University Library
  • Login
A gateway to Melbourne's research publications
Minerva Access is the University's Institutional Repository. It aims to collect, preserve, and showcase the intellectual output of staff and students of the University of Melbourne for a global audience.
View Item 
  • Minerva Access
  • Veterinary and Agricultural Sciences
  • Melbourne Veterinary School
  • Veterinary Biosciences
  • Veterinary Biosciences - Research Publications
  • View Item
  • Minerva Access
  • Veterinary and Agricultural Sciences
  • Melbourne Veterinary School
  • Veterinary Biosciences
  • Veterinary Biosciences - Research Publications
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

    Cloning and characterization of a novel sigma-like glutathione S-transferase from the giant panda parasitic nematode, Baylisascaris schroederi

    Thumbnail
    Download
    Published version (2.050Mb)

    Citations
    Scopus
    Altmetric
    17
    Author
    Xie, Y; Zhou, X; Chen, L; Zhang, Z; Wang, C; Gu, X; Wang, T; Peng, X; Yang, G
    Date
    2015-01-23
    Source Title
    Parasites and Vectors
    Publisher
    BMC
    University of Melbourne Author/s
    Wang, Tao
    Affiliation
    Veterinary Biosciences
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Xie, Y., Zhou, X., Chen, L., Zhang, Z., Wang, C., Gu, X., Wang, T., Peng, X. & Yang, G. (2015). Cloning and characterization of a novel sigma-like glutathione S-transferase from the giant panda parasitic nematode, Baylisascaris schroederi. PARASITES & VECTORS, 8 (1), https://doi.org/10.1186/s13071-014-0629-9.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/260356
    DOI
    10.1186/s13071-014-0629-9
    Abstract
    BACKGROUND: Baylisascaris schroederi, an intestinal nematode of the giant panda, is the cause of the often fatal disease, baylisascariasis. Glutathione S-transferases (GSTs) are versatile enzymes that can affect parasite survival and parasite-host interactions and, are therefore, potential targets for the development of diagnostic tests and vaccines. METHODS: In this study, we identified a full-length cDNA that encoded a novel, secretory sigma-like GST (Bsc-GSTσ) from a B. schroederi-omic dataset. Following cloning and sequencing, sequence and structural analyses and comparative modeling were performed using online-bioinformatics and proteomics tools. The recombinant Bsc-GSTσ (rBsc-GSTσ) protein was prokaryotically expressed and then used to detect antigenicity and reactivity using immunoblotting assays. In addition, the native protein in female adult B. schroederi was located via immunofluorescence techniques, while the preliminary ELISA-based serodiagnostic potential of rBsc-GSTσ was assessed in native and infected mouse sera. RESULTS: Bsc-GSTσ contained a 621-bp open reading frame that encoded a polypeptide of 206 amino acids with two typical sigma GST domain profiles, including a GST_N_Sigma_like at the N-terminus and a GST_C_Sigma_like at the C-terminus. The presence of an N-terminal signal sequence indicated that Bsc-GSTσ was a secretory protein. Sequence alignment and phylogenetic analyses showed that Bsc-GSTσ was a nematode-specific member of the Sigma class GSTs and shared the closest genetic distance with its homologue in Ascaris suum. Further comparative structure analyses indicated that Bsc-GSTσ possessed the essential structural motifs (e.g., βαβαββα) and the consensus secondary or tertiary structure that is typical for other characterized GSTσs. Immunolocalization revealed strong distributions of native Bsc-GSTσ in the body hypodermis, lateral chords, gut epithelium, gut microvilli, oviduct epithelium, and ovaries of adult female worms, similar to its homologue in A. suum. Building on good immunogenic properties, rBsc-GSTσ-based ELISA exhibited a sensitivity of 79.1% and a specificity of 82.0% to detect anti-B. schroederi IgG antibodies in the sera of experimentally infected mice. CONCLUSION: This study presents a comprehensive demonstration of sequence and structural-based analysis of a new, secretory sigma-like GST from a nematode, and its good serodiagnostic performance suggests that rBsc-GSTσ has the potential to detect B. schroederi and, therefore, could be used to develop an ELISA-based serological test to diagnose baylisascariasis in giant pandas.

    Export Reference in RIS Format     

    Endnote

    • Click on "Export Reference in RIS Format" and choose "open with... Endnote".

    Refworks

    • Click on "Export Reference in RIS Format". Login to Refworks, go to References => Import References


    Collections
    • Minerva Elements Records [52369]
    • Veterinary Biosciences - Research Publications [620]
    Minerva AccessDepositing Your Work (for University of Melbourne Staff and Students)NewsFAQs

    BrowseCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects
    My AccountLoginRegister
    StatisticsMost Popular ItemsStatistics by CountryMost Popular Authors