a homology arm as short as 35 base...

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Insight of Genus Corynebacterium: Ascertaining the Role of Pathogenic and Non-pathogenic Species

Cited by 84 publications

References 207 publications

Functional Characterization of a Small Alarmone Hydrolase in Corynebacterium glutamicum

Functional Characterization of a Small Alarmone Hydrolase in Corynebacterium glutamicum

Genome sequence of a multidrug-resistant Corynebacterium striatum isolated from bloodstream infection from a nosocomial outbreak in Rio de Janeiro, Brazil

The efficiency for recombineering is dependent on the source of the phage recombinase function unit

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