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At least 19 recordsLinked to original sources
PubMed2005

Prevalence of resistance mechanisms against macrolides and lincosamides in methicillin-resistant coagulase-negative staphylococci in the Czech Republic and occurrence of an undefined mechanism of resistance to lincosamides.

High occurrence of the non-macrolide-lincosamide-streptogramin B resistance genes msrA (53%) and linA/linA' (30%) was found among 98 methicillin-resistant coagulase-negative staphylococci additionally resistant to macrolides and/or lincosamides. The gene msrA predominated in Staphylococcus haemolyticus (43 of 62 isolates). In Staphylococcus epidermidis, it was present in 7 of 27 isolates. A novel mechanism of resistance to lincosamides appears to be present in 10 genetically related isolates of S. haemolyticus in the absence of ermA, ermC, msrA, and linA/linA'.

Anti-Bacterial Agents↗
PubMed1988

Novel mechanisms of resistance to lincosamides in Staphylococcus and Arthrobacter spp.

Clinical isolates of Staphylococcus and Arthrobacter spp. were screened for lincosamide resistance. Six different patterns of resistance were found. Strains designated SF27 and SF28 showed low-level resistance to lincosamides: one was susceptible to erythromycin (SF27) and the other was resistant (SF28). Analysis of ribosomes from the resistant strains in an in vitro poly(U)-dependent protein-synthesizing system showed that ribosomes of both strains were sensitive to lincomycin and clindamycin. Four patterns of high-level resistance to lincosamides were observed (strains SF4, SF19, SF30, and SF31). All of these except SF30 had ribosomes which were highly resistant in vitro to the antibiotics and showed a close correlation with results of the in vivo experiments. In vivo protein synthesis by strain SF30 was resistant to lincomycin and sensitive to clindamycin, whereas the ribosomes were sensitive when assayed in vitro. Lincosamide-inactivating enzymes were not detected in cell extracts of the six resistant strains. Strains SF19 and SF31 demonstrated two ribosome-mediated lincosamides resistance mechanisms that were not previously reported. Both strains were highly resistant to lincosamides and susceptible to erythromycin, but SF19 was also highly resistant to oleandomycin and partially resistant to various macrolides.

Aminoglycosides↗
PubMed1987

Kinetics of binding of macrolides, lincosamides, and synergimycins to ribosomes.

The synergistic effect of type A (virginiamycin M (VM)) and type B (virginiamycin S (VS)) synergimycins and their antagonistic effect against erythromycin (a 14-membered macrolide) for binding to the large ribosomal subunit (50 S) have been related. This investigation has now been extended to 16-membered macrolides (leucomycin A3 and spiramycin) and to lincosamides (lincomycin). A dissociation of VS-ribosome complexes was induced as well by 16-membered macrolides as by lincosamides. The observed dissociation rate constant of VS-ribosome complexes was identified with the kappa-vs in the case of 16-membered macrolides, but linearly related to lincomycin concentration, suggesting a direct binding of the latter antibiotic to VS-ribosome complexes and the triggering of a conformational change of particles entailing VS release. Two different mechanisms were also involved in the VM-promoted reassociation to ribosomes of VS previously displaced by either macrolides or lincosamides. By binding to lincosamide-ribosome complexes, VM induced a conformational change of ribosomes resulting in higher affinity for VS and lower affinity for lincosamides. On the contrary, an incompatibility for a simultaneous binding of VM and 16-membered macrolides to ribosomes was observed. These results have been interpreted by postulating specific (nonoverlapping) and aspecific (overlapping) antibiotic binding sites at the peptidyltransferase domain. All the kinetic constants of five antibiotic families (type A and B synergimycins, 14- and 16-membered macrolides, and lincosamides) and a topological model of peptidyltransferase are presently available.

Erythromycin↗
PubMed2000

Lincomycin and clindamycin conformations. A fragment shared by macrolides, ketolides and lincosamides determined from TRNOE ribosome-bound conformations.

Two important lincosamide antibiotics, lincomycin and clindamycin were studied in the complex state with the bacterial ribosome after a conformational analysis by 1H and 13C NMR spectroscopy and molecular modelling of the unbound molecules. Lincosamide-ribosome interactions were investigated using two-dimensional transferred nuclear Overhauser effect spectroscopy (TRNOESY), resulting in a bound structure compatible with the experimental NMR data. The results compared with the conformational analysis of the substrates in solution indicate that specific conformations are preferred in the bound state. Clindamycin, the more bioactive antibiotic studied, displayed a stronger NMR response than lincomycin showing that in lincosamide-ribosome interactions, a low affinity binding level is associated to the tight binding one and is related to biological activity. This study shows that conformation plays an essential role for the low affinity binding site. Superimposition of lincosamide, macrolide and ketolide bound structures exhibited conformational similarities in a particular fragment which is in agreement with a hypothesis of partial overlapping lincosamide and macrolide binding sites.

Anti-Bacterial Agents↗
PubMed2006

A new evolutionary variant of the streptogramin A resistance protein, Vga(A)LC, from Staphylococcus haemolyticus with shifted substrate specificity towards lincosamides.

We found a new variant of the streptogramin A resistance gene, vga(A)LC, in clinical isolates of Staphylococcus haemolyticus resistant to lincomycin and clindamycin but susceptible to erythromycin and in which no relevant lincosamide resistance gene was detected. The gene vga(A)LC, differing from the gene vga(A) at the protein level by seven amino acid substitutions, was present exclusively in S. haemolyticus strains resistant to both lincosamides and streptogramin A (LS(A) phenotype). Antibiotic resistance profiles of the ATP-binding cassette (ABC) proteins Vga(A)(LC) and Vga(A) in the antibiotic-susceptible host S. aureus RN4220 were compared. It was shown that Vga(A)LC conferred resistance to both lincosamides and streptogramin A, while Vga(A) conferred significant resistance to streptogramin A only. Detailed analysis of the seven amino acid substitutions, distinguishing the two related ABC proteins with different substrate specificities, identified the substrate-recognizing site: four clustered substitutions (L212S, G219V, A220T, and G226S) in the spacer between the two ATP-binding cassettes altered the substrate specificity and constituted the lincosamide-streptogramin A resistance phenotype. A transport experiment with radiolabeled lincomycin demonstrated that the mechanism of lincosamide resistance in S. haemolyticus was identical to that of the reported macrolide-streptogramin B resistance conferred by Msr(A).

Amino Acid Sequence↗
PubMed1981

Macrolide-lincosamide-streptogramin resistance patterns in Clostridium perfringens from animals.

Different patterns of resistance against commonly used macrolide, lincosamide, and streptogramin antibiotics were found in Clostridium perfringens of animal origin. The patterns were designated as (i) macrolide-lincosamide-streptogramin group B generalized resistance, (ii) macrolide-lincosamide generalized resistance, (iii) macrolide-lincosamide inducible resistance, and (iv) macrolide-lincosamide-streptogramin low-level generalized resistance. The strains of the fourth pattern were able to inactivate pristinamycin and virginiamycin. The macrolide-susceptible strains showed a bimodal distribution of lincomycin and clindamycin susceptibility levels. The susceptible strains were inhibited by 0.25 micrograms of lincomycin per ml and 0.03 micrograms of clindamycin per ml. The low-level resistant strains were inhibited at concentrations of 2 to 4 micrograms of lincomycin per ml and 0.5 to 2 micrograms of clindamycin per ml.

Animals↗
PubMed1986

[Lincosamides].

The two main antibiotics that make up the group of lincosamides are lincomycin and its more recent derivative clindamycin; the latter, more active drug is gaining preference over the former. These antibiotics are active primarily against Gram positive cocci (i.e. staphylococci, pneumococci and group A and unclassifiable streptococci) and against most anaerobes (including Bacteroides fragilis). This action originates in binding to the 50S ribosomal fraction. Lincosamides may be given per os, intramuscularly or intravenously. After an oral dose of clindamycin, 90% of the drug is absorbed, and the peak serum level is reached within the first hour. Drug absorption is not modified by meals. Regardless of the route of administration, the serum half life of clindamycin is 2 to 3.8 hours in healthy individuals. Longer half lives are observed in patients with severe renal or hepatic failure, requiring that lower dosages be given by widening the intervals between doses. Diffusion of lincosamides into tissues is of clinical significance except for the central nervous system, especially the cerebrospinal fluid. On the whole, lincosamides are well tolerated. Pseudomembranous colitis is a potential hazard. The main indications of clindamycin are infections due to anaerobes, especially intestinal and vaginal infections. As clindamycin has virtually no effect against Gram negative aerobic pathogens, in most instances another antibiotic, usually an aminoglycoside, is given simultaneously. Other less common indications are some instances of aspiration pneumonia, septicemias due to B. fragilis, and actinomycoses. Because of the risk of pseudomembranous colitis, prophylactic use of clindamycin to prevent postoperative infections following colorectal surgery seems unadvisable.

Adult↗
PubMed2006

Cloacal Lactobacillus isolates from broilers show high prevalence of resistance towards macrolide and lincosamide antibiotics.

Eighty-seven Lactobacillus strains isolated from cloacal swabs of broiler chickens derived from 20 different farms in Belgium were identified to species level and tested for susceptibility to macrolide and lincosamide antibiotics. Five different Lactobacillus species were identified as being predominantly present in the cloacae of broilers: Lactobacillus crispatus, Lactobacillus salivarius subsp. salivarius, Lactobacillus amylovorus, Lactobacillus gallinarum and Lactobacillu sreuteri. Acquired resistance prevalence to macrolides and lincosamides was very high in the investigated lactobacilli: 89% of the strains were resistant to either or both lincosamide and macrolide class antibiotics. The vast majority of these resistant strains (96%) displayed constitutive resistance. More than one-half of the macrolide and/or lincosamide resistant strains carried an erm(B), erm(C), mef(A), lnu(A) gene or a combination of these genes.

Animals↗
PubMed1981

A family of r-determinants in Streptomyces spp. that specifies inducible resistance to macrolide, lincosamide, and streptogramin type B antibiotics.

Inducible resistance to macrolide, lincosamide, and streptogramin type B antibiotics in Streptomyces spp. comprises a family of diverse phenotypes in which characteristic subsets of the macrolide-lincosamide-streptogramin antibiotics induce resistance mediated by mono- or dimethylation of adenine, or both, in 23S ribosomal ribonucleic acid. In these studies, diverse patterns of induction specificity in Streptomyces and associated ribosomal ribonucleic acid changes are described. In Streptomyces fradiae NRRL 2702 erythromycin induced resistance to vernamycin B, whereas in Streptomyces hygroscopicus IFO 12995, the reverse was found: vernamycin B induced resistance to erythromycin. In a Streptomyces viridochromogenes (NRRL 2860) model system studied in detail, tylosin induced resistance to erythromycin associated with N6-monomethylation of 23S ribosomal ribonucleic acid, whereas in Staphylococcus aureus, erythromycin induced resistance to tylosin mediated by N6-dimethylation of adenine. Inducible macrolide-lincosamide-streptogramin resistance was found in S. fradiae NRRL 2702 and S. hygroscopicus IFO 12995, which synthesize the macrolides tylosin and maridomycin, respectively, as well as in the lincosamide producer Streptomyces lincolnensis NRRL 2936 and the streptogramin type B producer Streptomyces diastaticus NRRL 2560. A wide range of different macrolides including chalcomycin, tylosin, and cirramycin induced resistance when tested in an appropriate system. Lincomycin was active as inducer in S. lincolnensis, the organism by which it is produced, and streptogramin type B antibiotics induced resistance in S. fradiae, S. hygroscopicus, and the streptogramin type B producer S. diastaticus. Patterns of adenine methylation found included (i) lincomycin-induced monomethylation in S. lincolnensis (and constitutive monomethylation in a mutant selected with maridomycin), (ii) concurrent equimolar levels of adenine mono- plus dimethylation in S. hygroscopicus, (iii) monomethylation in S. fradiae (and dimethylation in a mutant selected with erythromycin), and (iv) adenine dimethylation in S. diastaticus induced by ostreogrycin B.

Anti-Bacterial Agents↗
PubMed1988

Epidemiology of macrolide and lincosamide resistance in species of staphylococci in a general hospital.

During a 1-year period resistance to macrolides and lincosamides among staphylococci in a general hospital was studied. The macrolide-lincosamide resistance phenotype was found in 36.7% of coagulase-negative and in 3.7% of coagulase-positive species. Isolates showing this phenotype were more abundant from indwelling artificial devices, blood, respiratory tract and sterile fluids. The surgery and intensive care units of the hospital provided the highest proportion of such strains. Methicillin resistance was present in 13.9% of the staphylococci but no relationship between methicillin and macrolide-lincosamide resistance was observed.

Aminoglycosides↗
PubMed2001

Prevalence and mechanism of resistance against macrolides and lincosamides in Streptococcus suis isolates.

Eighty-seven Streptococcus suis isolates recovered in 1999-2000 from diseased pigs, all from different farms, were screened for resistance against macrolide and lincosamide antibiotics by the disk diffusion and agar dilution test and a PCR assay, amplifying the ermB gene and the mefA/E gene. Seventy-one percent of the isolates showed constitutive resistance to macrolide and lincosamide antibiotics (MLS(B)-phenotype). All these isolates were positive for the ermB gene in the PCR, but negative for the mefA/E gene. For all strains minimum inhibitory concentrations (MIC) against five other antimicrobial agents were determined. All strains were susceptible to penicillin. Ninety-nine percent of the isolates were susceptible to enrofloxacin and tiamulin. Eighty-five percent of the strains were resistant to doxycycline. A 540bp fragment of the ermB genes of eight S. suis strains was sequenced and compared with ermB genes of five S. pneumoniae and five S. pyogenes strains of human origin. A 100% homology was found between these fragments in seven S. suis, one S. pneumoniae and three of the S. pyogenes isolates. This study demonstrates that resistance against macrolides, lincosamides and streptogramin B is widespread in S. suis and mediated by ribosome methylation, encoded by the ermB gene.

Animals↗
PubMed2003

Macrolide and lincosamide resistance in the gram-positive nasal and tonsillar flora of pigs.

Macrolide and lincosamide resistance phenotypes and the presence of the erm(A), erm(B), erm(C), and mef(A) genes were determined in 344 bacterial strains belonging to 34 species and nine genera, isolated from the tonsils and nasal cavities of 2-week- and 6-week-old piglets, derived from four different farms. These piglets had never before been treated with macrolides or lincosamides. Macrolide and lincosamide resistance was most frequently present in Streptococcus and Enterococcus strains, of which over two-thirds were resistant. These genera were followed in decreasing order of resistance frequency by Lactobacillus, Rothia, Staphylococcus, Arcanobacterium, Actinomyces, Pediococcus strains. Only five infrequently occurring species did not show resistance. This high frequency of resistance in nontreated piglets indicates that resistant strains circulate in the herds. In streptococci, enterococci, and Lactobacillus strains, resistance was most often encoded by the erm(B) gene and in staphylococci by erm(A) or erm(C). The erm(B) gene was sporadically detected in other bacterial genera (Actinomyces, Rothia, Aerococcus, Pediococcus). The sequence of the erm(B) gene of 29 strains of 11 pigs originating from the four different farms was determined. This sequence was identical in 12 strains and only differed by 1-6 nucleotides in the other strains, indicating that exchanges of resistance genes might occur between bacterial species and genera belonging to the nasal or tonsillar flora of piglets.

Animals↗
PubMed2004

Antimicrobial resistance in Brachyspira pilosicoli with special reference to point mutations in the 23S rRNA gene associated with macrolide and lincosamide resistance.

A point mutation in the 23S rRNA gene causes macrolide and lincosamide resistance in Brachyspira hyodysenteriae. The possible occurrence of a similar mutation in Brachyspira pilosicoli was studied and the MICs of six antimicrobial agents for Swedish field isolates of B. pilosicoli were determined. Of 10 isolates with high MICs of macrolide and lincosamide antibiotics, six had a mutation in nucleotide position 2058 or 2059 in the 23S rRNA gene as compared to the wild type of Escherichia coli, whereas none of 10 tylosin-susceptible isolates were mutated in this region. The mutations found in position 2058 were A --> T transversions, and in position 2059 either A --> G transitions or A --> C transversions. The MICs at which 90% of the B. pilosicoli field isolates were inhibited by tylosin, erythromycin, clindamycin, virginiamycin, tiamulin, and carbadox, were >256, >256, >4, 4, 2, and 0.125 microg/ml, respectively. In conclusion, point mutations in positions 2058 and 2059 of the 23S rRNA gene can cause macrolide and lincosamide resistance in B. pilosicoli. Macrolide resistance is widespread among Swedish field isolates of B. pilosicoli. Notably also a few isolates with elevated MICs of tiamulin were found.

Animals↗
PubMed2005

Characterization of In Vivo acquired resistance of Mycoplasma hyopneumoniae to macrolides and lincosamides.

Macrolides and related antibiotics are used to control mycoplasma infections in the pig industry worldwide. Some porcine mycoplasmas, however, survive these treatments by acquiring resistance. The mechanism of acquired resistance to macrolides and lincosamides was studied in more detail for Mycoplasma hyopneumoniae by comparing both the phenotype and genotype of a resistant field isolate to five susceptible isolates. The MICs were significantly higher for the resistant strain for all antibiotics tested. The MICs for the 16-membered macrolide tylosin ranged from 8 to 16 microg for the resistant strain and from 0.03 to 0.125 microg/ml for the five susceptible strains. The MICs for the 15-membered macrolides and lincosamides were higher than 64 microg/ml for the resistant strain while only 0.06 to 0.5 microg/ml for the susceptible strains. Mycoplasma hyopneumoniae strains are intrinsically resistant to the 14-membered macrolides due to a G 2057 A transition (E. coli numbering) in their 23S rDNA. Therefore, high MICs were observed for all strains, although the MICs for the resistant strain were clearly increased. An additional, acquired A 2058 G point mutation was found in the 23S rRNA gene of the resistant strain. No differences linked to resistance were found in the ribosomal proteins L4 and L22. The present study showed that 23S rRNA mutations resulting in resistance to macrolides and lincosamides as described in other Mycoplasma spp. also occur under field conditions in M. hyopneumoniae.

Drug Resistance, Multiple, Bacterial↗
PubMed2002

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

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%).

Anti-Bacterial Agents↗
PubMed1987

Phenotypic expression and genetic heterogeneity of lincosamide inactivation in Staphylococcus spp.

We examined the resistance phenotype and the genetic basis of lincosamide modification in 25 clinical isolates of Staphylococcus spp. inactivating lincomycin and clindamycin. The strains were resistant to high levels of lincomycin but remained susceptible to clindamycin. However, MBCs and inoculum effects showed that the activity of clindamycin was impaired. The distribution in these strains of nucleotide sequences related to linA and linA', the genes encoding lincosamide nucleotidylation in Staphylococcus haemolyticus BM4610 and S. aureus BM4611, respectively, was studied by dot blot hybridization. The genes responsible for lincosamide inactivation in Staphylococcus spp. were found to constitute a family of related sequences which are not species specific.

Anti-Bacterial Agents↗
PubMed1990

Cloning of a lincosamide resistance determinant from Streptomyces caelestis, the producer of celesticetin, and characterization of the resistance mechanism.

Self-resistance has been investigated in Streptomyces caelestis (producer of the lincosamide antibiotic celesticetin), from which a lincosamide resistance determinant (clr) has been isolated on a 1-kilobase DNA fragment and cloned in Streptomyces lividans. The clr product is a specific methylase which produces a single residue of N6-monomethyladenine in 23S rRNA at position 2058, thereby rendering the 50S ribosmal subunit resistant to the action of lincosamides.

Anti-Bacterial Agents↗