Curtin University Homepage
  • Library
  • Help
    • Admin

    espace - Curtin’s institutional repository

    JavaScript is disabled for your browser. Some features of this site may not work without it.
    View Item 
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item
    • espace Home
    • espace
    • Curtin Research Publications
    • View Item

    Antibody Recognition of Cancer-Related Gangliosides and Their Mimics Investigated Using in silico Site Mapping

    215730_76536_journal.pone.0035457.pdf (741.7Kb)
    Access Status
    Open access
    Authors
    Agostino, Mark
    Yuriev, E.
    Ramsland, Paul
    Date
    2012
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Agostino, M. and Yuriev, E. and Ramsland, P. 2012. Antibody Recognition of Cancer-Related Gangliosides and Their Mimics Investigated Using in silico Site Mapping. PLoS ONE. 7 (4): Article ID e35457.
    Source Title
    PLoS ONE
    DOI
    10.1371/journal.pone.0035457
    ISSN
    19326203
    Remarks

    This open access article is distributed under the Creative Commons license http://creativecommons.org/licenses/by/3.0/

    URI
    http://hdl.handle.net/20.500.11937/39513
    Collection
    • Curtin Research Publications
    Abstract

    Modified gangliosides may be overexpressed in certain types of cancer, thus, they are considered a valuable target in cancer immunotherapy. Structural knowledge of their interaction with antibodies is currently limited, due to the large size and high flexibility of these ligands. In this study, we apply our previously developed site mapping technique to investigate the recognition of cancer-related gangliosides by anti-ganglioside antibodies. The results reveal a potential ganglioside-binding motif in the four antibodies studied, suggesting the possibility of structural convergence in the anti-ganglioside immune response. The structural basis of the recognition of ganglioside-mimetic peptides is also investigated using site mapping and compared to ganglioside recognition. The peptides are shown to act as structural mimics of gangliosides by interacting with many of the same binding site residues as the cognate carbohydrate epitopes. These studies provide important clues as to the structural basis of immunological mimicry of carbohydrates.

    Related items

    Showing items related by title, author, creator and subject.

    • Molecular docking of carbohydrate ligands to antibodies: Structural validation against crystal structures
      Agostillo, M.; Jene, C.; Boyle, T.; Ramsland, Paul; Yuriev, E. (2009)
      Cell surface glycoproteins play vital roles in cellular homeostasis and disease. Antibody recognition of glycosylation on different cells and pathogens is critically important for immune surveillance. Conversely, adverse ...
    • Peptide inhibitors of xenoreactive antibodies mimic the interaction profile of the native carbohydrate antigens
      Agostino, Mark; Sandrin, M.; Thompson, P.; Ramsland, P.; Yuriev, E. (2011)
      Carbohydrate–antibody interactions mediate many cellular processes and immune responses. Carbohydrates expressed on the surface of cells serve as recognition elements for particular cell types, for example, in the ABO(H) ...
    • In silico analysis of antibody-carbohydrate interactions and its application to xenoreactive antibodies
      Agostino, Mark; Sandrin, M.; Thompson, P.; Yuriev, E.; Ramsland, Paul (2009)
      Antibody-carbohydrate interactions play central roles in stimulating adverse immune reactions. The most familiar example of such a process is the reaction observed in ABO-incompatible blood transfusion and organ ...
    Advanced search

    Browse

    Communities & CollectionsIssue DateAuthorTitleSubjectDocument TypeThis CollectionIssue DateAuthorTitleSubjectDocument Type

    My Account

    Admin

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

    Follow Curtin

    • 
    • 
    • 
    • 
    • 

    CRICOS Provider Code: 00301JABN: 99 143 842 569TEQSA: PRV12158

    Copyright | Disclaimer | Privacy statement | Accessibility

    Curtin would like to pay respect to the Aboriginal and Torres Strait Islander members of our community by acknowledging the traditional owners of the land on which the Perth campus is located, the Whadjuk people of the Nyungar Nation; and on our Kalgoorlie campus, the Wongutha people of the North-Eastern Goldfields.