Your browser doesn't support javascript.
loading
A large scale Plasmodium vivax- Saimiri boliviensis trophozoite-schizont transition proteome.
Anderson, D C; Lapp, Stacey A; Barnwell, John W; Galinski, Mary R.
Affiliation
  • Anderson DC; Bioscience Division, SRI International, Harrisonburg, VA, United States of America.
  • Lapp SA; Emory Vaccine Center, Yerkes National Primate Research Center, Emory University, Atlanta, GA, United States of America.
  • Barnwell JW; Malaria Branch, Division of Parasitic Diseases, Centers for Disease Control and Prevention, Atlanta, GA, United States of America.
  • Galinski MR; Emory Vaccine Center, Yerkes National Primate Research Center, Emory University, Atlanta, GA, United States of America.
PLoS One ; 12(8): e0182561, 2017.
Article de En | MEDLINE | ID: mdl-28829774
Plasmodium vivax is a complex protozoan parasite with over 6,500 genes and stage-specific differential expression. Much of the unique biology of this pathogen remains unknown, including how it modifies and restructures the host reticulocyte. Using a recently published P. vivax reference genome, we report the proteome from two biological replicates of infected Saimiri boliviensis host reticulocytes undergoing transition from the late trophozoite to early schizont stages. Using five database search engines, we identified a total of 2000 P. vivax and 3487 S. boliviensis proteins, making this the most comprehensive P. vivax proteome to date. PlasmoDB GO-term enrichment analysis of proteins identified at least twice by a search engine highlighted core metabolic processes and molecular functions such as glycolysis, translation and protein folding, cell components such as ribosomes, proteasomes and the Golgi apparatus, and a number of vesicle and trafficking related clusters. Database for Annotation, Visualization and Integrated Discovery (DAVID) v6.8 enriched functional annotation clusters of S. boliviensis proteins highlighted vesicle and trafficking-related clusters, elements of the cytoskeleton, oxidative processes and response to oxidative stress, macromolecular complexes such as the proteasome and ribosome, metabolism, translation, and cell death. Host and parasite proteins potentially involved in cell adhesion were also identified. Over 25% of the P. vivax proteins have no functional annotation; this group includes 45 VIR members of the large PIR family. A number of host and pathogen proteins contained highly oxidized or nitrated residues, extending prior trophozoite-enriched stage observations from S. boliviensis infections, and supporting the possibility of oxidative stress in relation to the disease. This proteome significantly expands the size and complexity of the known P. vivax and Saimiri host iRBC proteomes, and provides in-depth data that will be valuable for ongoing research on this parasite's biology and pathogenesis.
Sujet(s)

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Plasmodium vivax / Protéines de protozoaire / Protéome / Trophozoïtes Limites: Animals Langue: En Journal: PLoS One Sujet du journal: CIENCIA / MEDICINA Année: 2017 Type de document: Article Pays d'affiliation: États-Unis d'Amérique Pays de publication: États-Unis d'Amérique

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Plasmodium vivax / Protéines de protozoaire / Protéome / Trophozoïtes Limites: Animals Langue: En Journal: PLoS One Sujet du journal: CIENCIA / MEDICINA Année: 2017 Type de document: Article Pays d'affiliation: États-Unis d'Amérique Pays de publication: États-Unis d'Amérique