Scanning the structure and antigenicity of HPV-16 E6 and E7 oncoproteins using antipeptide antibodies.

2.50
Hdl Handle:
http://hdl.handle.net/10541/96107
Title:
Scanning the structure and antigenicity of HPV-16 E6 and E7 oncoproteins using antipeptide antibodies.
Authors:
Stacey, Simon N; Eklund, C; Jordan, Deborah; Smith, Nigel K; Stern, Peter L; Dillner, J; Arrand, John R
Abstract:
The 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.
Affiliation:
Cancer Research Campaign Department of Molecular Biology, Paterson Institute for Cancer Research, Christie Hospital, Manchester, UK.
Citation:
Scanning the structure and antigenicity of HPV-16 E6 and E7 oncoproteins using antipeptide antibodies. 1994, 9 (2):635-45 Oncogene
Journal:
Oncogene
Issue Date:
Feb-1994
URI:
http://hdl.handle.net/10541/96107
PubMed ID:
7507231
Type:
Article
Language:
en
ISSN:
0950-9232
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorStacey, Simon Nen
dc.contributor.authorEklund, Cen
dc.contributor.authorJordan, Deborahen
dc.contributor.authorSmith, Nigel Ken
dc.contributor.authorStern, Peter Len
dc.contributor.authorDillner, Jen
dc.contributor.authorArrand, John Ren
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.en
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

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