rdf-syntax-grammar
mods:
  schema location: http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
  title info:
    non sort: The
    title: role of Apical Membrane Antigen-1 in erythrocyte invasion by the zoonotic apicomplexan Babesia microti
  name:
    name part: Baradji, Issa.
    role:
      role term: creator
  name:
    name part: Holman, Patricia J.
    role:
      role term: thesis advisor.
  type of resource: text
  genre: bibliography
  origin info:
    place:
      place term: txu
    date issued: 2010
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: electronic
    form: remote
    extent: 1 online resource.
  abstract: Babesia microti is a tickborne hemoprotozoan parasite that causes the disease babesiosis in humans. Babesia microti Apical Membrane Antigen-1 (AMA-1) is a micronemal protein suspected to play a role in erythrocyte invasion. To investigate interaction between AMA-1 and the host cell, the ectodomain region of the B. microti ama-1 gene was cloned into an expression vector, expressed as a histidine-tagged fusion protein, and used to probe red blood cell membrane proteins in far Western blot assays. The B. microti ama-1 ectodomain, which excludes the signal peptide and the transmembrane region of the open reading frame, was amplified from a cloned gene sequence. The AMA-1 ectodomain is a membrane bound polypeptide that extends into the extracellular space and is most likely to interact or initiate interaction with the host red blood cell surface receptor(s). The amplicon was ligated into a protein expression vector to produce a 58.1 kDa recombinant His-tagged fusion protein, which was confirmed by Western blot analysis. The recombinant B. microti AMA-1 fusion protein was enriched on nickel affinity columns and then used to probe mouse, human and horse red blood cell membrane proteins in far Western blot assays. Babesia microti AMA-1 consistently reacted strongly with a protein migrating at 49 kDa. A similar reaction occurred between the B. microti AMA-1 and horse red blood cell membrane proteins, suggesting that similar interacting proteins of this size are shared by red blood cells from the three species. The B. microti AMA-1 may bind to red blood cell membrane sialic-acid groups, as shown for other Babesia spp. This may explain the signal at the 49 kDa position observed between B. microti AMA-1 and red blood cell membrane proteins from three different species. Further studies may determine if the binding epitopes of the red blood cell binding partner at this position vary and contribute to the specificity of each parasite AMA-1 for their respective host cells.
  note: by Issa Baradji.
  note: "Major Subject: Veterinary Microbiology"
  note: Title from author supplied metadata (automated record created 2010-03-12 12:08:51).
  note: Electronic resource.
  note: Doctor of Philosophy Texas A&M University 2008 http://hdl.handle.net/1969.1/ETD-TAMU-2008-08-68
  note: Includes bibliographical references.
  note: Text (Dissertation)
  subject:
    topic: Major veterinary microbiology
  subject:
    topic: Babesia microti
  subject:
    topic: Apical Membrane Antigen-1
  subject:
    topic: AMA-1
  subject:
    topic: erythrocyte
  subject:
    topic: parasite ligand
  subject:
    topic: red blood cell
  subject:
    topic: receptor
  subject:
    topic: protein-protein interaction
  identifier: http://hdl.handle.net/1969.1/ETD-TAMU-2008-08-68
  record info:
    record content source: TXA
    record creation date: 100426
    record change date: 20151201120110.0
    record identifier: in00002595186