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Article: Cloning and characterisation of malE in Burkholderia pseudomallei

TitleCloning and characterisation of malE in Burkholderia pseudomallei
Authors
Issue Date2001
PublisherSociety for General Microbiology. The Journal's web site is located at http://jmm.sgmjournals.org
Citation
Journal of Medical Microbiology, 2001, v. 50 n. 4, p. 330-338 How to Cite?
AbstractNo recombinant protein is available for serodiagnosis or skin test in the diagnosis of melioidosis. This report describes the cloning of the male gene, which encodes an immunogenic protein of Burkholderia pseudomallei. Bi-directional DNA sequencing of malE revealed that the gene contained a single open reading frame encoding 416 amino acid residues with a predicted molecular mass of 44.4 kDa. BLAST analysis showed that the putative protein encoded by male is homologous to the maltose-binding protein (MBP) of other bacteria. It has 48% and 63% amino acid identity and similarity with the MBP of Brucella abortus, and malE complementation assay showed that it partially complemented the function of the MBP of Escherichia coli. Several highly conserved regions among the MBP of B. pseudomallei, Br. abortus, Salmonella enterica serotype Typhimurium, E. coli and Enterobacter aerogenes were observed. These regions represent signatures A, B, C, D and F identified in the MBP of E. coli. Further sequence analysis revealed that the first 24 amino acid residues of the MBP of B. pseudomallei probably represent the N-terminal signal peptide of the protein. Similar to the signal peptide of the MBP of E. coli, Ent. aerogenes and S. Typhimurium, the MBP of B. pseudomallei contains two basic residues in the first eight amino acids, followed by a hydrophobic core, with the last three amino acids in the signal peptide being Ala-Gln-Ala, conforming to the consensus sequence Ala-X-Ala at positions -3 to -1 relative to the site of proteolytic cleavage for recognition by signal peptidase I. Further studies on serodiagnosis of melioidosis with recombinant MBP should be performed.
Persistent Identifierhttp://hdl.handle.net/10722/157325
ISSN
2015 Impact Factor: 2.269
2015 SCImago Journal Rankings: 1.060
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWoo, PCYen_US
dc.contributor.authorLeung, PKLen_US
dc.contributor.authorTsoi, HWen_US
dc.contributor.authorYuen, KYen_US
dc.date.accessioned2012-08-08T08:48:56Z-
dc.date.available2012-08-08T08:48:56Z-
dc.date.issued2001en_US
dc.identifier.citationJournal of Medical Microbiology, 2001, v. 50 n. 4, p. 330-338en_US
dc.identifier.issn0022-2615en_US
dc.identifier.urihttp://hdl.handle.net/10722/157325-
dc.description.abstractNo recombinant protein is available for serodiagnosis or skin test in the diagnosis of melioidosis. This report describes the cloning of the male gene, which encodes an immunogenic protein of Burkholderia pseudomallei. Bi-directional DNA sequencing of malE revealed that the gene contained a single open reading frame encoding 416 amino acid residues with a predicted molecular mass of 44.4 kDa. BLAST analysis showed that the putative protein encoded by male is homologous to the maltose-binding protein (MBP) of other bacteria. It has 48% and 63% amino acid identity and similarity with the MBP of Brucella abortus, and malE complementation assay showed that it partially complemented the function of the MBP of Escherichia coli. Several highly conserved regions among the MBP of B. pseudomallei, Br. abortus, Salmonella enterica serotype Typhimurium, E. coli and Enterobacter aerogenes were observed. These regions represent signatures A, B, C, D and F identified in the MBP of E. coli. Further sequence analysis revealed that the first 24 amino acid residues of the MBP of B. pseudomallei probably represent the N-terminal signal peptide of the protein. Similar to the signal peptide of the MBP of E. coli, Ent. aerogenes and S. Typhimurium, the MBP of B. pseudomallei contains two basic residues in the first eight amino acids, followed by a hydrophobic core, with the last three amino acids in the signal peptide being Ala-Gln-Ala, conforming to the consensus sequence Ala-X-Ala at positions -3 to -1 relative to the site of proteolytic cleavage for recognition by signal peptidase I. Further studies on serodiagnosis of melioidosis with recombinant MBP should be performed.en_US
dc.languageengen_US
dc.publisherSociety for General Microbiology. The Journal's web site is located at http://jmm.sgmjournals.orgen_US
dc.relation.ispartofJournal of Medical Microbiologyen_US
dc.subject.meshAtp-Binding Cassette Transportersen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAntibodies, Bacterial - Blooden_US
dc.subject.meshAntigens, Bacterial - Immunologyen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshBlotting, Westernen_US
dc.subject.meshBurkholderia Pseudomallei - Genetics - Immunologyen_US
dc.subject.meshCarrier Proteins - Chemistry - Genetics - Immunology - Metabolismen_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshEscherichia Coli Proteinsen_US
dc.subject.meshGenetic Complementation Testen_US
dc.subject.meshGuinea Pigsen_US
dc.subject.meshHumansen_US
dc.subject.meshMaltose-Binding Proteinsen_US
dc.subject.meshMelioidosis - Diagnosis - Microbiologyen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMonosaccharide Transport Proteinsen_US
dc.subject.meshPeriplasmic Binding Proteinsen_US
dc.subject.meshSequence Analysis, Dnaen_US
dc.titleCloning and characterisation of malE in Burkholderia pseudomalleien_US
dc.typeArticleen_US
dc.identifier.emailWoo, PCY: pcywoo@hkucc.hku.hken_US
dc.identifier.emailTsoi, HW: hwtsoi@hkucc.hku.hken_US
dc.identifier.emailYuen, KY: kyyuen@hkucc.hku.hken_US
dc.identifier.authorityWoo, PCY=rp00430en_US
dc.identifier.authorityTsoi, HW=rp00439en_US
dc.identifier.authorityYuen, KY=rp00366en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.pmid11289518-
dc.identifier.scopuseid_2-s2.0-0035079776en_US
dc.identifier.hkuros61979-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0035079776&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume50en_US
dc.identifier.issue4en_US
dc.identifier.spage330en_US
dc.identifier.epage338en_US
dc.identifier.isiWOS:000167651500005-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridWoo, PCY=7201801340en_US
dc.identifier.scopusauthoridLeung, PKL=55085129100en_US
dc.identifier.scopusauthoridTsoi, HW=6603822102en_US
dc.identifier.scopusauthoridYuen, KY=36078079100en_US
dc.customcontrol.immutablesml 130524-

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