A class of natural cyclic peptide antibiotics produced by certain subspecies of STREPTOMYCES. They include two structurally unrelated components, STREPTOGRAMIN GROUP A and STREPTOGRAMIN GROUP B, which generally act synergistically to inhibit bacterial growth.
A cyclic polypeptide antibiotic complex from Streptomyces virginiae, S. loidensis, S. mitakaensis, S. pristina-spiralis, S. ostreogriseus, and others. It consists of 2 major components, VIRGINIAMYCIN FACTOR M1 and virginiamycin Factor S1. It is used to treat infections with gram-positive organisms and as a growth promoter in cattle, swine, and poultry.
A specific streptogramin group A antibiotic produced by Streptomyces graminofaciens and other bacteria.
An antibiotic mixture originally isolated from Streptomyces pristinaspiralis. It is a mixture of compounds from STREPTOGRAMIN GROUP A: pristinamycin IIA and IIB and from STREPTOGRAMIN GROUP B: pristinamycin IA, pristinamycin IB, pristinamycin IC.
A family of LINCOMYCIN-related glycosides that contain a pyrrolidine ring linked via an amide-bond to a pyranose moiety. Individual members of this family are defined by the arrangement of specific constituent groups on the lyncomycin molecule. Many lincosamides are ANTIBIOTICS produced by a variety STREPTOMYCES species.
Substances that reduce the growth or reproduction of BACTERIA.
A genus of gram-positive aerobic cocci found in the soil, that is highly resistant to radiation, especially ionizing radiation (RADIATION, IONIZING). Deinococcus radiodurans is the type species.
Constituent of 50S subunit of prokaryotic ribosomes containing about 3200 nucleotides. 23S rRNA is involved in the initiation of polypeptide synthesis.
A group of often glycosylated macrocyclic compounds formed by chain extension of multiple PROPIONATES cyclized into a large (typically 12, 14, or 16)-membered lactone. Macrolides belong to the POLYKETIDES class of natural products, and many members exhibit ANTIBIOTIC properties.
The ability of microorganisms, especially bacteria, to resist or to become tolerant to chemotherapeutic agents, antimicrobial agents, or antibiotics. This resistance may be acquired through gene mutation or foreign DNA in transmissible plasmids (R FACTORS).
Acyltransferases that use AMINO ACYL TRNA as the amino acid donor in formation of a peptide bond. There are ribosomal and non-ribosomal peptidyltransferases.
Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.
Any tests that demonstrate the relative efficacy of different chemotherapeutic agents against specific microorganisms (i.e., bacteria, fungi, viruses).

The lactococcal secondary multidrug transporter LmrP confers resistance to lincosamides, macrolides, streptogramins and tetracyclines. (1/29)

The active efflux of toxic compounds by (multi)drug transporters is one of the mechanisms that bacteria have developed to resist cytotoxic drugs. The authors describe the role of the lactococcal secondary multidrug transporter LmrP in the resistance to a broad range of clinically important antibiotics. Cells expressing LmrP display an increased resistance to the lincosamide, streptogramin, tetracycline and 14- and 15-membered macrolide antibiotics. The streptogramin antibiotic quinupristin, present in the fourth-generation antibiotic RP 59500, can inhibit LmrP-mediated Hoechst 33342 transport, but is not transported by LmrP, indicating that quinupristin acts as a modulator of LmrP activity. LmrP-expressing Lactococcus lactis cells in which a proton-motive force is generated accumulate significantly less tetracycline than control cells without LmrP expression. In contrast, LmrP-expressing and control cells accumulate equal amounts of tetracycline in the absence of metabolic energy. These findings demonstrate that the increased antibiotic resistance in LmrP-expressing cells is a result of the active extrusion of antibiotics from the cell.  (+info)

Indication of transposition of a mobile DNA element containing the vat(D) and erm(B) genes in Enterococcus faecium. (2/29)

The vat(D) and erm(B) genes encoding streptogramin resistance in Enterococcus faecium transferred together, and a direct physical link between erm(B) and vat(D) was detected. Both the vat(D) and erm(B) probes hybridized to fragments of different sizes in the donor and transconjugants, which indicated a transposition event.  (+info)

Diversity of ribosomal mutations conferring resistance to macrolides, clindamycin, streptogramin, and telithromycin in Streptococcus pneumoniae. (3/29)

Mechanisms of resistance were studied in 22 macrolide-resistant mutants selected in vitro from 5 parental strains of macrolide-susceptible Streptococcus pneumoniae by serial passage in various macrolides (T. A. Davies, B. E. Dewasse, M. R. Jacobs, and P. C. Appelbaum, Antimicrob. Agents Chemother., 44:414-417, 2000). Portions of genes encoding ribosomal proteins L22 and L4 and 23S rRNA (domains II and V) were amplified by PCR and analyzed by single-strand conformational polymorphism analysis to screen for mutations. The DNA sequences of amplicons from mutants that differed from those of parental strains by their electrophoretic migration profiles were determined. In six mutants, point mutations were detected in the L22 gene (G95D, P99Q, A93E, P91S, and G83E). The only mutant selected by telithromycin (for which the MIC increased from 0.008 to 0.25 microg/ml) contained a combination of three mutations in the L22 gene (A93E, P91S, and G83E). L22 mutations were combined with an L4 mutation (G71R) in one strain and with a 23S rRNA mutation (C2611A) in another strain. Nine other strains selected by various macrolides had A2058G (n = 1), A2058U (n = 2), A2059G (n = 1), C2610U (n = 1), and C2611U (n = 4) mutations (Escherichia coli numbering) in domain V of 23S rRNA. One mutant selected by clarithromycin and resistant to all macrolides tested (MIC, >32 microg/ml) and telithromycin (MIC, 4 microg/ml) had a single base deletion (A752) in domain II. In six remaining mutants, no mutations in L22, L4, or 23S rRNA could be detected.  (+info)

Prevalence of resistance to macrolide, lincosamide and streptogramin antibiotics in Gram-positive cocci isolated in a Korean hospital. (4/29)

To investigate the prevalence of resistance to macrolide, lincosamide and streptogramin (MLS) antibiotics in Gram-positive cocci isolated in a Korean hospital, we tested the antibiotic susceptibility of 1097 clinical isolates of Staphylococcus aureus, coagulase-negative staphylococci (CNS) and enterococci to the macrolides erythromycin, clarithromycin, azithromycin and josamycin, the lincosamide clindamycin and the streptogramin pristinamycin. These three groups of organisms were mostly resistant to macrolides and lincosamide, but were commonly susceptible to pristinamycin. The resistance phenotypes of erythromycin-resistant isolates were determined by the double-disc test with erythromycin and clindamycin, which showed that most exhibited constitutive MLS resistance. In order to determine the prevalence of the resistance genotypes and the resistance mechanisms, the presence of the erm(A), erm(B), erm(C) and mef genes in the erythromycin-resistant isolates was identified by PCR analysis. The resistance was due mainly to the presence of erm(A) in S. aureus (82.5%), erm(B) in enterococci (55%) and erm(C) in CNS (47.2%).  (+info)

Novel locus required for expression of high-level macrolide-lincosamide-streptogramin B resistance in Staphylococcus aureus. (5/29)

The yycF1(Ts) mutation in Staphylococcus aureus conferred hypersensitivity to macrolide-lincosamide-streptogramin B (MLS(B)) antibiotics on strains either containing or lacking ermB. The overexpression of the S. aureus Ssa protein restored the yycF1 mutant to wild-type levels of susceptibility. Inactivation of ssa in an unmutagenized strain dramatically reduced ermB-based resistance. Conditional loss of function or expression of ssa in the yycF1 mutant is proposed to result in the observed hypersensitivity to MLS(B) antibiotics.  (+info)

Prevalence of streptogramin resistance genes among Enterococcus isolates recovered from retail meats in the Greater Washington DC area. (6/29)

The prevalence of streptogramin resistance genes in enterococci recovered from retail poultry in the Greater Washington DC area was examined. Forty-three chicken and 32 turkey retail samples were analysed. Thirty-one non-Enterococcus faecalis enterococcal strains were isolated that displayed MICs of quinupristin-dalfopristin and virginiamycin of > or = 4 mg/L. These included Enterococcus faecium (turkey n = 4, chicken n = 23), Enterococcus gallinarum (turkey n = 2, chicken n = 1) and Enterococcus hirae (chicken n = 1). The presence of streptogramin resistance genes was examined by PCR in all non-E. faecalis isolates. The vat(E) gene was detected in 10/23 chicken E. faecium and from 2/4 turkey E. faecium. No other streptogramin resistance genes were detected by PCR. In addition, erm(B) was detected in all the E. faecium and E. gallinarum found in turkeys and in 7/23 E. faecium found in chickens. The vat(E) gene was transferable by conjugation from only two of the 12 E. faecium isolates (one from chicken and one from turkey). This study suggests that there is a high prevalence of low-level streptogramin resistance among enterococci found in retail poultry and that other, yet to be identified, mechanisms operate in these isolates that confer streptogramin resistance in enterococci.  (+info)

Oral streptogramins in the management of patients with methicillin-resistant Staphylococcus aureus (MRSA) infections. (7/29)

OBJECTIVES: Chronic methicillin-resistant Staphylococcus aureus (MRSA) infections in debilitated patients are difficult to treat. We studied the clinical efficacy and safety of an oral streptogramin, pristinamycin, for these patients. PATIENTS AND METHODS: Patients were admitted consecutively to receive pristinamycin, usually with doxycycline, for 7-21 days. Fifty-six patients (average age 75 years) from hospital and community were treated for skin, soft tissue, chest and other infections. RESULTS: The overall clinical response rate was 39 of 53 patients (74%; 95% CI: 60%, 85%) cured or substantially improved, from 53 of 56 (95%) patients clinically and 49 of 56 (87.5%) patients bacteriologically evaluable. Toxic effects comprised gastrointestinal disturbances in eight patients (14%) and one (2%) possible skin rash. CONCLUSION: This study suggests that oral streptogramins may be useful in the management of debilitated patients with MRSA infections.  (+info)

Isolation of streptogramin-resistant Enterococcus faecium from human and non-human sources in a rural community. (8/29)

OBJECTIVES: To detect quinupristin-dalfopristin and virginiamycin M1 resistance in Enterococcus faecium from human, food and environmental sources. MATERIALS AND METHODS: Enterococcal isolates derived from human faeces and urine, meat and seawater were screened for resistance to quinupristin-dalfopristin and virginiamycin M1 by an agar dilution method. Identification of all E. faecium strains and the presence of streptogramin acetyltransferase genes were confirmed using a PCR method. RESULTS: No high-level quinupristin-dalfopristin-resistant strains were isolated. Two isolates from faeces and five from seawater were confirmed to be high-level virginiamycin M1-resistant E. faecium (MIC 32 mg/L); none of these carried the vat(D) or vat(E) acetyltransferase genes that mediate high-level resistance to streptogramin A compounds. CONCLUSION: High-level quinupristin-dalfopristin-resistant strains of E. faecium are uncommon in Cornwall. However streptogramin A-resistant strains were detected from human and animal sources.  (+info)

Streptogramins are a class of antibiotics produced by various species of Streptomyces bacteria. They are composed of two components, Group A and Group B, that work synergistically to inhibit bacterial protein synthesis. The combination of these two groups is often referred to as a "streptogramin pair."

Streptogramin A binds to the peptidyl transferase center of the 50S ribosomal subunit and prevents the addition of new amino acids to the growing peptide chain. Streptogramin B, on the other hand, binds to a different site on the 50S subunit and causes conformational changes that enhance the activity of streptogramin A.

Together, these antibiotics inhibit bacterial protein synthesis and disrupt bacterial growth, making them effective against a range of Gram-positive bacteria, including some drug-resistant strains. Examples of streptogramins include dalfopristin, quinupristin, and pristinamycin. They are often used in combination with other antibiotics to treat serious infections caused by methicillin-resistant Staphylococcus aureus (MRSA) and vancomycin-resistant Enterococci (VRE).

Virginiamycin is not a medical condition or disease, but rather an antibiotic used in veterinary medicine to promote growth and prevent or treat certain bacterial infections in animals, particularly in livestock such as cattle, swine, and poultry. It is a mixture of two components, virginiamycin M1 and virginiamycin S1, which have antibacterial properties against gram-positive bacteria.

Virginiamycin belongs to the streptogramin class of antibiotics and works by binding to the bacterial ribosome, inhibiting protein synthesis and ultimately killing the bacteria. It is not approved for use in humans, except under certain circumstances as part of an investigational new drug (IND) protocol or in specific medical devices.

It's important to note that the use of antibiotics in livestock can contribute to the development of antibiotic-resistant bacteria, which can have negative impacts on human health. Therefore, responsible and judicious use of antibiotics is essential to minimize this risk.

Streptogramin A is not a medical condition or disease, but rather a type of antibiotic. According to the World Health Organization (WHO) and other medical sources, streptogramins are a class of antibiotics that are produced by certain species of Streptomyces bacteria. They consist of two components, streptogramin A and streptogramin B, which work together to inhibit bacterial protein synthesis.

Specifically, streptogramin A binds to the peptidyl transferase center of the ribosome and blocks the formation of new peptide bonds, while streptogramin B binds to a different site on the ribosome and helps to stabilize the interaction between streptogramin A and the ribosome. This dual action makes streptogramins effective against a wide range of bacteria, including some that are resistant to other antibiotics.

However, it's worth noting that the use of streptogramins is generally reserved for serious infections that are unresponsive to other treatments, due to their potential side effects and the risk of developing resistance. They are typically administered in combination with other antibiotics, such as streptogramin B, to enhance their effectiveness and reduce the likelihood of resistance.

Pristinamycin is an antibiotic that belongs to the streptogramin class. It is composed of two components, pristinamycin I and pristinamycin IIA, which work synergistically to inhibit bacterial protein synthesis. Pristinamycin is primarily used in the treatment of severe skin and soft tissue infections, including those caused by methicillin-resistant Staphylococcus aureus (MRSA) and vancomycin-resistant Enterococci (VRE). It is important to note that pristinamycin's use is more common in European countries than in the United States.

Lincosamides are a class of antibiotics that are structurally related to limcosamine and consist of lincomycin and its derivatives such as clindamycin. They bind to the 50S ribosomal subunit and inhibit bacterial protein synthesis. These antibiotics have a bacteriostatic effect and are primarily used to treat anaerobic infections, as well as some Gram-positive bacterial infections. Common side effects include gastrointestinal symptoms such as diarrhea and nausea. Additionally, lincosamides can cause pseudomembranous colitis, a potentially serious condition caused by the overgrowth of Clostridium difficile bacteria in the gut.

Anti-bacterial agents, also known as antibiotics, are a type of medication used to treat infections caused by bacteria. These agents work by either killing the bacteria or inhibiting their growth and reproduction. There are several different classes of anti-bacterial agents, including penicillins, cephalosporins, fluoroquinolones, macrolides, and tetracyclines, among others. Each class of antibiotic has a specific mechanism of action and is used to treat certain types of bacterial infections. It's important to note that anti-bacterial agents are not effective against viral infections, such as the common cold or flu. Misuse and overuse of antibiotics can lead to antibiotic resistance, which is a significant global health concern.

'Deinococcus' is a genus of bacteria that are characterized by their extreme resistance to various environmental stresses, such as radiation, desiccation, and oxidative damage. The most well-known species in this genus is Deinococcus radiodurans, which is often referred to as "conan the bacterium" because of its exceptional ability to survive high doses of ionizing radiation that would be lethal to most other organisms.

Deinococcus bacteria have a unique cell wall structure and contain multiple copies of their chromosome, which may contribute to their resistance to DNA damage. They are typically found in environments with high levels of radiation or oxidative stress, such as radioactive waste sites, dry deserts, and the gut of animals. While some species of Deinococcus have been shown to have potential applications in bioremediation and other industrial processes, others are considered opportunistic pathogens that can cause infections in humans with weakened immune systems.

23S Ribosomal RNA (rRNA) is a type of rRNA that is a component of the large ribosomal subunit in both prokaryotic and eukaryotic cells. In prokaryotes, the large ribosomal subunit contains 50S, which consists of 23S rRNA, 5S rRNA, and around 33 proteins. The 23S rRNA plays a crucial role in the decoding of mRNA during protein synthesis and also participates in the formation of the peptidyl transferase center, where peptide bonds are formed between amino acids.

The 23S rRNA is a long RNA molecule that contains both coding and non-coding regions. It has a complex secondary structure, which includes several domains and subdomains, as well as numerous stem-loop structures. These structures are important for the proper functioning of the ribosome during protein synthesis.

In addition to its role in protein synthesis, 23S rRNA has been used as a target for antibiotics that inhibit bacterial growth. For example, certain antibiotics bind to specific regions of the 23S rRNA and interfere with the function of the ribosome, thereby preventing bacterial protein synthesis and growth. However, because eukaryotic cells do not have a 23S rRNA equivalent, these antibiotics are generally not toxic to human cells.

Macrolides are a class of antibiotics derived from natural products obtained from various species of Streptomyces bacteria. They have a large ring structure consisting of 12, 14, or 15 atoms, to which one or more sugar molecules are attached. Macrolides inhibit bacterial protein synthesis by binding to the 50S ribosomal subunit, thereby preventing peptide bond formation. Common examples of macrolides include erythromycin, azithromycin, and clarithromycin. They are primarily used to treat respiratory, skin, and soft tissue infections caused by susceptible gram-positive and gram-negative bacteria.

Microbial drug resistance is a significant medical issue that refers to the ability of microorganisms (such as bacteria, viruses, fungi, or parasites) to withstand or survive exposure to drugs or medications designed to kill them or limit their growth. This phenomenon has become a major global health concern, particularly in the context of bacterial infections, where it is also known as antibiotic resistance.

Drug resistance arises due to genetic changes in microorganisms that enable them to modify or bypass the effects of antimicrobial agents. These genetic alterations can be caused by mutations or the acquisition of resistance genes through horizontal gene transfer. The resistant microbes then replicate and multiply, forming populations that are increasingly difficult to eradicate with conventional treatments.

The consequences of drug-resistant infections include increased morbidity, mortality, healthcare costs, and the potential for widespread outbreaks. Factors contributing to the emergence and spread of microbial drug resistance include the overuse or misuse of antimicrobials, poor infection control practices, and inadequate surveillance systems.

To address this challenge, it is crucial to promote prudent antibiotic use, strengthen infection prevention and control measures, develop new antimicrobial agents, and invest in research to better understand the mechanisms underlying drug resistance.

Peptidyl transferase is not a medical term per se, but rather a biochemical term used to describe an enzymatic function or activity. It is often mentioned in the context of molecular biology, protein synthesis, and ribosome structure.

Peptidyl transferase refers to the catalytic activity of ribosomes that facilitates the formation of peptide bonds between amino acids during protein synthesis. More specifically, peptidyl transferase is responsible for transferring the peptidyl group (the growing polypeptide chain) from the acceptor site (A-site) to the donor site (P-site) of the ribosome, creating a new peptide bond and elongating the polypeptide chain. This activity occurs within the large subunit of the ribosome, near the peptidyl transferase center (PTC).

While it is often attributed to the ribosomal RNA (rRNA) component of the ribosome, recent research suggests that both rRNA and specific ribosomal proteins contribute to this enzymatic activity.

Ribosomes are complex macromolecular structures composed of ribonucleic acid (RNA) and proteins that play a crucial role in protein synthesis within cells. They serve as the site for translation, where messenger RNA (mRNA) is translated into a specific sequence of amino acids to create a polypeptide chain, which eventually folds into a functional protein.

Ribosomes consist of two subunits: a smaller subunit and a larger subunit. These subunits are composed of ribosomal RNA (rRNA) molecules and proteins. In eukaryotic cells, the smaller subunit is denoted as the 40S subunit, while the larger subunit is referred to as the 60S subunit. In prokaryotic cells, these subunits are named the 30S and 50S subunits, respectively. The ribosome's overall structure resembles a "doughnut" or a "cotton reel," with grooves and binding sites for various factors involved in protein synthesis.

Ribosomes can be found floating freely within the cytoplasm of cells or attached to the endoplasmic reticulum (ER) membrane, forming part of the rough ER. Membrane-bound ribosomes are responsible for synthesizing proteins that will be transported across the ER and ultimately secreted from the cell or inserted into the membrane. In contrast, cytoplasmic ribosomes synthesize proteins destined for use within the cytoplasm or organelles.

In summary, ribosomes are essential components of cells that facilitate protein synthesis by translating mRNA into functional polypeptide chains. They can be found in various cellular locations and exist as either free-floating entities or membrane-bound structures.

Microbial sensitivity tests, also known as antibiotic susceptibility tests (ASTs) or bacterial susceptibility tests, are laboratory procedures used to determine the effectiveness of various antimicrobial agents against specific microorganisms isolated from a patient's infection. These tests help healthcare providers identify which antibiotics will be most effective in treating an infection and which ones should be avoided due to resistance. The results of these tests can guide appropriate antibiotic therapy, minimize the potential for antibiotic resistance, improve clinical outcomes, and reduce unnecessary side effects or toxicity from ineffective antimicrobials.

There are several methods for performing microbial sensitivity tests, including:

1. Disk diffusion method (Kirby-Bauer test): A standardized paper disk containing a predetermined amount of an antibiotic is placed on an agar plate that has been inoculated with the isolated microorganism. After incubation, the zone of inhibition around the disk is measured to determine the susceptibility or resistance of the organism to that particular antibiotic.
2. Broth dilution method: A series of tubes or wells containing decreasing concentrations of an antimicrobial agent are inoculated with a standardized microbial suspension. After incubation, the minimum inhibitory concentration (MIC) is determined by observing the lowest concentration of the antibiotic that prevents visible growth of the organism.
3. Automated systems: These use sophisticated technology to perform both disk diffusion and broth dilution methods automatically, providing rapid and accurate results for a wide range of microorganisms and antimicrobial agents.

The interpretation of microbial sensitivity test results should be done cautiously, considering factors such as the site of infection, pharmacokinetics and pharmacodynamics of the antibiotic, potential toxicity, and local resistance patterns. Regular monitoring of susceptibility patterns and ongoing antimicrobial stewardship programs are essential to ensure optimal use of these tests and to minimize the development of antibiotic resistance.

"Lincosamides, Oxazolidinones, and Streptogramins". Merck Manual of Diagnosis and Therapy. Merck & Co. May 2020. Archived from ... Tetracyclines, Macrolides, Clindamycin, Chloramphenicol, Streptogramins, & Oxazolidinones. In: Katzung BG. eds. Basic & ...
Streptogramins are a class of antibiotics. Streptogramins are effective in the treatment of vancomycin-resistant Staphylococcus ...
Osono, T.; Umezawa, H. (July 1985). "Pharmacokinetics of macrolides, lincosamides and streptogramins". The Journal of ... lincosamides and streptogramins B. The gene family responsible for encoding of these methyltransferases is referred to as the " ...
Chloramphenicol, Tetracyclines, Macrolides, Clindamycin, Streptogramins, & Linezolid , Katzung & Trevor's Pharmacology: ...
When both streptogramins are bound to the ribosome, they form an extremely stable ternary complex. In 1999 the FDA had approved ... By themselves, streptogramins A and B are bacteriostatic. However, when used in conjunction with one another, the ... Streptogramin A is a group of antibiotics within the larger family of antibiotics known as streptogramins. They are synthesized ... Vannuffel, P.; Cocito, C. (1996). "Mechanism of action of streptogramins and macrolides". Drugs. 51: 20-30. doi:10.2165/ ...
Streptogramins". Katzung & Trevor's Pharmacology: Examination & Board Review (9th ed.). New York: McGraw-Hill Medical. pp. 389- ...
Streptogramins also cause premature release of the peptide chain. Retapamulin Mupirocin Fusidic acid The following antibiotics ... Macrolides Telithromycin Streptogramins Retapamulin Biology portal Protein biosynthesis Bacterial translation Eukaryotic ...
Streptogramins A and B synergically inhibit cell growth of gram positive, less so gram negative bacteria by inhibiting protein ... The molecular target of streptogramins is the 23S rRNA. Both streptogramin A and B bind to the P binding site of the 50S ... Many of the members of the streptogramins reported in the literature have the same structure and different names; for example, ... Cocito C, Di Giambattista M, Nyssen E, Vannuffel P (May 1997). "Inhibition of protein synthesis by streptogramins and related ...
... a combination of two streptogramins, not active against E. faecalis); daptomycin (Cubicin, a lipopeptide); and ceftobiprole ( ...
Linezolid, daptomycin, tigecycline and the streptogramins (e.g. quinupristin/dalfopristin) can have activity against VRE. VRE ...
8-16 times higher in vitro bactericidal activity is seen against many gram-positive bacteria when the two streptogramins are ...
... streptogramins, rifampicin, fusidic acid, and fosfomycin. P. gergoviae is also resistant to cefoxitin, likely due to β- ...
... and streptogramins (an MLS-resistant phenotype). Two other forms of acquired resistance include the production of drug- ...
... lincosamides and streptogramins and the pS194-like str gene is for chloramphenicol and streptomycin resistance. Genetic ...
Linezolid and Tedizolid Streptogramins such as quinupristin-dalfopristin Advanced generation tetracyclines: Tigecycline, ...
... streptogramins, and phosphonic acid antibiotics. The aminoglycoside antibiotic streptomycin, for example, was discovered from ...
... streptogramins MeSH D04.345.566.802.249 - mikamycin MeSH D04.345.566.802.374 - pristinamycin MeSH D04.345.566.802.500 - ...
... streptogramins MeSH D12.644.641.802.249 - mikamycin MeSH D12.644.641.802.374 - pristinamycin MeSH D12.644.641.802.500 - ...
Streptogramins: Dosing, Uses, Side Effects, Interactions, Patient Handouts, Pricing and more from Medscape Reference ...
They consist of a mixture of two different types of chemical substances - the group A streptogramins, which are polyunsaturated ... Streptogramins are potent drugs against numerous highly resistant pathogens and therefore are used as antibiotics of last- ... Streptogramins - two are better than one! Yvonne Mast et al. Int J Med Microbiol. 2014 Jan. ... Streptogramins - two are better than one! Yvonne Mast 1 , Wolfgang Wohlleben 2 ...
... and Streptogramins - Etiology, pathophysiology, symptoms, signs, diagnosis & prognosis from the MSD Manuals - Medical ... and streptogramins (dalfopristin [streptogramin A] and quinupristin [streptogramin B Quinupristin and Dalfopristin Quinupristin ...
Streptogramins. The failure of glycopeptide antibiotics led to the creation of a new class of drug, the streptogramins, a ...
Mechanism of action of streptogramins and macrolides. Drugs. 1996;51(Suppl 1):20-30. DOIPubMedGoogle Scholar ... Inhibition of protein synthesis by streptogramins and related antibiotics. J Antimicrob Chemother. 1997;39(Suppl A):7-13. DOI ... Macrolides, Lincosamides, and Streptogramins (MLS). Another class of antibacterials containing newly developed bactericidal ... The bactericidal mechanism of action of quinupristin/dalfopristin, a combination of two streptogramins, is unique (65). ...
"Lincosamides, Oxazolidinones, and Streptogramins". Merck Manual of Diagnosis and Therapy. Merck & Co. May 2020. Archived from ... Tetracyclines, Macrolides, Clindamycin, Chloramphenicol, Streptogramins, & Oxazolidinones. In: Katzung BG. eds. Basic & ...
Streptogramins. Virginiamycina. Tetracyclines. Chlortetracyclinea. Oxytetracycline. Tetracycline. aLabeled as growth promoter ...
First of a class of antimicrobial agents known as streptogramins. Works by irreversibly binding to 50S and 70S ribosomes, which ...
The most commonly-detected ARGs encoded resistance to macrolides, lincosamides, and streptogramins (100% of children); ...
resistant to macrolide-lincosamides-streptogramins was mainly isolated on PET [32].. Although non-biodegradable plastic-made ...
The most commonly-detected ARGs encoded resistance to macrolides, lincosamides, and streptogramins (100% of children); ...
Pharmacodynamics of Macrolides, Azalides, and Streptogramins: Effect on Extracellular Pathogens. Clin. Infect. Dis., 27:28-32. ...
Overcoming Bacterial Resistance by Dual Target Inhibition: The Case of Streptogramins. Journal: Current Drug Targets - ...
J01F MACROLIDES, LINCOSAMIDES AND STREPTOGRAMINS. This group comprises macrolide, lincosamide and streptogramin antibacterials ...
Macrolides, ketolides and streptogramins]. Mensa J, García-Vázquez E, Vila J. Mensa J, et al. Enferm Infecc Microbiol Clin. ...
... lincosamides and streptogramins B (MLSB) [45, 54]. This gene was found on chromosomes, plasmids and transposons of ...
This methylase alters the usual ribosomal binding site for macrolides, lincosamides, and the B-streptogramins (quinupristin). ... Resistance to macrolide antibiotics such as azithromycin, clindamycin (a lincosamide antibiotic) and streptogramins, has been ...
... streptogramins, and ansamycins. Among the virulence array there were genes encoding to several factors, like increased serum ...
5. [The correlation between phenotypes and genotypes of macrolides, lincosamides and streptogramins B resistance in ... Resistance to macrolides, lincosamides, streptogramins, and linezolid among members of the Staphylococcus sciuri group. ... Molecular basis of resistance to macrolides, lincosamides and streptogramins in Staphylococcus saprophyticus clinical isolates. ... 4. Distribution of genes encoding resistance to macrolides, lincosamides and streptogramins among clinical staphylococcal ...
... streptogramins, linezolid, and aminoglycosides has been reported.3,4E asburiae is a gramnegative rod that has been isolated ...
The novel and transferable erm(51) gene confers Macrolides, Lincosamides, and Streptogramins B (MLSB) resistance to clonal ...
Streptogramins,N0000011418, Antigens, Bacterial,N0000011417, Indolequinones,N0000011416, Lactams, Macrocyclic,N0000011415, ...
Streptogramins - Preferred Concept UI. M0022748. Scope note. A class of natural cyclic peptide antibiotics produced by certain ...
Streptogramins Preferred Term Term UI T043219. Date12/03/1992. LexicalTag NON. ThesaurusID NLM (1994). ... Streptogramins Preferred Concept UI. M0022748. Registry Number. 0. Scope Note. A class of natural cyclic peptide antibiotics ... 2002; see VIRGINIAMYCIN 1994-2001, see STREPTOGRAMINS 1981-1993. History Note. 2002, 1981-1993; use VIRGINIAMYCIN 1994-2001. ... Streptogramins. Tree Number(s). D04.345.566.802. D12.644.641.802. Unique ID. D025361. RDF Unique Identifier. http://id.nlm.nih. ...
Mechanism of action of streptogramins and macrolides. Drugs. 1996;51(Suppl 1):20-30. DOIPubMedGoogle Scholar ... Inhibition of protein synthesis by streptogramins and related antibiotics. J Antimicrob Chemother. 1997;39(Suppl A):7-13. DOI ... Macrolides, Lincosamides, and Streptogramins (MLS). Another class of antibacterials containing newly developed bactericidal ... The bactericidal mechanism of action of quinupristin/dalfopristin, a combination of two streptogramins, is unique (65). ...
Streptogramins Preferred Term Term UI T043219. Date12/03/1992. LexicalTag NON. ThesaurusID NLM (1994). ... Streptogramins Preferred Concept UI. M0022748. Registry Number. 0. Scope Note. A class of natural cyclic peptide antibiotics ... 2002; see VIRGINIAMYCIN 1994-2001, see STREPTOGRAMINS 1981-1993. History Note. 2002, 1981-1993; use VIRGINIAMYCIN 1994-2001. ... Streptogramins. Tree Number(s). D04.345.566.802. D12.644.641.802. Unique ID. D025361. RDF Unique Identifier. http://id.nlm.nih. ...
Cross-resistance to lincosamides, streptogramins A and pleuromutilins in Streptococcus agalactiae isolates from the USA. ...
Comparison of the tiamulin binding site with other PTC targeting drugs, like chloramphenicol, clindamycin and streptogramins, ...
  • Alteration of the 50S ribosomal subunit reduces the affinity of macrolides linezolid and streptogramins for the ribosome. (med2date.com)
  • Lincosamides, Oxazolidinones, and Streptogramins Lincosamides ( clindamycin), oxazolidinones ( linezolid, tedizolid), and streptogramins ( dalfopristin [streptogramin A] and quinupristin [streptogramin B]) are structurally different but are. (merckmanuals.com)
  • Streptogramins, oxazolidinones, and other inhibitors of bacterial protein synthesis. (mcmaster.ca)
  • The collection was used in a study exploring how the modification of group A streptogramins, a class of antibiotics discovered and isolated in France in the 1960s, can restore their efficacy by enabling them to overcome the resistance mechanisms employed by the bacteria they are intended to destroy. (pasteur.fr)
  • Streptogramins, isolated then brought to market in the early 1960s, are one of the last classes of antibiotics to have been discovered. (pasteur.fr)
  • Quinupristin-dalfopristin, the first formulation of a distinct class of antibiotics known as the streptogramins, has activity against a range of gram-positive bacteria that are usually resistant to other agents, including vancomycin-resistant Enterococcus faecium . (aafp.org)
  • The streptogramins are macromolecular antibiotics produced by Streptomyces pristinaepiralis . (aafp.org)
  • 4 Streptogramins The streptogramin antibiotics were discovered more than four decades ago but until recently were of more academic than practical interest. (forexsignalx.com)
  • His Enterococcus faecium study integrates concerns from other disciplines, such as Enterococcus, Avoparcin, Streptogramins, Enterococcus faecalis and Streptogramin. (research.com)
  • To understand the main determinants behind worldwide antibiotic resistance dynamics, scientists from the Institut Pasteur, Inserm, Université de Versailles Saint-Quentin-en-Yvelines and Université Paris-Saclay developed a statistical model based on a large-scale spatial-temporal analysis. (pasteur.fr)
  • Streptogramins also act on ribosomes 50S subunit and stop the protein synthesis. (askmicrobiology.com)
  • At the Institut Pasteur we worked extensively on genes and mechanisms of resistance to streptogramins in the laboratories led by Névine El Solh and Patrice Courvalin. (pasteur.fr)
  • In this context, the research by chemists at the University of California San Francisco (UCSF) is particularly innovative: they have designed a modular production process entirely based on the use of synthetic precursors, enabling tailored, large-scale modification of the group A component of streptogramins, a component that is vital for the biological efficacy of streptogramins but has a chemically complex structure (macrocyclic lactone with several double bonds). (pasteur.fr)
  • Macrolides, ketolides and streptogramins]. (nih.gov)
  • This methylase alters the usual ribosomal binding site for macrolides, lincosamides, and the B-streptogramins (quinupristin). (khanacademy.org)
  • 4. Distribution of genes encoding resistance to macrolides, lincosamides and streptogramins among clinical staphylococcal isolates in a Turkish university hospital. (nih.gov)
  • 5. [The correlation between phenotypes and genotypes of macrolides, lincosamides and streptogramins B resistance in Staphylococcus aureus]. (nih.gov)
  • 9. [Selection of constitutive mutants of gram-positive cocci inducible resistant to macrolides, lincosamides and streptogramins (MLS): comparison of the selective effects of the MLS]. (nih.gov)
  • 11. Resistance to macrolides, lincosamides, streptogramins, and linezolid among members of the Staphylococcus sciuri group. (nih.gov)
  • 14. Molecular basis of resistance to macrolides, lincosamides and streptogramins in Staphylococcus saprophyticus clinical isolates. (nih.gov)
  • Cross resistance has been demonstrated between lincosamides, macrolides and streptogramins B in some organisms. (nih.gov)
  • The failure of glycopeptide antibiotics led to the creation of a new class of drug, the streptogramins, a combination of quini pristin and dalfopristin. (medscape.com)
  • Resistance to macrolide antibiotics such as azithromycin, clindamycin (a lincosamide antibiotic) and streptogramins, has been demonstrated in vitro. (khanacademy.org)
  • Cross-resistance to lincosamides, streptogramins A and pleuromutilins in Streptococcus agalactiae isolates from the USA. (cdc.gov)
  • Streptogramins are potent drugs against numerous highly resistant pathogens and therefore are used as antibiotics of last-resort human therapy. (nih.gov)
  • First of a class of antimicrobial agents known as streptogramins. (medscape.com)