-
Journal of Clinical Microbiology Feb 1985Staphylococcus simulans was identified as the etiological agent of osteomyelitis and septic arthritis in an adult male who had sustained a fracture of the fibula and...
Staphylococcus simulans was identified as the etiological agent of osteomyelitis and septic arthritis in an adult male who had sustained a fracture of the fibula and syndesmosis separation which required the installation of orthopedic hardware. Identifying characteristics and antibiograms for this organism, recovered from blood, wound exudate, and deep tissue samples, were determined. Recent evidence has linked slime production (adherence to smooth surfaces) by coagulase-negative staphylococci to infections by these organisms at sites where foreign bodies had been inserted. Tests for adherence showed this S. simulans strain to be a strong slime producer. This is the first reported case of osteomyelitis and septicemia due to S. simulans.
Topics: Adult; Arthritis, Infectious; Chronic Disease; Coagulase; Humans; Male; Osteomyelitis; Sepsis; Staphylococcal Infections; Staphylococcus
PubMed: 3972995
DOI: 10.1128/jcm.21.2.255-257.1985 -
Antimicrobial Agents and Chemotherapy Jan 1990A penicillin-binding protein of molecular weight 76,000 inducible by beta-lactams was detected in methicillin-resistant Staphylococcus haemolyticus and Staphylococcus...
A penicillin-binding protein of molecular weight 76,000 inducible by beta-lactams was detected in methicillin-resistant Staphylococcus haemolyticus and Staphylococcus simulans. DNA from these strains hybridized to the mecA gene from Staphylococcus aureus; however, the chromosomal HindIII fragments containing the mecA genes were 3.4 kilobases in S. haemolyticus and 4.3 kilobases in S. simulans.
Topics: Bacterial Proteins; Blotting, Southern; Carrier Proteins; Culture Media; DNA, Bacterial; Deoxyribonuclease HindIII; Electrophoresis, Polyacrylamide Gel; Gene Expression Regulation, Bacterial; Genes, Bacterial; Hexosyltransferases; Methicillin; Muramoylpentapeptide Carboxypeptidase; Nucleic Acid Hybridization; Penicillin Resistance; Penicillin-Binding Proteins; Peptidyl Transferases; Restriction Mapping; Staining and Labeling; Staphylococcus; Staphylococcus aureus
PubMed: 1691614
DOI: 10.1128/AAC.34.1.170 -
Plasmid May 2013Staphylococcus simulans biovar staphylolyticus contains five plasmids, designated pACK1-pACK5. Recently, the nucleotide sequences of three of these plasmids, pACK1,...
Staphylococcus simulans biovar staphylolyticus contains five plasmids, designated pACK1-pACK5. Recently, the nucleotide sequences of three of these plasmids, pACK1, pACK3, and pACK4, were reported. In order to complete the characterization of these five plasmids, the nucleotide sequences of the two remaining plasmids, pACK2 (37683 bp) and pACK5 (3191 bp), were determined. pACK5 is comprised of two regions, one with 85% identity at the nucleotide level to a region of pWBG1773 and another region with an ORF that shares no significant similarity to sequences previously described in GenBank. pACK2 encodes proteins for cadmium resistance and enhanced biofilm formation. The similarities at the nucleotide level among regions of the plasmids of S. simulans bv. staphylolyticus suggest that these plasmids have undergone multiple intermolecular rearrangements.
Topics: Bacterial Proteins; Base Sequence; Biofilms; Cadmium Compounds; DNA Replication; DNA, Bacterial; Gene Rearrangement; Open Reading Frames; Operon; Plasmids; Replication Origin; Sequence Homology, Nucleic Acid; Staphylococcus; Sulfates
PubMed: 23396145
DOI: 10.1016/j.plasmid.2013.01.008 -
Biochemical and Biophysical Research... May 1989Staphylococcus simulans biovar staphylolyticus, the lysostaphin-producing organism, secretes a staphylolytic endopeptidase (EC 3.4.99.17) that is encoded on plasmid...
Staphylococcus simulans biovar staphylolyticus, the lysostaphin-producing organism, secretes a staphylolytic endopeptidase (EC 3.4.99.17) that is encoded on plasmid pACK1. Susceptibility of pACK1-cured strains to lysis by endopeptidase established that resistance to this enzyme is not an inherent property of the organism but rather is encoded on this dispensable plasmid. Furthermore, the enzyme is not an autolysin that is essential for cell wall synthesis because strains lacking the endopeptidase gene grew normally.
Topics: Lysostaphin; Mutation; Plasmids; Staphylococcus
PubMed: 2730641
DOI: 10.1016/s0006-291x(89)80117-2 -
Biochemical and Biophysical Research... Sep 2016Sortase mediated transpeptidation reactions play a significant role in covalent attachment of surface proteins to the cell wall of Gram-positive bacteria. Earlier...
Sortase mediated transpeptidation reactions play a significant role in covalent attachment of surface proteins to the cell wall of Gram-positive bacteria. Earlier studies have shown that sortase A (StrA) is required for the virulence of Staphylococci. The human pathogen Staphylococcus simulans CJ16 carries a putative sortase A (SsiStrA) encoding gene, but neither transpeptidation activity nor biochemical characteristics of SsiStrA have been investigated. Here, we identified and characterized StrA from coagulase-negative Staphylococci. SsiStrA was cloned and overexpressed in Escherichia coli BL21 in a soluble form. Size-exclusion chromatography, cross-linking and dynamic light scattering demonstrated that SsiStrA existed as monomer-dimer equilibrium in vitro. We further demonstrated that SsiStrA has sortase activity, and it recognized and cleaved the sorting motif LXPTG. H117, C180 and R193 residues were critical for enzyme activity, and calcium ions enhanced activity.
Topics: Amino Acid Motifs; Amino Acid Sequence; Aminoacyltransferases; Bacterial Proteins; Binding Sites; Calcium; Catalytic Domain; Cell Wall; Chromatography, Gel; Circular Dichroism; Cysteine Endopeptidases; Escherichia coli; Immunoblotting; Kinetics; Models, Molecular; Protein Domains; Protein Multimerization; Recombinant Proteins; Sequence Homology, Amino Acid; Staphylococcus; Substrate Specificity
PubMed: 27591898
DOI: 10.1016/j.bbrc.2016.08.175 -
Applied and Environmental Microbiology Mar 1994The lysostaphin gene of Staphylococcus simulans was cloned into Escherichia coli. The 5' end of the gene was modified to include a eukaryotic start codon, the Kozak...
The lysostaphin gene of Staphylococcus simulans was cloned into Escherichia coli. The 5' end of the gene was modified to include a eukaryotic start codon, the Kozak expression start site consensus sequence, and an enzyme site to facilitate manipulation of the gene. Transcription of the modified gene in vitro yielded an RNA transcript which, when added to a rabbit reticulocyte cell-free translation system, directed the synthesis of several products. The largest product, migrating at approximately 93 kDa, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, was probably preprolysostaphin, since it was cleaved in the presence of an S. simulans culture supernatant to yield a polypeptide of a size similar to that of mature lysostaphin. When canine pancreatic microsomal vesicles were added to the translation system, translocation of the newly synthesized polypeptides occurred, as judged by protection from proteolysis. The gene was also expressed transiently from the human cytomegalovirus promoter in COS-7 cells. Active enzyme could be detected in the cell lysate, and the prokaryotic signal appeared to target secretion of active enzyme to the culture medium. The successful expression of the lysostaphin gene and processing of the precursor to produce active secreted enzyme open up the possibility of controlling staphylococcal mastitis by targeting expression of this gene to the mammary glands of transgenic animals.
Topics: Animals; Base Sequence; Cells, Cultured; Cloning, Molecular; Dogs; Escherichia coli; Eukaryotic Cells; Gene Expression Regulation, Enzymologic; Haplorhini; Lysostaphin; Molecular Sequence Data; Rabbits; Staphylococcus; Transcription, Genetic
PubMed: 8161174
DOI: 10.1128/aem.60.3.771-776.1994 -
Biochimica Et Biophysica Acta.... Mar 2024Epilancin 15X is a lantibiotic that has an antimicrobial activity in the nanomolar concentration range towards Staphylococcus simulans. Such low MICs usually imply that... (Review)
Review
Epilancin 15X is a lantibiotic that has an antimicrobial activity in the nanomolar concentration range towards Staphylococcus simulans. Such low MICs usually imply that these peptides employ a mechanism of action (MoA) involving high affinity targets. Here we studied this MoA by using epilancin 15X's ability to dissipate the membrane potential of intact S. simulans cells. These membrane depolarization assays showed that treatment of the bacteria by antibiotics known to affect the bacterial cell wall synthesis pathway decreased the membrane depolarization effects of epilancin 15X. Disruption of the Lipid II cycle in intact bacteria using several methods led to a decrease in the activity of epilancin 15X. Antagonism-based experiments on 96-well plate and agar diffusion plate pointed towards a possible interaction between epilancin 15X and Lipid II and this was confirmed by Circular Dichroism (CD) based experiments. However, this interaction did not lead to a detectable effect on either carboxyfluorescein (CF) leakage or proton permeability. All experiments point to the involvement of a phosphodiester-containing target within a polyisoprene-based biosynthesis pathway, yet the exact identity of the target remains obscure so far.
Topics: Amino Acid Sequence; Bacteriocins; Anti-Bacterial Agents; Peptides
PubMed: 38218577
DOI: 10.1016/j.bbamem.2024.184282 -
Case Reports in Infectious Diseases 2018is a coagulase-negative organism, mainly an animal pathogen. Reports of human infection have been infrequent, mainly in patients with repeated animal contact. We report...
is a coagulase-negative organism, mainly an animal pathogen. Reports of human infection have been infrequent, mainly in patients with repeated animal contact. We report the first case of pleural empyema in an elderly woman. tends to cause more severe infection because of a biofilm layer which helps in adherence and colonization of smooth surfaces, especially prosthetic devices, shunts, and catheters. The challenging problem even after CoNS isolation and identification is the assessment of their clinical relevance. Major factors that inhibit the penetration of antibiotics is the large-sized effusions/empyema, thickness of pleura, and the nature of antibiotic itself. Source control for septic patients remains the cornerstone of treatment along with optimal antimicrobial coverage. , a coagulase-negative staphylococcus, is emerging as an important cause of virulent infections with high mortality in humans. Given its propensity for multidrug resistance, including vancomycin, there is an imperative for early and accurate identification of the isolate. Despite aggressive treatment, the patient succumbed to her illness.
PubMed: 30405924
DOI: 10.1155/2018/7831284 -
Journal of Dairy Science May 2011A longitudinal study in 3 dairy herds was conducted to profile the distribution of coagulase-negative Staphylococcus (CNS) species causing bovine intramammary infection...
A longitudinal study in 3 dairy herds was conducted to profile the distribution of coagulase-negative Staphylococcus (CNS) species causing bovine intramammary infection (IMI) using molecular identification and to gain more insight in the pathogenic potential of CNS as a group and of the most prevalent species causing IMI. Monthly milk samples from 25 cows in each herd as well as samples from clinical mastitis were collected over a 13-mo period. Coagulase-negative staphylococci were identified to the species level using transfer-RNA intergenic spacer PCR. The distribution of CNS causing IMI was highly herd-dependent, but overall, Staphylococcus chromogenes, Staphylococcus xylosus, Staphylococcus cohnii, and Staphylococcus simulans were the most prevalent. No CNS species were found to cause clinical mastitis. The effect of the most prevalent species on the quarter milk somatic cell count (SCC) was analyzed using a linear mixed model, showing that Staph. chromogenes, Staph. simulans, and Staph. xylosus induced an increase in the SCC that is comparable with that of Staphylococcus aureus. Almost all CNS species were able to cause persistent IMI, with Staph. chromogenes causing the most persistent infections. In conclusion, accurate species identification cannot be ignored when studying the effect of CNS on udder health, as the effect on SCC differs between species and species distribution is herd-specific. Staphylococcus chromogenes, Staph. simulans, and Staph. xylosus seem to be the more important species and deserve special attention in further studies. Reasons for herd dependency and possible cow- and quarter-level risk factors should be examined in detail for the different species, eventually leading to cost-benefit analyses for management changes and, if needed, treatment recommendations.
Topics: Animals; Cattle; Coagulase; Female; Longitudinal Studies; Mammary Glands, Animal; Mastitis, Bovine; Milk; Polymerase Chain Reaction; Species Specificity; Staphylococcal Infections; Staphylococcus
PubMed: 21524522
DOI: 10.3168/jds.2010-3741 -
Saudi Journal of Biological Sciences Mar 2018An extracellular lipase of a newly isolated strain ALA1 (SAL4) was purified from the optimized culture medium. The SAL4 specific activity determined at 60 °C and pH...
An extracellular lipase of a newly isolated strain ALA1 (SAL4) was purified from the optimized culture medium. The SAL4 specific activity determined at 60 °C and pH 12 by using olive oil emulsion or TC4, reached 7215 U/mg and 2484 U/mg, respectively. The 38 NH-terminal amino acid sequence of the purified enzyme starting with two extra amino acid residues (LK) was similar to known staphylococcal lipase sequences. This novel lipase maintained almost 100% and 75% of its full activity in a pH range of 4.0-12 after a 24 h incubation or after 0.5 h treatment at 70 °C, respectively. Interestingly, SAL4 displayed appreciable stability toward oxidizing agents, anionic and non-ionic surfactants in addition to its compatibility with several commercial detergents. Overall, these interesting characteristics make this new lipase promising for its application in detergent industry.
PubMed: 29686504
DOI: 10.1016/j.sjbs.2016.10.006