dc.creator | Petinaki, E. | en |
dc.creator | Guérin-Faublée, V. | en |
dc.creator | Pichereau, V. | en |
dc.creator | Villers, C. | en |
dc.creator | Achard, A. | en |
dc.creator | Malbruny, B. | en |
dc.creator | Leclercq, R. | en |
dc.date.accessioned | 2015-11-23T10:45:25Z | |
dc.date.available | 2015-11-23T10:45:25Z | |
dc.date.issued | 2008 | |
dc.identifier | 10.1128/AAC.01126-07 | |
dc.identifier.issn | 664804 | |
dc.identifier.uri | http://hdl.handle.net/11615/32176 | |
dc.description.abstract | Streptococcus uberis UCN 42, isolated from a case of bovine mastitis, was intermediately resistant to lincomycin (MIC = 2 μg/ml) while remaining susceptible to clindamycin (MIC = 0.06 μg/ml) and erythromycin. A 1.1-kb SacI fragment was cloned from S. uberis UCN 42 total DNA on plasmid pUC 18 and introduced into Escherichia coli AG100A, where it conferred resistance to both clindamycin and lincomycin. The sequence analysis of the fragment showed the presence of a new gene, named lnu(D), that encoded a 164-amino-acid protein with 53% identity with Lnu(C) previously reported to occur in Streptococcus agalactiae:Crude lysates of E. coli AG100A containing the cloned lnu(D) gene inactivated lincomycin and clindamycin in the presence of ATP and MgCl 2. Mass spectrometry experiments demonstrated that the lnu(D) enzyme catalyzed adenylylation of clindamycin. A domain conserved in deduced sequences of lincosamide O-nucleotidyltransferases Lnu(A), Lnu(C), LinAN2, and Lin(D) and in the aminoglycoside nucleotidyltransferase ANT(2″) was identified. Copyright © 2008, American Society for Microbiology. All Rights Reserved. | en |
dc.source.uri | http://www.scopus.com/inward/record.url?eid=2-s2.0-38649135737&partnerID=40&md5=380c0cd6eb098d4cded6647d1d81b78a | |
dc.subject | adenosine triphosphate | en |
dc.subject | aminoglycoside nucleotidyltransferase | en |
dc.subject | bacterial protein | en |
dc.subject | clindamycin | en |
dc.subject | erythromycin | en |
dc.subject | gene product | en |
dc.subject | lincomycin | en |
dc.subject | lincosamide o nucleotidyltransferase | en |
dc.subject | magnesium chloride | en |
dc.subject | nucleotidyltransferase | en |
dc.subject | pirlimycin | en |
dc.subject | unclassified drug | en |
dc.subject | adenylation | en |
dc.subject | antibiotic resistance | en |
dc.subject | antibiotic sensitivity | en |
dc.subject | article | en |
dc.subject | bacterial gene | en |
dc.subject | bacterium isolation | en |
dc.subject | catalysis | en |
dc.subject | cattle disease | en |
dc.subject | controlled study | en |
dc.subject | Escherichia coli | en |
dc.subject | gene sequence | en |
dc.subject | genetic code | en |
dc.subject | inu gene | en |
dc.subject | lina gene | en |
dc.subject | linan2 gene | en |
dc.subject | lind gene | en |
dc.subject | mass spectrometry | en |
dc.subject | minimum inhibitory concentration | en |
dc.subject | molecular cloning | en |
dc.subject | nonhuman | en |
dc.subject | nucleotide sequence | en |
dc.subject | plasmid | en |
dc.subject | priority journal | en |
dc.subject | protein domain | en |
dc.subject | sequence analysis | en |
dc.subject | Streptococcus agalactiae | en |
dc.subject | Streptococcus uberis | en |
dc.subject | Amino Acid Sequence | en |
dc.subject | Animals | en |
dc.subject | Anti-Bacterial Agents | en |
dc.subject | Bacterial Proteins | en |
dc.subject | Cattle | en |
dc.subject | Drug Resistance, Bacterial | en |
dc.subject | Female | en |
dc.subject | Mastitis, Bovine | en |
dc.subject | Microbial Sensitivity Tests | en |
dc.subject | Molecular Sequence Data | en |
dc.subject | Nucleotidyltransferases | en |
dc.subject | Sequence Analysis, DNA | en |
dc.subject | Streptococcus | en |
dc.title | Lincomycin resistance gene lnu(D) in Streptococcus uberis | en |
dc.type | journalArticle | en |