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Article: β-Lactamases in Shigella flexneri isolates from Hong Kong and Shanghai and a novel OXA-1-like β-lactamase, OXA-30

Titleβ-Lactamases in Shigella flexneri isolates from Hong Kong and Shanghai and a novel OXA-1-like β-lactamase, OXA-30
Authors
Issue Date2000
PublisherAmerican Society for Microbiology.
Citation
Antimicrobial Agents and Chemotherapy, 2000, v. 44 n. 8, p. 2034-2038 How to Cite?
AbstractNinety-one ampicillin-resistant Shigella flexneri strains from Hong Kong and Shanghai were studied for production of β-lactamases. TEM-1-like and OXA-1-like enzymes were identified in 21 and 79% of the strains, respectively, by isoelectric focusing (IEF). No difference in the pattern of β-lactamase production was found between strains from Hong Kong and Shanghai. Four ribotypes were detected. Over 88% of OXA-producing strains had the same ribotype. All TEM-1-like strains harbored a plasmid which hybridized positively with the bla(TEM) probe. Total DNA from OXA-1-like strains failed to hybridize or only hybridized weakly with an OXA probe. The OXA resistance was not transferable. OXA-1-like enzymes exhibited substrate and inhibition profiles similar to that of OXA-1 and were shown to have a pI of 7.3 by further IEF using a narrow-range ampholine gel. The gene encoding the OXA-1- like enzyme from one isolate (CH-07) was cloned, sequenced, and found to differ from bla(OXA-1) at codon 131 (AGA→GGA; Arg to Gly), resulting in the novel designation OXA-30. The predominance of OXA-type enzymes in ampicillin- resistant S. flexneri suggests host preference for specific β-lactamases.
Persistent Identifierhttp://hdl.handle.net/10722/49198
ISSN
2021 Impact Factor: 5.938
2020 SCImago Journal Rankings: 2.070
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSiu, LKen_HK
dc.contributor.authorLo, JYCen_HK
dc.contributor.authorYuen, KYen_HK
dc.contributor.authorChau, PYen_HK
dc.contributor.authorNg, MHen_HK
dc.contributor.authorHo, PLen_HK
dc.date.accessioned2008-06-12T06:36:34Z-
dc.date.available2008-06-12T06:36:34Z-
dc.date.issued2000en_HK
dc.identifier.citationAntimicrobial Agents and Chemotherapy, 2000, v. 44 n. 8, p. 2034-2038en_HK
dc.identifier.issn0066-4804en_HK
dc.identifier.urihttp://hdl.handle.net/10722/49198-
dc.description.abstractNinety-one ampicillin-resistant Shigella flexneri strains from Hong Kong and Shanghai were studied for production of β-lactamases. TEM-1-like and OXA-1-like enzymes were identified in 21 and 79% of the strains, respectively, by isoelectric focusing (IEF). No difference in the pattern of β-lactamase production was found between strains from Hong Kong and Shanghai. Four ribotypes were detected. Over 88% of OXA-producing strains had the same ribotype. All TEM-1-like strains harbored a plasmid which hybridized positively with the bla(TEM) probe. Total DNA from OXA-1-like strains failed to hybridize or only hybridized weakly with an OXA probe. The OXA resistance was not transferable. OXA-1-like enzymes exhibited substrate and inhibition profiles similar to that of OXA-1 and were shown to have a pI of 7.3 by further IEF using a narrow-range ampholine gel. The gene encoding the OXA-1- like enzyme from one isolate (CH-07) was cloned, sequenced, and found to differ from bla(OXA-1) at codon 131 (AGA→GGA; Arg to Gly), resulting in the novel designation OXA-30. The predominance of OXA-type enzymes in ampicillin- resistant S. flexneri suggests host preference for specific β-lactamases.en_HK
dc.format.extent384 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherAmerican Society for Microbiology.en_HK
dc.relation.ispartofAntimicrobial Agents and Chemotherapyen_HK
dc.subject.meshShigella flexneri - drug effects - enzymology - genetics - isolation & purificationen_HK
dc.subject.meshbeta-Lactamases - chemistry - genetics - metabolismen_HK
dc.subject.meshAnti-Bacterial Agents - pharmacologyen_HK
dc.subject.meshBlotting, Southernen_HK
dc.subject.meshCloning, Molecularen_HK
dc.titleβ-Lactamases in Shigella flexneri isolates from Hong Kong and Shanghai and a novel OXA-1-like β-lactamase, OXA-30en_HK
dc.typeArticleen_HK
dc.identifier.emailYuen, KY:kyyuen@hkucc.hku.hken_HK
dc.identifier.emailHo, PL:plho@hkucc.hku.hken_HK
dc.identifier.authorityYuen, KY=rp00366en_HK
dc.identifier.authorityHo, PL=rp00406en_HK
dc.description.naturelink_to_OA_fulltexten_HK
dc.identifier.doi10.1128/AAC.44.8.2034-2038.2000en_HK
dc.identifier.pmid10898672-
dc.identifier.pmcidPMC90010en_HK
dc.identifier.scopuseid_2-s2.0-0033929536en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0033929536&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume44en_HK
dc.identifier.issue8en_HK
dc.identifier.spage2034en_HK
dc.identifier.epage2038en_HK
dc.identifier.isiWOS:000088308200005-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridSiu, LK=7006651154en_HK
dc.identifier.scopusauthoridLo, JYC=7201650939en_HK
dc.identifier.scopusauthoridYuen, KY=36078079100en_HK
dc.identifier.scopusauthoridChau, PY=36509704300en_HK
dc.identifier.scopusauthoridNg, MH=7202076421en_HK
dc.identifier.scopusauthoridHo, PL=7402211363en_HK
dc.identifier.issnl0066-4804-

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