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A large scale Plasmodium vivax- Saimiri boliviensis trophozoite-schizont transition proteome. | LitMetric

A large scale Plasmodium vivax- Saimiri boliviensis trophozoite-schizont transition proteome.

PLoS One

Emory Vaccine Center, Yerkes National Primate Research Center, Emory University, Atlanta, GA, United States of America.

Published: October 2017

AI Article Synopsis

  • Plasmodium vivax is a complex protozoan parasite with a large genome and unique biology, particularly in how it interacts with the host's reticulocytes during its life cycle.
  • Researchers utilized a new reference genome to analyze the proteome of infected Saimiri boliviensis reticulocytes, identifying around 5,487 proteins, making this the most extensive study of P. vivax proteins to date.
  • The study highlighted key metabolic functions and cellular structures, found numerous proteins without known function, and indicated a potential link between oxidative stress and the disease, offering valuable data for future research.

Article Abstract

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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5567661PMC
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0182561PLOS

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