ANTIMICROBIAL RESISTANCE - MOLECULAR ANALYSIS OF THE MACROLIDE-LINCOSAMIDE RESISTANCE GENE REGION OF A NOVEL PLASMID FROM STAPHYLOCOCCUS-HYICUS

Citation
S. Schwarz et al., ANTIMICROBIAL RESISTANCE - MOLECULAR ANALYSIS OF THE MACROLIDE-LINCOSAMIDE RESISTANCE GENE REGION OF A NOVEL PLASMID FROM STAPHYLOCOCCUS-HYICUS, Journal of Medical Microbiology, 47(1), 1998, pp. 63-70
Citations number
41
Categorie Soggetti
Microbiology
ISSN journal
00222615
Volume
47
Issue
1
Year of publication
1998
Pages
63 - 70
Database
ISI
SICI code
0022-2615(1998)47:1<63:AR-MAO>2.0.ZU;2-I
Abstract
Resistance to macrolides and lincosamides in Staphylococcus hyicus has been shown to be encoded by a 4.0-kb plasmid designated pSES21. It di ffered distinctly in its restriction map from all other staphylococcal macrolide resistance plasmids reported so far. Southern blot hybridis ation with gene probes specific for staphylococcal erm genes demonstra ted that the macrolide resistance gene belonged to hybridisation class C. Analysis of the ermC gene revealed that the deduced amino-acid seq uence of the pSES21-encoded ErmC methylase exhibited c. 93% identity w ith the ErmC methylase encoded by plasmid pE194. The ermC gene of pSES 21 was expressed constitutively and sequence analysis of the regulator y region showed multiple base-pair insertions and substitutions in the translational attenuator. As a consequence of these mutations, the re ading frame of the small regulatory peptide was destroyed and a novel pair of inverted repeated sequences was generated. Previous studies id entified sequence deletions and sequence duplications in the ermC regu latory region as the basis for constitutive ermC gene expression. The multiple point mutations shown in the pSES21-encoded ermC translationa l attenuator represent a novel kind of structural alteration in this r egulatory region and may explain constitutive ermC gene expression by pairing of the newly generated inverted repeated segments in the prese nce of a functionally deleted reading frame for the small regulatory p eptide.