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Article: The E1 sequence of bovine adenovirus type 3 and complementation of human adenovirus type 5 E1A function in bovine cells

TitleThe E1 sequence of bovine adenovirus type 3 and complementation of human adenovirus type 5 E1A function in bovine cells
Authors
Issue Date1994
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/virusres
Citation
Virus Research, 1994, v. 31 n. 2, p. 163-186 How to Cite?
AbstractThe bovine adenovirus type 3 (BAV3) genome was sequenced from the left end to the HindIII site at 11%. This region comprises the entire E1 transcription unit including the open reading frames (ORF) for proteins homologous to the E1A, E1B proteins and protein IX of human adenovirus type 5 (Ad5). A portion of the BAV3 E1A protein showed significant homology with conserved region 3 (CR3), the principal transactivation region of Ad5 E1A. The BAV3 E1A protein also contains a consensus sequence known to be important for interaction with the cellular Rb protein but lacks most of the sequence corresponding to the second exon of Ad5 E1A. Promoter sequences for BAV3 E1B were not defined though the relevant region contains a 35-base pair repeat sequence. Two ORFs define the BAV3 E1B coding unit; one with regions homologous to sequences within the Ad5 E1B 19k protein, and an overlapping ORF with significant homology to the Ad5 E1B 55k protein. The encoded BAV3 E1B proteins of 157 and 420 amino acid residues (R) have predicted unmodified molecular weights of 17,393 and 46,734 respectively. Immediately following the E1B coding region there is a transcription unit containing an SP1 binding site and TATA box followed by an ORF which encodes a protein of 125R and predicted molecular weight of 13,706 with homology to protein IX of Ad5. Five concensus poly A addition sites are located in the 350 base pairs immediately following the protein IX coding region. The homology of sequences in the Ad5 E1A CR3 region and the corresponding BAV3 protein suggested that the BAV3 protein could transactivate certain Ad5 genes normally transactivated by the Ad5 E1A product. Evidence for this hypothesis was obtained in studies in which bovine cells in culture were coinfected with BAV3 and a human adenovirus type 5 (Ad5) recombinant viral vector lacking the E1A region and having a lacZ reporter gene within the E3 region dependent on E1A for its expression. Coinfection resulted in the induction of β-galactosidase activity and the increased expression of other Ad5 early (E2A 72k) and late (hexon) proteins.
Persistent Identifierhttp://hdl.handle.net/10722/157265
ISSN
2015 Impact Factor: 2.526
2015 SCImago Journal Rankings: 1.259
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorZheng, Ben_US
dc.contributor.authorMittal, SKen_US
dc.contributor.authorGraham, FLen_US
dc.contributor.authorPrevec, Len_US
dc.date.accessioned2012-08-08T08:48:31Z-
dc.date.available2012-08-08T08:48:31Z-
dc.date.issued1994en_US
dc.identifier.citationVirus Research, 1994, v. 31 n. 2, p. 163-186en_US
dc.identifier.issn0168-1702en_US
dc.identifier.urihttp://hdl.handle.net/10722/157265-
dc.description.abstractThe bovine adenovirus type 3 (BAV3) genome was sequenced from the left end to the HindIII site at 11%. This region comprises the entire E1 transcription unit including the open reading frames (ORF) for proteins homologous to the E1A, E1B proteins and protein IX of human adenovirus type 5 (Ad5). A portion of the BAV3 E1A protein showed significant homology with conserved region 3 (CR3), the principal transactivation region of Ad5 E1A. The BAV3 E1A protein also contains a consensus sequence known to be important for interaction with the cellular Rb protein but lacks most of the sequence corresponding to the second exon of Ad5 E1A. Promoter sequences for BAV3 E1B were not defined though the relevant region contains a 35-base pair repeat sequence. Two ORFs define the BAV3 E1B coding unit; one with regions homologous to sequences within the Ad5 E1B 19k protein, and an overlapping ORF with significant homology to the Ad5 E1B 55k protein. The encoded BAV3 E1B proteins of 157 and 420 amino acid residues (R) have predicted unmodified molecular weights of 17,393 and 46,734 respectively. Immediately following the E1B coding region there is a transcription unit containing an SP1 binding site and TATA box followed by an ORF which encodes a protein of 125R and predicted molecular weight of 13,706 with homology to protein IX of Ad5. Five concensus poly A addition sites are located in the 350 base pairs immediately following the protein IX coding region. The homology of sequences in the Ad5 E1A CR3 region and the corresponding BAV3 protein suggested that the BAV3 protein could transactivate certain Ad5 genes normally transactivated by the Ad5 E1A product. Evidence for this hypothesis was obtained in studies in which bovine cells in culture were coinfected with BAV3 and a human adenovirus type 5 (Ad5) recombinant viral vector lacking the E1A region and having a lacZ reporter gene within the E3 region dependent on E1A for its expression. Coinfection resulted in the induction of β-galactosidase activity and the increased expression of other Ad5 early (E2A 72k) and late (hexon) proteins.en_US
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/virusresen_US
dc.relation.ispartofVirus Researchen_US
dc.subject.meshAdenoviridae - Chemistry - Geneticsen_US
dc.subject.meshAdenovirus E1 Proteins - Chemistry - Geneticsen_US
dc.subject.meshAdenoviruses, Human - Chemistry - Geneticsen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshCattleen_US
dc.subject.meshDna, Viral - Geneticsen_US
dc.subject.meshGenetic Complementation Testen_US
dc.subject.meshHumansen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshOpen Reading Framesen_US
dc.subject.meshSequence Homology, Amino Aciden_US
dc.subject.meshTata Boxen_US
dc.titleThe E1 sequence of bovine adenovirus type 3 and complementation of human adenovirus type 5 E1A function in bovine cellsen_US
dc.typeArticleen_US
dc.identifier.emailZheng, B:bzheng@hkucc.hku.hken_US
dc.identifier.authorityZheng, B=rp00353en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/0168-1702(94)90002-7en_US
dc.identifier.pmid8178572-
dc.identifier.scopuseid_2-s2.0-0028107367en_US
dc.identifier.volume31en_US
dc.identifier.issue2en_US
dc.identifier.spage163en_US
dc.identifier.epage186en_US
dc.identifier.isiWOS:A1994MV70900002-
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridZheng, B=7201780588en_US
dc.identifier.scopusauthoridMittal, SK=7201413085en_US
dc.identifier.scopusauthoridGraham, FL=35821642700en_US
dc.identifier.scopusauthoridPrevec, L=7003455531en_US

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