• Login
    View Item 
    •   Home
    • The Manchester Institute Cancer Research UK
    • All Paterson Institute for Cancer Research
    • View Item
    •   Home
    • The Manchester Institute Cancer Research UK
    • All Paterson Institute for Cancer Research
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of ChristieCommunitiesTitleAuthorsIssue DateSubmit DateSubjectsThis CollectionTitleAuthorsIssue DateSubmit DateSubjects

    My Account

    LoginRegister

    Local Links

    The Christie WebsiteChristie Library and Knowledge Service

    Statistics

    Display statistics

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

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Authors
    Stacey, Simon N
    Eklund, C
    Jordan, Deborah
    Smith, Nigel K
    Stern, Peter L
    Dillner, J
    Arrand, John R
    Affiliation
    Cancer Research Campaign Department of Molecular Biology, Paterson Institute for Cancer Research, Christie Hospital, Manchester, UK.
    Issue Date
    1994-02
    
    Metadata
    Show full item record
    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.
    Citation
    Scanning the structure and antigenicity of HPV-16 E6 and E7 oncoproteins using antipeptide antibodies. 1994, 9 (2):635-45 Oncogene
    Journal
    Oncogene
    URI
    http://hdl.handle.net/10541/96107
    PubMed ID
    7507231
    Type
    Article
    Language
    en
    ISSN
    0950-9232
    Collections
    All Paterson Institute for Cancer Research

    entitlement

    Related articles

    • Identification of B-epitopes in the human papillomavirus 18 E7 open reading frame protein.
    • Authors: Selvey LA, Tindle RW, Geysen HM, Haller CJ, Smith JA, Frazer IH
    • Issue date: 1990 Nov 1
    • Suppression of tumorigenesis by transcription units expressing the antisense E6 and E7 messenger RNA (mRNA) for the transforming proteins of the human papilloma virus and the sense mRNA for the retinoblastoma gene in cervical carcinoma cells.
    • Authors: Hu G, Liu W, Hanania EG, Fu S, Wang T, Deisseroth AB
    • Issue date: 1995 Mar
    • [Modification of HPV type 16 E6 and E7 genes, and analysis of stability and immunogenicity of the modified proteins].
    • Authors: Zhi H, Han L, Ren J, Tian H, Luo W, Liang Y, Ruan L
    • Issue date: 2002 Jun
    • In vitro antigene therapy targeting HPV-16 E6 and E7 in cervical carcinoma.
    • Authors: Madrigal M, Janicek MF, Sevin BU, Perras J, Estape R, Peñalver M, Averette HE
    • Issue date: 1997 Jan
    • Immunological responses in human papillomavirus 16 E6/E7-transgenic mice to E7 protein correlate with the presence of skin disease.
    • Authors: Frazer IH, Leippe DM, Dunn LA, Liem A, Tindle RW, Fernando GJ, Phelps WC, Lambert PF
    • Issue date: 1995 Jun 15
    DSpace software (copyright © 2002 - 2023)  DuraSpace
    Quick Guide | Contact Us
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.