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Article: Polyclonal antibodies to glutathione S-transferase-verotoxin subunit A fusion proteins neutralize verotoxins

TitlePolyclonal antibodies to glutathione S-transferase-verotoxin subunit A fusion proteins neutralize verotoxins
Authors
Issue Date2002
PublisherAmerican Society for Microbiology.
Citation
Clinical And Diagnostic Laboratory Immunology, 2002, v. 9 n. 3, p. 687-692 How to Cite?
AbstractThe A1 subunits of verotoxin-1 (VT1) and VT2 genes were cloned into pGEX-4T-2 for the expression of glutathione S-transferase (GST) fusion proteins. The N-terminal and the transmembrane regions of the A1 subunits were excluded from the constructs in order to increase the product yields. Polyclonal anti-VT1A1 and anti-VT2A1 antibodies were produced by immunizing rabbits with GST-VT1A1 and GST-VT2A1 fusion proteins, respectively. The antibodies were tested for their ability to neutralize active toxins from 45 VT-producing Escherichia coli (VTEC) strains. The antibodies had significantly high neutralizing activities against their homologous toxins. The average percentages of neutralization of VT1 by anti-GST-VT1A1 and anti-GST-VT2A1 were 76.7% ∓ 7.9% and 3.6% ± 2.3%, respectively, and those of VT2 were 1.7% ± 2.3% and 82.5% ± 13.9%, respectively. VT2 variant toxin was neutralized by anti-GST-VT2A1, with cross neutralization being a possible consequence of sequence homology between VT2 and a VT2 variant. To our knowledge, this is the first report on the production of polyclonal antibodies from GST-VT fusion proteins. The antibodies were shown to exhibit specific toxin neutralizing activities and may be useful for immunological diagnosis of VTEC infections.
Persistent Identifierhttp://hdl.handle.net/10722/49217
ISSN
2007 Impact Factor: 2.511
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLeung, PHMen_HK
dc.contributor.authorPeiris, JSMen_HK
dc.contributor.authorNg, WWSen_HK
dc.contributor.authorYam, WCen_HK
dc.date.accessioned2008-06-12T06:36:56Z-
dc.date.available2008-06-12T06:36:56Z-
dc.date.issued2002en_HK
dc.identifier.citationClinical And Diagnostic Laboratory Immunology, 2002, v. 9 n. 3, p. 687-692en_HK
dc.identifier.issn1071-412Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/49217-
dc.description.abstractThe A1 subunits of verotoxin-1 (VT1) and VT2 genes were cloned into pGEX-4T-2 for the expression of glutathione S-transferase (GST) fusion proteins. The N-terminal and the transmembrane regions of the A1 subunits were excluded from the constructs in order to increase the product yields. Polyclonal anti-VT1A1 and anti-VT2A1 antibodies were produced by immunizing rabbits with GST-VT1A1 and GST-VT2A1 fusion proteins, respectively. The antibodies were tested for their ability to neutralize active toxins from 45 VT-producing Escherichia coli (VTEC) strains. The antibodies had significantly high neutralizing activities against their homologous toxins. The average percentages of neutralization of VT1 by anti-GST-VT1A1 and anti-GST-VT2A1 were 76.7% ∓ 7.9% and 3.6% ± 2.3%, respectively, and those of VT2 were 1.7% ± 2.3% and 82.5% ± 13.9%, respectively. VT2 variant toxin was neutralized by anti-GST-VT2A1, with cross neutralization being a possible consequence of sequence homology between VT2 and a VT2 variant. To our knowledge, this is the first report on the production of polyclonal antibodies from GST-VT fusion proteins. The antibodies were shown to exhibit specific toxin neutralizing activities and may be useful for immunological diagnosis of VTEC infections.en_HK
dc.format.extent386 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherAmerican Society for Microbiology.en_HK
dc.relation.ispartofClinical and Diagnostic Laboratory Immunologyen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.rightsClinical and Diagnostic Laboratory Immunology. Copyright © American Society for Microbiology.en_HK
dc.rightsCopyright © American Society for Microbiology, Clinical and Diagnostic Laboratory Immunology, 2002, v. 9 n. 3, p. 687-692en_HK
dc.subject.meshAntibodies, Bacterial - biosynthesis - genetics - immunologyen_HK
dc.subject.meshAntigens, Bacterial - genetics - immunology - isolation & purificationen_HK
dc.subject.meshShiga Toxin 1 - genetics - immunology - isolation & purificationen_HK
dc.subject.meshShiga Toxin 2 - genetics - immunology - isolation & purificationen_HK
dc.subject.meshCloning, Molecularen_HK
dc.titlePolyclonal antibodies to glutathione S-transferase-verotoxin subunit A fusion proteins neutralize verotoxinsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1071-412X&volume=9&issue=3&spage=687&epage=692&date=2002&atitle=Polyclonal+antibodies+to+glutathione+S-transferase--verotoxin+subunit+a+fusion+proteins+neutralize+verotoxinsen_HK
dc.identifier.emailPeiris, JSM: malik@hkucc.hku.hken_HK
dc.identifier.emailYam, WC: wcyam@hkucc.hku.hken_HK
dc.identifier.authorityPeiris, JSM=rp00410en_HK
dc.identifier.authorityYam, WC=rp00313en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.doi10.1128/CDLI.9.3.687-692.2002en_HK
dc.identifier.pmid11986278-
dc.identifier.pmcidPMC120006en_HK
dc.identifier.scopuseid_2-s2.0-0036116414en_HK
dc.identifier.hkuros72911-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0036116414&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume9en_HK
dc.identifier.issue3en_HK
dc.identifier.spage687en_HK
dc.identifier.epage692en_HK
dc.identifier.isiWOS:000175713100027-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLeung, PHM=7401747852en_HK
dc.identifier.scopusauthoridPeiris, JSM=7005486823en_HK
dc.identifier.scopusauthoridNg, WWS=36787042600en_HK
dc.identifier.scopusauthoridYam, WC=7004281720en_HK

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