Prevalence of phenotypic resistance of Staphylococcus aureus isolates to macrolide, lincosamide, streptogramin B, ketolid and linezolid antibiotics in Turkey

Adaleti, Rıza; Nakipoğlu, Yaşar; Ceran, Nurgül; Tasdemir, Cihan; Kaya, Fatma Nur; Taşdemir, Semiha

doi:10.1016/s1413-8670(10)70003-9

Cited by 19 publications

(14 citation statements)

References 17 publications

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“…These findings were different from the results obtained in a study conducted amongS. aureus isolates in Turkey, whereby the cMLS B phenotype was the predominant resistance phenotype (63%) [27]. Otherwise, we reported a similar distribution of MLS resistance phenotypes to that described in the UK by Hamilton-Miller et al [28].…”

Section: Discussioncontrasting

confidence: 99%

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Characterization of resistance genes to macrolides, lincosamides and streptogramins (MLS) among clinical isolates of Staphylococcus aureus in North Lebanon

Osman

Nasbeh²,

Rafei³

et al. 2015

int. arab. j antimicrob. agents

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Objective: Staphylococcus aureus is one of the most significant pathogens causing significant morbidity and mortality. Moreover, the incidence of MLS S. aureus (resistant at least for one macrolide) infections continues to grow globally. The aim of this study is to examine the expression of resistance of S. aureus isolates to MLS and the prevalence of genes involved in this resistance using PCR. Methods:A total 38 strains of S. aureus MLS-resistant were isolated in the Microbiology Labs at Nini Hospital in North Lebanon. The disk diffusion method was used to determine the phenotype of the MLS resistance. The resistance genes involved were detected by PCR using specific gene primers for ermA, ermB, ermC, msrA, linA, mefA, vat and vgb genes.Results: A total of 55.3% of the isolates were positive for inducible phenotype (iMLS B ), of these 15.8% were positive for the constitutive phenotype (cMLS B ), 23.7% for MS B phenotype and 5.2% for L phenotype. The ermC gene was the most prevalent (52.6%), while ermA, ermB, msrA and linA genes were observed with lower prevalence. A combination of several of these genes was detected,whereas the vgb, vat and mefA genes were not detected in any of the clinical isolates. Conclusion:This study is the first investigated characterization of MLS resistance genes in clinical isolates of S. aureus in Lebanon according to

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Section: Discussioncontrasting

confidence: 99%

“…Otherwise, we reported a similar distribution of MLS resistance phenotypes to that described in the UK by Hamilton-Miller et al [28]. However, various studies conducted in Turkey [27], Europe [29], Japan …”

Section: Discussionsupporting

confidence: 89%

Characterization of resistance genes to macrolides, lincosamides and streptogramins (MLS) among clinical isolates of Staphylococcus aureus in North Lebanon

Osman

Nasbeh²,

Rafei³

et al. 2015

int. arab. j antimicrob. agents

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“…kangalına da bağlanarak, eritromisine dirençli gram-pozitif mikroorganizmalar da dahil olmak üzere pek çok patojene karşı daha etki gösterir 9,10 . Ancak son yıllarda yapılan çeşitli çalışmalarda, eritromisine dirençli stafilokok izolatlarında, telitromisin direnci bildirilmeye başlanmıştır 4,11 . MLS B direncinin sıklığı ülkeden ülkeye hatta aynı ülkede merkezler, hasta grupları ve bakteri türleri arasında değişiklik göstermektedir.…”

Section: Introductionunclassified

Macrolide-Lincosamide-Streptogramin B (MLSB) Resistance Phenotypes in Clinical Staphylococcus Isolates and Investigation of Telithromycin Activity

Uzun¹,

Güngör²,

Pektaş³

et al. 2014

Mikrobiyol Bul

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“…1) is currently used as a synergetic pair against Gram-positive resistant strain, such as methicillin-resistant Staphylococcus aureus (MSRA) and vancomycin-resistant Enterococcus faecium (VREF) (3,4). Since its clinical approval by the US Food and Drug Administration (FDA) in 1999, this drug combination suffers some resistance by MSRA (5,6). The synergistic effect of the streptogramins is driven by the streptogramin A (i.e., Dalfopristin) member, which upon binding to the 50S subunit significantly increases the K a of the streptogramin B (i.e., Quinupristin) component (7).…”

mentioning

confidence: 99%

Crystal structure of the synergistic antibiotic pair, lankamycin and lankacidin, in complex with the large ribosomal subunit

Belousoff

Shapira

Bashan

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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The structures of the large ribosomal subunit of Deinococcus radiodurans (D50S) in complex with the antibiotic lankamycin (3.2 Å) and a double antibiotic complex of lankamycin and lankacidin C (3.45 Å) have been determined, in continuation of previous crystallographic studies on lankacidin-D50S complex. These two drugs have been previously reported to inhibit ribosomal function with mild synergistic effect. Lankamycin, a member of the macrolide family, binds in a similar manner to erythromycin. However, when in complex with lankacidin, lankamycin is located so that it can form interactions with lankacidin in the adjacent ribosomal binding site. When compared to the well-documented synergistic antibiotics, Streptogramins A and B, the pair of lankacidin and lankamycin bind in similar sites, the peptidyl transferase center and nascent peptide exit tunnel, respectively. Herein, we discuss the structural basis for antibiotic synergism and highlight the key factors involved in ribosomal inhibition.protein exit tunnel | ribosomes

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Prevalence of phenotypic resistance of Staphylococcus aureus isolates to macrolide, lincosamide, streptogramin B, ketolid and linezolid antibiotics in Turkey

Cited by 19 publications

References 17 publications

Characterization of resistance genes to macrolides, lincosamides and streptogramins (MLS) among clinical isolates of Staphylococcus aureus in North Lebanon

Characterization of resistance genes to macrolides, lincosamides and streptogramins (MLS) among clinical isolates of Staphylococcus aureus in North Lebanon

Macrolide-Lincosamide-Streptogramin B (MLSB) Resistance Phenotypes in Clinical Staphylococcus Isolates and Investigation of Telithromycin Activity

Crystal structure of the synergistic antibiotic pair, lankamycin and lankacidin, in complex with the large ribosomal subunit

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