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dc.contributor.authorStacey, Simon N
dc.contributor.authorEklund, C
dc.contributor.authorJordan, Deborah
dc.contributor.authorSmith, Nigel K
dc.contributor.authorStern, Peter L
dc.contributor.authorDillner, J
dc.contributor.authorArrand, John R
dc.date.accessioned2010-04-09T10:10:58Z
dc.date.available2010-04-09T10:10:58Z
dc.date.issued1994-02
dc.identifier.citationScanning the structure and antigenicity of HPV-16 E6 and E7 oncoproteins using antipeptide antibodies. 1994, 9 (2):635-45 Oncogeneen
dc.identifier.issn0950-9232
dc.identifier.pmid7507231
dc.identifier.urihttp://hdl.handle.net/10541/96107
dc.description.abstractThe structure and antigenicity of the HPV-16 E6 and E7 oncoproteins was studied using a set of antisera against overlapping synthetic peptides. We report that antigenic, mobile regions of the native proteins, as defined by reactivity with antipeptide antisera, occur at the N-termini of both E6 and E7 proteins, corresponding to regions of known or suspected protein-protein interactions. The putative zinc finger domains were consistently non-reactive, despite computer predictions of relatively high antigenicity, suggesting that the proposed zinc finger regions are held in stable secondary structures that the peptides were not able to mimic. In E6, the linker region between the two zinc fingers was antigenic, indicating that the two zinc finger structures might be able to articulate relative to one another by a flexible linker region. The highly antigenic N-terminal region of HPV-16 E7 was also found to be antigenic in E7 of both HPV-11 and HPV-18, indicating that the E7 proteins of different HPV types have similar antigenic structures. The identification of antigenic regions of the E6 and E7 proteins should be therefore be useful in the design of site-directed antibodies against E6 and E7 for numerous HPV types.
dc.language.isoenen
dc.subjectCancer DNAen
dc.subjectCultured Tumour Cellsen
dc.subjectUterine Cervical Canceren
dc.subject.meshAmino Acid Sequence
dc.subject.meshAntibodies, Viral
dc.subject.meshAntibody Specificity
dc.subject.meshBase Sequence
dc.subject.meshBlotting, Western
dc.subject.meshDNA, Neoplasm
dc.subject.meshEnzyme-Linked Immunosorbent Assay
dc.subject.meshEpitopes
dc.subject.meshFemale
dc.subject.meshHela Cells
dc.subject.meshHumans
dc.subject.meshMolecular Sequence Data
dc.subject.meshOncogene Proteins, Viral
dc.subject.meshPapillomaviridae
dc.subject.meshPeptide Mapping
dc.subject.meshRepressor Proteins
dc.subject.meshTumor Cells, Cultured
dc.subject.meshUterine Cervical Neoplasms
dc.subject.meshZinc Fingers
dc.titleScanning the structure and antigenicity of HPV-16 E6 and E7 oncoproteins using antipeptide antibodies.en
dc.typeArticleen
dc.contributor.departmentCancer Research Campaign Department of Molecular Biology, Paterson Institute for Cancer Research, Christie Hospital, Manchester, UK.en
dc.identifier.journalOncogeneen
html.description.abstractThe structure and antigenicity of the HPV-16 E6 and E7 oncoproteins was studied using a set of antisera against overlapping synthetic peptides. We report that antigenic, mobile regions of the native proteins, as defined by reactivity with antipeptide antisera, occur at the N-termini of both E6 and E7 proteins, corresponding to regions of known or suspected protein-protein interactions. The putative zinc finger domains were consistently non-reactive, despite computer predictions of relatively high antigenicity, suggesting that the proposed zinc finger regions are held in stable secondary structures that the peptides were not able to mimic. In E6, the linker region between the two zinc fingers was antigenic, indicating that the two zinc finger structures might be able to articulate relative to one another by a flexible linker region. The highly antigenic N-terminal region of HPV-16 E7 was also found to be antigenic in E7 of both HPV-11 and HPV-18, indicating that the E7 proteins of different HPV types have similar antigenic structures. The identification of antigenic regions of the E6 and E7 proteins should be therefore be useful in the design of site-directed antibodies against E6 and E7 for numerous HPV types.


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