Details:

Alternative Title:
PLoS One
Publisher's site:
http://dx.doi.org/10.1371/journal.pone.0182561
Personal Author:
Anderson, D. C. ; Lapp, Stacey A. ; Barnwell, John W. ; Galinski, Mary R.
Anderson, D. C. ; Lapp, Stacey A. ; Barnwell, John W. ; Galinski, Mary R. Less -
Description:
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.
Subject:
[+]
Animals Plasmodium Vivax Proteome Protozoan Proteins Trophozoites
Source:
PLoS One. 12(8).
Pubmed ID:
28829774
Pubmed Central ID:
PMC5567661
Document Type:
Journal Article
Funding:
P40 OD010938/OD/NIH HHS/United States ; P51 OD011132/OD/NIH HHS/United States ; R01 AI024710/AI/NIAID NIH HHS/United States ; HHSN272201200031C/AI/NIAID NIH HHS/United States ; P51 RR000165/RR/NCRR NIH HHS/United States
P40 OD010938/OD/NIH HHS/United States ; P51 OD011132/OD/NIH HHS/United States ; R01 AI024710/AI/NIAID NIH HHS/United States ; HHSN272201200031C/AI/NIAID NIH HHS/United States ; P51 RR000165/RR/NCRR NIH HHS/United States Less -
Collection(s):
CDC Public Access
Main Document Checksum:
[+]
urn:sha256:062f737978b7745c793ee954b50b168f9e3601e959fac10109911b3450536bc7
Download URL:
https://stacks.cdc.gov/view/cdc/48091/cdc_48091_DS1.pdf
File Type:

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