Identification and characterization of a Streptomyces sp. isolate exhibiting activity against multidrug-resistant coagulase-negative Staphylococci

Aim To investigate the epidemiology of S. aureus and MRSA nasal carriage among people with diabetes at the Korle Bu Teaching Hospital in Accra, including the prevalence, predictors of carriage, and antibiotic resistance. Methodology This study was cross-sectional, involving 300 diabetes patients and 106 non-diabetic individuals. Swab specimens of the nares were obtained from the participants and bacteriologically-cultured. Identification and characterization of S. aureus and MRSA were based on standard bacteriological methods; antimicrobial susceptibility testing was by the Kirby-Bauer method. Results The prevalence of staphylococcal carriage, the diabetes group relative to the non-diabetes group, were 31.0% and 10.4% (S. aureus), and 3.3% and 0.0% (MRSA). Presence of diabetes predisposed to S. aureus carriage, but not MRSA nor coagulase-negative staphylococci (CoNS) carriage (OR = 3.88; p < 0.0001). Colonization with CoNS was protective of S. aureus (OR = 0.039, p < 0.001) and MRSA (OR = 0.115, p = 0.043) colonization among the diabetics. The antimicrobial resistance patterns recorded among the S. aureus isolated from the diabetic individuals relative to the non-diabetics were as follows: penicillin (95% vs. 91%), tetracycline (37% vs. 27%), cotrimoxazole (30% vs. 36%), erythromycin (17% vs. 0%), norfloxacin (13% vs. 0%), clindamycin (12% vs. 0%), gentamicin (9% vs. 0%), fusidic acid (10% vs. 9%), linezolid (4% vs. 0%), and rifampicin (5% vs. 0%). The proportion of multidrug resistant S. aureus was 41% (n = 38) in the diabetes group and 0% in the non-diabetes group; this difference was statistically significant (p = 0.01). Conclusions The presence of diabetes predisposed the participants to S. aureus carriage by almost four folds, but not MRSA carriage. Colonization with CoNS was protective of S. aureus and MRSA carriage in the diabetes group. Finally, linezolid remains a good therapeutic agent for anti-MRSA therapy.

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Identification and characterization of a novel spermidine/spermine acetyltransferase encoded by gene ste26 from Streptomyces sp. 139

Biochimie ◽

10.1016/j.biochi.2011.04.014 ◽

2011 ◽

Vol 93 (9) ◽

pp. 1401-1407 ◽

Cited By ~ 8

Author(s):

Liping Bai ◽

Ming Chang ◽

Junjie Shan ◽

Rong Jiang ◽

Yang Zhang ◽

...

Keyword(s):

Streptomyces Sp ◽

Identification And Characterization

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Identification and Characterization of Quorum-Quenching Activity of N-Acylhomoserine Lactonase from Coagulase-Negative Staphylococci

Antibiotics ◽

10.3390/antibiotics9080483 ◽

2020 ◽

Vol 9 (8) ◽

pp. 483

Author(s):

Tomohiro Morohoshi ◽

Yaoki Kamimura ◽

Nobutaka Someya

Keyword(s):

Quorum Sensing ◽

Opportunistic Pathogen ◽

Quorum Quenching ◽

Coagulase Negative Staphylococci ◽

Sensing Systems ◽

Genes Encoding ◽

Acyl Chains ◽

Gene Homologue ◽

Identification And Characterization

N-Acylhomoserine lactones (AHLs) are used as quorum-sensing signals in Gram-negative bacteria. Many genes encoding AHL-degrading enzymes have been cloned and characterized in various microorganisms. Coagulase-negative staphylococci (CNS) are present on the skin of animals and are considered low-virulent species. The AHL-lactonase gene homologue, ahlS, was present in the genomes of the CNS strains Staphylococcus carnosus, Staphylococcus haemolyticus, Staphylococcus saprophyticus, and Staphylococcus sciuri. We cloned the candidate ahlS homologue from six CNS strains into the pBBR1MCS5 vector. AhlS from the CNS strains showed a higher degrading activity against AHLs with short acyl chains compared to those with long acyl chains. AhlS from S. sciuri was expressed and purified as a maltose-binding protein (MBP) fusion. Pseudomonas aeruginosa is an opportunistic pathogen that regulates several virulence factors such as elastase and pyocyanin by quorum-sensing systems. When MBP-AhlS was added to the culture of P. aeruginosa PAO1, pyocyanin production and elastase activity were substantially reduced compared to those in untreated PAO1. These results demonstrate that the AHL-degrading activity of AhlS from the CNS strains can inhibit quorum sensing in P. aeruginosa PAO1.

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Identification and Characterization of Multidrug-Resistant Extended-Spectrum Beta-Lactamase-Producing Bacteria from Healthy and Diseased Dogs and Cats Admitted to a Veterinary Hospital in Brazil

Microbial Drug Resistance ◽

10.1089/mdr.2020.0043 ◽

2020 ◽

Author(s):

Ricardo Antonio Pilegi Sfaciotte ◽

Leandro Parussolo ◽

Fernanda Danielle Melo ◽

Paula Wildemann ◽

Giseli Bordignon ◽

...

Keyword(s):

Multidrug Resistant ◽

Beta Lactamase ◽

Extended Spectrum Beta Lactamase ◽

Extended Spectrum ◽

Veterinary Hospital ◽

Identification And Characterization

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Identification and Characterization of a Novel aac(6′)-Iag Associated with the blaIMP-1–Integron in a Multidrug-Resistant Pseudomonas aeruginosa

PLoS ONE ◽

10.1371/journal.pone.0070557 ◽

2013 ◽

Vol 8 (8) ◽

pp. e70557 ◽

Cited By ~ 12

Author(s):

Kanao Kobayashi ◽

Ikue Hayashi ◽

Syuntaro Kouda ◽

Fuminori Kato ◽

Tamaki Fujiwara ◽

...

Keyword(s):

Pseudomonas Aeruginosa ◽

Multidrug Resistant ◽

Identification And Characterization

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Identification and Characterization of Class 1 Integron Resistance Gene Cassettes among Salmonella Strains Isolated from Imported Seafood

Applied and Environmental Microbiology ◽

10.1128/aem.02054-08 ◽

2008 ◽

Vol 75 (4) ◽

pp. 1192-1196 ◽

Cited By ~ 27

Author(s):

Ashraf A. Khan ◽

Elizabeth Ponce ◽

M. S. Nawaz ◽

Chorng-Ming Cheng ◽

Junaid A. Khan ◽

...

Keyword(s):

Salmonella Enterica ◽

Southern Hybridization ◽

Multidrug Resistant ◽

The Philippines ◽

Streptomycin Resistance ◽

Class 1 Integron ◽

Class 1 ◽

Identification And Characterization ◽

Multiple Antibiotics

ABSTRACT A total of 210 Salmonella isolates, representing 64 different serovars, were isolated from imported seafood samples, and 55/210 isolates were found to be resistant to at least one antibiotic. Class 1 integrons from three multidrug-resistant Salmonella enterica strains (Salmonella enterica serovars Newport [strain 62], Typhimurium var. Copenhagen [strain 629], and Lansing [strain 803], originating from Hong Kong, the Philippines, and Taiwan, respectively) were characterized. Southern hybridization of plasmids isolated from these strains, using a class 1 integron probe, showed that trimethoprim-sulfamethoxazole and streptomycin resistance genes were located on a megaplasmid in strain 629. Our study indicates that imported seafood could be a reservoir for Salmonella isolates resistant to multiple antibiotics.

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Identification and characterization of a biosynthetic gene cluster for tryptophan dimers in deep sea-derived Streptomyces sp. SCSIO 03032

Applied Microbiology and Biotechnology ◽

10.1007/s00253-017-8375-5 ◽

2017 ◽

Vol 101 (15) ◽

pp. 6123-6136 ◽

Cited By ~ 6

Author(s):

Liang Ma ◽

Wenjun Zhang ◽

Yiguang Zhu ◽

Guangtao Zhang ◽

Haibo Zhang ◽

...

Keyword(s):

Gene Cluster ◽

Deep Sea ◽

Biosynthetic Gene Cluster ◽

Biosynthetic Gene ◽

Streptomyces Sp ◽

Identification And Characterization

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Activation and Identification of a Griseusin Cluster in Streptomyces sp. CA-256286 by Employing Transcriptional Regulators and Multi-Omics Methods

Molecules ◽

10.3390/molecules26216580 ◽

2021 ◽

Vol 26 (21) ◽

pp. 6580

Author(s):

Charlotte Beck ◽

Tetiana Gren ◽

Francisco Javier Ortiz-López ◽

Tue Sparholt Jørgensen ◽

Daniel Carretero-Molina ◽

...

Keyword(s):

Biosynthetic Pathway ◽

Genome Mining ◽

Gene Clusters ◽

Transcriptional Regulators ◽

Biosynthetic Gene ◽

Biosynthetic Gene Clusters ◽

Heterologous Host ◽

Streptomyces Sp ◽

Identification And Characterization

Streptomyces are well-known producers of a range of different secondary metabolites, including antibiotics and other bioactive compounds. Recently, it has been demonstrated that “silent” biosynthetic gene clusters (BGCs) can be activated by heterologously expressing transcriptional regulators from other BGCs. Here, we have activated a silent BGC in Streptomyces sp. CA-256286 by overexpression of a set of SARP family transcriptional regulators. The structure of the produced compound was elucidated by NMR and found to be an N-acetyl cysteine adduct of the pyranonaphtoquinone polyketide 3′-O-α-d-forosaminyl-(+)-griseusin A. Employing a combination of multi-omics and metabolic engineering techniques, we identified the responsible BGC. These methods include genome mining, proteomics and transcriptomics analyses, in combination with CRISPR induced gene inactivations and expression of the BGC in a heterologous host strain. This work demonstrates an easy-to-implement workflow of how silent BGCs can be activated, followed by the identification and characterization of the produced compound, the responsible BGC, and hints of its biosynthetic pathway.

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Coordinated Action of NRPS, Baeyer-Villiger Monooxygenase, and Methyltransferase Ensures the Economical Biosynthesis of Bohemamines in Streptomyces sp. CB02009

10.26434/chemrxiv.11687139 ◽

2020 ◽

Author(s):

Ling Liu ◽

Sainan Li ◽

Runze Sun ◽

Xiangjing Qin ◽

Jianhua Ju ◽

...

Keyword(s):

Methyl Groups ◽

Ribosome Engineering ◽

Methyl Group ◽

Proteinogenic Amino Acid ◽

Streptomyces Sp ◽

Coordinated Action ◽

Peptide Synthetase ◽

Identification And Characterization ◽

Shed Light

Bohemamines (BHMs) are bacterial alkaloids containing a pyrrolizidine core with two unprecedented methyl groups. Herein we report the activation of BHMs biosynthesis in Streptomyces sp. CB02009 using a ribosome engineering approach. Identification and characterization of the bhm gene cluster reveals a coordinated action of nonribosomal peptide synthetase BhmJ, Baeyer-villiger monooxygenase BhmK and methyltransferase BhmG for BHMs biosynthesis. BhmG is responsible for the C-methylation on C-7, while the C-9 methyl group is from a non-proteinogenic amino acid (2S,5S)-5-methylproline, required for BHMs production in three model Streptomyces hosts. Our study shed light on the intricate interaction of BhmJ/BhmK/BhmG for the economical biosynthesis of BHMs in their native producer, and also unraveled that BhmJ and BhmK are competent biocatalysts in Streptomyce albus.

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