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dc.creatorPetinaki, E.en
dc.creatorGuérin-Faublée, V.en
dc.creatorPichereau, V.en
dc.creatorVillers, C.en
dc.creatorAchard, A.en
dc.creatorMalbruny, B.en
dc.creatorLeclercq, R.en
dc.date.accessioned2015-11-23T10:45:25Z
dc.date.available2015-11-23T10:45:25Z
dc.date.issued2008
dc.identifier10.1128/AAC.01126-07
dc.identifier.issn664804
dc.identifier.urihttp://hdl.handle.net/11615/32176
dc.description.abstractStreptococcus 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.urihttp://www.scopus.com/inward/record.url?eid=2-s2.0-38649135737&partnerID=40&md5=380c0cd6eb098d4cded6647d1d81b78a
dc.subjectadenosine triphosphateen
dc.subjectaminoglycoside nucleotidyltransferaseen
dc.subjectbacterial proteinen
dc.subjectclindamycinen
dc.subjecterythromycinen
dc.subjectgene producten
dc.subjectlincomycinen
dc.subjectlincosamide o nucleotidyltransferaseen
dc.subjectmagnesium chlorideen
dc.subjectnucleotidyltransferaseen
dc.subjectpirlimycinen
dc.subjectunclassified drugen
dc.subjectadenylationen
dc.subjectantibiotic resistanceen
dc.subjectantibiotic sensitivityen
dc.subjectarticleen
dc.subjectbacterial geneen
dc.subjectbacterium isolationen
dc.subjectcatalysisen
dc.subjectcattle diseaseen
dc.subjectcontrolled studyen
dc.subjectEscherichia colien
dc.subjectgene sequenceen
dc.subjectgenetic codeen
dc.subjectinu geneen
dc.subjectlina geneen
dc.subjectlinan2 geneen
dc.subjectlind geneen
dc.subjectmass spectrometryen
dc.subjectminimum inhibitory concentrationen
dc.subjectmolecular cloningen
dc.subjectnonhumanen
dc.subjectnucleotide sequenceen
dc.subjectplasmiden
dc.subjectpriority journalen
dc.subjectprotein domainen
dc.subjectsequence analysisen
dc.subjectStreptococcus agalactiaeen
dc.subjectStreptococcus uberisen
dc.subjectAmino Acid Sequenceen
dc.subjectAnimalsen
dc.subjectAnti-Bacterial Agentsen
dc.subjectBacterial Proteinsen
dc.subjectCattleen
dc.subjectDrug Resistance, Bacterialen
dc.subjectFemaleen
dc.subjectMastitis, Bovineen
dc.subjectMicrobial Sensitivity Testsen
dc.subjectMolecular Sequence Dataen
dc.subjectNucleotidyltransferasesen
dc.subjectSequence Analysis, DNAen
dc.subjectStreptococcusen
dc.titleLincomycin resistance gene lnu(D) in Streptococcus uberisen
dc.typejournalArticleen


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