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Article: Retrospective Chart Review of Advanced Practice Pharmacist Prescribing of Controlled Substances for Pain Management at the Harry S. Truman Memorial Veterans' Hospital.

Kominek, Courtney

Federal practitioner : for the health care professionals of the VA, DoD, and PHS

2021 Volume 38, Issue 1, Page(s) 20–27

Abstract: ... care through the outpatient Pharmacy Pain Clinic in-person or via telephone who were enrolled at the Harry S. Truman Memorial ...

Abstract	Background: The US Department of Health and Human Services' 5-point strategy to combat the opioid overdose public health crisis includes improved pain management. There is a shortage of adequately trained health care providers in pain management. Advanced practice pharmacists may be able to help fill that void. The objective of this project was to identify the impact of an advanced practice pharmacist with controlled substance prescriptive authority on morphine milligram equivalent dose (MME) and compliance with opioid risk mitigation. Methods: In March 2020, a single-site retrospective chart review was conducted of patients who were prescribed controlled substances from July 1, 2018 to January 31, 2020. Patients received care through the outpatient Pharmacy Pain Clinic in-person or via telephone who were enrolled at the Harry S. Truman Memorial Veterans' Hospital in Columbia, Missouri, or associated outlying outpatient clinics. Patients were included if they were referred to the Pharmacy Pain Clinic and prescribed a Schedule II or III opioid medication. A 2-sided Results: Patients seen in Pharmacy Pain Clinic had a statistically significant reduction in MME from consult (93 MME) to discharge (31 MME) ( Conclusions: An advanced practice pharmacist with controlled substance prescriptive authority improved patient care with demonstrated statistically significant differences in MME and adherence with opioid risk mitigation from consult to discharge. Health care teams should look to add advanced practice pharmacists to their team as medication experts to deliver comprehensive medication management, which can include controlled substance prescribing and management.
Language	English
Publishing date	2021-02-11
Publishing country	United States
Document type	Journal Article
ISSN	1078-4497
ISSN	1078-4497
DOI	10.12788/fp.0079
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Article ; Online: Non-immune binding of human IgG to M-related proteins confers resistance to phagocytosis of group A streptococci in blood.

Courtney, Harry S / Li, Yi

PloS one

2013 Volume 8, Issue 10, Page(s) e78719

Abstract: The non-immune binding of immunoglobulins by bacteria is thought to contribute to the pathogenesis of infections. M-related proteins (Mrp) are group A streptococcal (GAS) receptors for immunoglobulins, but it is not known if this binding has any impact ... ...

Abstract	The non-immune binding of immunoglobulins by bacteria is thought to contribute to the pathogenesis of infections. M-related proteins (Mrp) are group A streptococcal (GAS) receptors for immunoglobulins, but it is not known if this binding has any impact on virulence. To further investigate the binding of immunoglobulins to Mrp, we engineered mutants of an M type 4 strain of GAS by inactivating the genes for mrp, emm, enn, sof, and sfbX and tested these mutants in IgG-binding assays. Inactivation of mrp dramatically decreased the binding of human IgG, whereas inactivation of emm, enn, sof, and sfbx had only minor effects, indicating that Mrp is a major IgG-binding protein. Binding of human immunoglobulins to a purified, recombinant form of Mrp indicated that it selectively binds to the Fc domain of human IgG, but not IgA or IgM and that it preferentially bound subclasses IgG₁>IgG₄>IgG₂>IgG₃. Recombinant proteins encompassing different regions of Mrp were engineered and used to map its IgG-binding domain to its A-repeat region and a recombinant protein with 3 A-repeats was a better inhibitor of IgG binding than one with a single A-repeat. A GAS mutant expressing Mrp with an in-frame deletion of DNA encoding the A-repeats had a dramatically reduced ability to bind human IgG and to grow in human blood. Mrp exhibited host specificity in binding IgG; human IgG was the best inhibitor of the binding of IgG followed by pig, horse, monkey, and rabbit IgG. IgG from goat, mouse, rat, cow, donkey, chicken, and guinea pig were poor inhibitors of binding. These findings indicate that Mrp preferentially binds human IgG and that this binding contributes to the ability of GAS to resist phagocytosis and may be a factor in the restriction of GAS infections to the human host.
MeSH term(s)	Amino Acid Sequence ; Animals ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Blood/microbiology ; Host Specificity ; Humans ; Immunoglobulin G/metabolism ; Molecular Sequence Data ; Phagocytosis ; Protein Binding ; Protein Structure, Tertiary ; Repetitive Sequences, Amino Acid ; Streptococcus pyogenes/metabolism ; Streptococcus pyogenes/physiology ; Substrate Specificity
Chemical Substances	Bacterial Proteins ; Immunoglobulin G
Language	English
Publishing date	2013-10-25
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0078719
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Article ; Online: Non-immune binding of human IgG to M-related proteins confers resistance to phagocytosis of group A streptococci in blood.

Harry S Courtney / Yi Li

PLoS ONE, Vol 8, Iss 10, p e

2013 Volume 78719

Abstract	The non-immune binding of immunoglobulins by bacteria is thought to contribute to the pathogenesis of infections. M-related proteins (Mrp) are group A streptococcal (GAS) receptors for immunoglobulins, but it is not known if this binding has any impact on virulence. To further investigate the binding of immunoglobulins to Mrp, we engineered mutants of an M type 4 strain of GAS by inactivating the genes for mrp, emm, enn, sof, and sfbX and tested these mutants in IgG-binding assays. Inactivation of mrp dramatically decreased the binding of human IgG, whereas inactivation of emm, enn, sof, and sfbx had only minor effects, indicating that Mrp is a major IgG-binding protein. Binding of human immunoglobulins to a purified, recombinant form of Mrp indicated that it selectively binds to the Fc domain of human IgG, but not IgA or IgM and that it preferentially bound subclasses IgG₁>IgG₄>IgG₂>IgG₃. Recombinant proteins encompassing different regions of Mrp were engineered and used to map its IgG-binding domain to its A-repeat region and a recombinant protein with 3 A-repeats was a better inhibitor of IgG binding than one with a single A-repeat. A GAS mutant expressing Mrp with an in-frame deletion of DNA encoding the A-repeats had a dramatically reduced ability to bind human IgG and to grow in human blood. Mrp exhibited host specificity in binding IgG; human IgG was the best inhibitor of the binding of IgG followed by pig, horse, monkey, and rabbit IgG. IgG from goat, mouse, rat, cow, donkey, chicken, and guinea pig were poor inhibitors of binding. These findings indicate that Mrp preferentially binds human IgG and that this binding contributes to the ability of GAS to resist phagocytosis and may be a factor in the restriction of GAS infections to the human host.
Keywords	Medicine ; R ; Science ; Q
Subject code	572
Language	English
Publishing date	2013-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
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Article ; Online: Diagnostic management of acute pulmonary embolism: a prediction model based on a patient data meta-analysis.

European heart journal

2024 Volume 44, Issue 32, Page(s) 3073–3081

Abstract: Aims: Risk stratification is used for decisions regarding need for imaging in patients with clinically suspected acute pulmonary embolism (PE). The aim was to develop a clinical prediction model that provides an individualized, accurate probability ... ...

Abstract	Aims: Risk stratification is used for decisions regarding need for imaging in patients with clinically suspected acute pulmonary embolism (PE). The aim was to develop a clinical prediction model that provides an individualized, accurate probability estimate for the presence of acute PE in patients with suspected disease based on readily available clinical items and D-dimer concentrations. Methods and results: An individual patient data meta-analysis was performed based on sixteen cross-sectional or prospective studies with data from 28 305 adult patients with clinically suspected PE from various clinical settings, including primary care, emergency care, hospitalized and nursing home patients. A multilevel logistic regression model was built and validated including ten a priori defined objective candidate predictors to predict objectively confirmed PE at baseline or venous thromboembolism (VTE) during follow-up of 30 to 90 days. Multiple imputation was used for missing data. Backward elimination was performed with a P-value <0.10. Discrimination (c-statistic with 95% confidence intervals [CI] and prediction intervals [PI]) and calibration (outcome:expected [O:E] ratio and calibration plot) were evaluated based on internal-external cross-validation. The accuracy of the model was subsequently compared with algorithms based on the Wells score and D-dimer testing. The final model included age (in years), sex, previous VTE, recent surgery or immobilization, haemoptysis, cancer, clinical signs of deep vein thrombosis, inpatient status, D-dimer (in µg/L), and an interaction term between age and D-dimer. The pooled c-statistic was 0.87 (95% CI, 0.85-0.89; 95% PI, 0.77-0.93) and overall calibration was very good (pooled O:E ratio, 0.99; 95% CI, 0.87-1.14; 95% PI, 0.55-1.79). The model slightly overestimated VTE probability in the lower range of estimated probabilities. Discrimination of the current model in the validation data sets was better than that of the Wells score combined with a D-dimer threshold based on age (c-statistic 0.73; 95% CI, 0.70-0.75) or structured clinical pretest probability (c-statistic 0.79; 95% CI, 0.76-0.81). Conclusion: The present model provides an absolute, individualized probability of PE presence in a broad population of patients with suspected PE, with very good discrimination and calibration. Its clinical utility needs to be evaluated in a prospective management or impact study. Registration: PROSPERO ID 89366.
MeSH term(s)	Adult ; Humans ; Venous Thromboembolism/diagnosis ; Venous Thromboembolism/epidemiology ; Prospective Studies ; Cross-Sectional Studies ; Models, Statistical ; Prognosis ; Pulmonary Embolism/diagnosis ; Pulmonary Embolism/epidemiology ; Fibrin Fibrinogen Degradation Products/analysis
Chemical Substances	Fibrin Fibrinogen Degradation Products
Language	English
Publishing date	2024-04-01
Publishing country	England
Document type	Meta-Analysis ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	603098-1
ISSN	1522-9645 ; 0195-668X
ISSN (online)	1522-9645
ISSN	0195-668X
DOI	10.1093/eurheartj/ehad417
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Article ; Online: Promotion of phagocytosis of Streptococcus pyogenes in human blood by a fibrinogen-binding peptide.

Li, Yi / Courtney, Harry S

Microbes and infection

2011 Volume 13, Issue 4, Page(s) 413–418

Abstract: ... if this domain has a therapeutic potential to enhance phagocytosis of S. pyogenes in human blood. Using a series ... to S. pyogenes and promoted phagocytosis of the streptococci in human blood. The data support ... the hypothesis that the binding of fibrinogen by S. pyogenes is centrally involved in their resistance ...

Abstract	The binding of fibrinogen to M-related protein (Mrp) is known to contribute to the ability of Streptococcus pyogenes to evade phagocytosis by preventing the deposition of complement on the streptococcal surface. The objectives of this investigation were to map the common fibrinogen-binding domain of Mrp and to determine if this domain has a therapeutic potential to enhance phagocytosis of S. pyogenes in human blood. Using a series of recombinant, truncated proteins of Mrp, two fibrinogen-binding domains (FBD) were mapped. FBD1 was contained within amino acid residues 1-55 of Mrp and FBD2 within residues 81-138. FBD2 is found in all Mrp sequenced to date whereas FBD1 is not. Both FBD1 and FBD2 peptides but not a control peptide blocked the binding of fibrinogen to S. pyogenes and promoted phagocytosis of the streptococci in human blood. The data support the hypothesis that the binding of fibrinogen by S. pyogenes is centrally involved in their resistance to phagocytosis in human blood and suggest that treatments that interfere with the binding of fibrinogen to S. pyogenes may help in fighting infections by these organisms.
MeSH term(s)	Amino Acid Sequence ; Blood/microbiology ; Fibrinogen/metabolism ; Humans ; Molecular Sequence Data ; Peptides/chemistry ; Peptides/genetics ; Peptides/metabolism ; Peptides/pharmacology ; Phagocytosis/drug effects ; Phagocytosis/immunology ; Phylogeny ; Protein Binding ; Protein Interaction Domains and Motifs/genetics ; Protein Interaction Domains and Motifs/immunology ; Sequence Alignment ; Sequence Homology, Amino Acid ; Streptococcus pyogenes/classification ; Streptococcus pyogenes/immunology
Chemical Substances	Peptides ; Fibrinogen (9001-32-5)
Language	English
Publishing date	2011-04
Publishing country	France
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1465093-9
ISSN	1769-714X ; 1286-4579
ISSN (online)	1769-714X
ISSN	1286-4579
DOI	10.1016/j.micinf.2010.12.008
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Article ; Online: Wild herbivores enhance resistance to invasion by exotic cacti in an African savanna

Wells, Harry B. M. / Crego, Ramiro D. / Alston, Jesse M. / Ndung'u, S. Kimani / Khasoha, Leo M. / Reed, Courtney G. / Hassan, Abdikadir A. / Kurukura, Samson / Ekadeli, Jackson / Namoni, Mathew / Stewart, Peter S. / Kimuyu, Duncan M. / Wolf, Amelia A. / Young, Truman P. / Kartzinel, Tyler R. / Palmer, Todd M. / Goheen, Jacob R. / Pringle, Robert M.

Journal of Ecology. 2023 Jan., v. 111, no. 1 p.33-44

2023

Abstract: Whether wild herbivores confer biotic resistance to invasion by exotic plants remains a key question in ecology. There is evidence that wild herbivores can impede invasion by exotic plants, but it is unclear whether and how this generalises across ... ...

Abstract	Whether wild herbivores confer biotic resistance to invasion by exotic plants remains a key question in ecology. There is evidence that wild herbivores can impede invasion by exotic plants, but it is unclear whether and how this generalises across ecosystems with varying wild herbivore diversity and functional groups of plants, particularly over long‐term (decadal) time frames. Using data from three long‐term (13‐ to 26‐year) exclosure experiments in central Kenya, we tested the effects of wild herbivores on the density of exotic invasive cacti, Opuntia stricta and O. ficus‐indica (collectively, Opuntia), which are among the worst invasive species globally. We also examined relationships between wild herbivore richness and elephant occurrence probability with the probability of O. stricta presence at the landscape level (6150 km²). Opuntia densities were 74% to 99% lower in almost all plots accessible to wild herbivores compared to exclosure plots. Opuntia densities also increased more rapidly across time in plots excluding wild herbivores. These effects were largely driven by megaherbivores (≥1000 kg), particularly elephants. At the landscape level, modelled Opuntia stricta occurrence probability was negatively correlated with estimated species richness of wild herbivores and elephant occurrence probability. On average, O. stricta occurrence probability fell from ~0.56 to ~0.45 as wild herbivore richness increased from 6 to 10 species and fell from ~0.57 to ~0.40 as elephant occurrence probability increased from ~0.41 to ~0.84. These multi‐scale results suggest that any facilitative effects of Opuntia by wild herbivores (e.g. seed/vegetative dispersal) are overridden by suppression (e.g. consumption, uprooting, trampling). Synthesis. Our experimental and observational findings that wild herbivores confer resistance to invasion by exotic cacti add to evidence that conserving and restoring native herbivore assemblages (particularly megaherbivores) can increase community resistance to plant invasions.
Keywords	Opuntia stricta ; herbivores ; invasive species ; landscapes ; probability ; savannas ; species richness ; Kenya
Language	English
Dates of publication	2023-01
Size	p. 33-44.
Publishing place	John Wiley & Sons, Ltd
Document type	Article ; Online
Note	JOURNAL ARTICLE
ZDB-ID	3023-5
ISSN	0022-0477
ISSN	0022-0477
DOI	10.1111/1365-2745.14010
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: TosR-Mediated Regulation of Adhesins and Biofilm Formation in Uropathogenic Escherichia coli.

Luterbach, Courtney L / Forsyth, Valerie S / Engstrom, Michael D / Mobley, Harry L T

mSphere

2018 Volume 3, Issue 3

Abstract: ... ...

Abstract	Uropathogenic
MeSH term(s)	Adhesins, Escherichia coli/biosynthesis ; Biofilms/growth & development ; Escherichia coli Proteins/metabolism ; Gene Deletion ; Gene Expression Profiling ; Gene Expression Regulation, Bacterial ; Gene Regulatory Networks ; Genetic Complementation Test ; Metabolic Networks and Pathways/genetics ; Real-Time Polymerase Chain Reaction ; Regulon ; Repressor Proteins/metabolism ; Uropathogenic Escherichia coli/genetics ; Uropathogenic Escherichia coli/physiology
Chemical Substances	Adhesins, Escherichia coli ; Escherichia coli Proteins ; Repressor Proteins ; TosR protein, E coli
Language	English
Publishing date	2018-05-16
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	2379-5042
ISSN (online)	2379-5042
DOI	10.1128/mSphere.00222-18
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Article ; Online: The structure and function of serum opacity factor: a unique streptococcal virulence determinant that targets high-density lipoproteins.

Courtney, Harry S / Pownall, Henry J

Journal of biomedicine & biotechnology

2010 Volume 2010, Page(s) 956071

Abstract: Serum opacity factor (SOF) is a virulence determinant expressed by a variety of streptococcal and staphylococcal species including both human and animal pathogens. SOF derives its name from its ability to opacify serum where it targets and disrupts the ... ...

Abstract	Serum opacity factor (SOF) is a virulence determinant expressed by a variety of streptococcal and staphylococcal species including both human and animal pathogens. SOF derives its name from its ability to opacify serum where it targets and disrupts the structure of high-density lipoproteins resulting in formation of large lipid vesicles that cause the serum to become cloudy. SOF is a multifunctional protein and in addition to its opacification activity, it binds to a number of host proteins that mediate adhesion of streptococci to host cells, and it plays a role in resistance to phagocytosis in human blood. This article will provide an overview of the structure and function of SOF, its role in the pathogenesis of streptococcal infections, its vaccine potential, its prevalence and distribution in bacteria, and the molecular mechanism whereby SOF opacifies serum and how an understanding of this mechanism may lead to therapies for reducing high-cholesterol concentrations in blood, a major risk factor for cardiovascular disease.
MeSH term(s)	Bacterial Vaccines/immunology ; Biological Assay ; Humans ; Lipoproteins, HDL/metabolism ; Peptide Hydrolases/chemistry ; Peptide Hydrolases/genetics ; Peptide Hydrolases/metabolism ; Streptococcus/genetics ; Streptococcus/immunology ; Streptococcus/pathogenicity ; Virulence
Chemical Substances	Bacterial Vaccines ; Lipoproteins, HDL ; opacity factor ; Peptide Hydrolases (EC 3.4.-)
Language	English
Publishing date	2010-07-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
ZDB-ID	2052552-7
ISSN	1110-7251 ; 1110-7243
ISSN (online)	1110-7251
ISSN	1110-7243
DOI	10.1155/2010/956071
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Article ; Online: Ciprofloxacin and Rifampin Dual Antibiotic-Loaded Biopolymer Chitosan Sponge for Bacterial Inhibition.

Wells, Carlos M / Beenken, Karen E / Smeltzer, Mark S / Courtney, Harry S / Jennings, Jessica A / Haggard, Warren O

Military medicine

2018 Volume 183, Issue suppl_1, Page(s) 433–444

Abstract: ... of vancomycin-resistant S. aureus has become a critical challenge in nosocomial infection prevention in the USA ... model (S. aureus and Escherichia coli) the combination was able to achieve complete clearance ...

Abstract	Complex extremity wounds in Wounded Warriors can become contaminated with microbes, which may cause clinical outcomes resulting in amputation, morbidity, or even fatality. Local delivery of multiple or broad-spectrum antibiotics allows practicing clinicians treatment solutions that may inhibit biofilm formation. Propagation of vancomycin-resistant Staphylococcus aureus is also a growing concern. The development of vancomycin-resistant S. aureus has become a critical challenge in nosocomial infection prevention in the USA, but to date has seen little occurrence in osteomyelitis. As an alternative, locally delivered ciprofloxacin and rifampin were investigated in a preclinical model for the prevention of biofilm in complex extremity wounds with implanted fixation device. In vitro assays demonstrated ciprofloxacin and rifampin possess an additive effect against Gram-negative Pseudomonas aeruginosa and were actively eluted from a chitosan sponge based local delivery system. In an in vivo orthopedic hardware-associated polymicrobial model (S. aureus and Escherichia coli) the combination was able to achieve complete clearance of both bacterial strains. E. coli was detected in bone of untreated animals, but did not form biofilm on wires. Results reveal the clinical potential of antibiotic-loaded chitosan sponges to inhibit infection through tailored antibiotic selection at desired concentrations with efficacy towards biofilm inhibition.
MeSH term(s)	Analysis of Variance ; Animals ; Anti-Bacterial Agents/administration & dosage ; Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/therapeutic use ; Bacterial Infections/drug therapy ; Bacterial Infections/prevention & control ; Biopolymers/pharmacology ; Biopolymers/therapeutic use ; Chitosan/pharmacology ; Chitosan/therapeutic use ; Chromatography, High Pressure Liquid/methods ; Ciprofloxacin/administration & dosage ; Ciprofloxacin/therapeutic use ; Mice ; Microbial Sensitivity Tests/methods ; Rifampin/administration & dosage ; Rifampin/therapeutic use ; Staphylococcus aureus/drug effects
Chemical Substances	Anti-Bacterial Agents ; Biopolymers ; Ciprofloxacin (5E8K9I0O4U) ; Chitosan (9012-76-4) ; Rifampin (VJT6J7R4TR)
Language	English
Publishing date	2018-04-07
Publishing country	England
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	391061-1
ISSN	1930-613X ; 0026-4075
ISSN (online)	1930-613X
ISSN	0026-4075
DOI	10.1093/milmed/usx150
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Article ; Online: Cis-2-decenoic acid inhibits S. aureus growth and biofilm in vitro: a pilot study.

Jennings, Jessica Amber / Courtney, Harry S / Haggard, Warren O

Clinical orthopaedics and related research

2012 Volume 470, Issue 10, Page(s) 2663–2670

Abstract: Background: Cis-2 decenoic acid (C2DA) disperses biofilm in many strains of microorganisms. However, whether C2DA inhibits bacterial growth or has potential to boost the actions of antibiotics is unknown.: Questions/purposes: We asked whether (1) ... ...

Abstract	Background: Cis-2 decenoic acid (C2DA) disperses biofilm in many strains of microorganisms. However, whether C2DA inhibits bacterial growth or has potential to boost the actions of antibiotics is unknown. Questions/purposes: We asked whether (1) C2DA inhibited MRSA growth and biofilm, (2) antibiotics increased inhibitory effects, (3) inhibitory concentrations of C2DA were cytotoxic to human cells, and (4) effective concentrations could be delivered from a chitosan sponge drug delivery device. Methods: Broth containing seven concentrations of C2DA and six concentrations of either daptomycin, vancomycin, or linezolid was inoculated with a clinical isolate of MRSA and added to a total of 504 coated microtiter plate wells in triplicate (n = 3) for turbidity bacterial growth and crystal violet biofilm mass quantification. We used fibroblast cell viability assays of six C2DA concentrations (n = 4) to evaluate preliminary biocompatibility. We measured the elution of C2DA from a chitosan sponge drug delivery device with two representative loading concentrations (n = 3). Results: C2DA at concentrations of 500 μg/mL and above inhibited growth, while 125 μg/mL C2DA inhibited biofilm. Combination with antibiotics increased these effects. At concentrations up to 500 μg/mL, there were no cytotoxic effects on fibroblasts. Chitosan sponges loaded with 100 mg of C2DA eluted concentrations at or above biofilm-inhibitory concentrations for 5 days. Conclusions: C2DA inhibited biofilm formation by MRSA at biocompatible concentrations, with increasing biofilm reduction with added antibiotics. Elution of C2DA from a chitosan sponge can be modified through adjusting loading concentration. Clinical relevance: By inhibiting biofilm formation on implant surfaces, C2DA may reduce the number of infections in musculoskeletal trauma.
MeSH term(s)	Biofilms/drug effects ; Biofilms/growth & development ; Fatty Acids, Monounsaturated/pharmacology ; Humans ; Methicillin-Resistant Staphylococcus aureus/drug effects ; Methicillin-Resistant Staphylococcus aureus/growth & development ; Microbial Sensitivity Tests ; Pilot Projects
Chemical Substances	Fatty Acids, Monounsaturated ; 2-decenoic acid (332T8TH7B1)
Language	English
Publishing date	2012-05-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	80301-7
ISSN	1528-1132 ; 0009-921X
ISSN (online)	1528-1132
ISSN	0009-921X
DOI	10.1007/s11999-012-2388-2
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