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Identification of a PH domain-containing protein which is localized to crystalloid bodies of Plasmodium ookinetes.

Rachaneeporn JenwithisukNiwat KangwanrangsanMayumi TachibanaAmporn ThongkukiatkulHitoshi OtsukiJetsumon SattabongkotTakafumi TsuboiMotomi ToriiTomoko Ishino
Published in: Malaria journal (2018)
CryPH, containing a signal peptide and PH domain, is predominantly expressed in zygotes and ookinetes and is localized to crystalloid bodies in P. yoelii. CryPH accumulates in vesicle-like structures prior to the appearance of typical crystalloid bodies. Unlike other known crystalloid body localized proteins, CryPH does not appear to have a multiple domain architecture characteristic of the LAP/CCp family proteins. Although CryPH is highly conserved among Plasmodium, Babesia, Theileria, and Cryptosporidium, PyCryPH is dispensable for the development of invasive ookinetes and sporozoites in mosquito bodies.
Keyphrases
  • plasmodium falciparum
  • high resolution
  • binding protein
  • protein protein
  • amino acid
  • dengue virus