PXD002180

PXD002180 is an original dataset announced via ProteomeXchange.

Title	Architecture of a host-parasite interface: complex targeting mechanisms revealed through proteomics
Description	Surface membrane organization and composition is key to cellular function, and membrane proteins serve many essential roles in endocytosis, secretion and cell recognition. The surface of parasitic organisms, however, is a double-edged sword; this is the primary interface between parasites and their hosts, and those crucial cellular processes must be carried out while avoiding elimination by the host immune defenses. For extracellular African trypanosomes, the surface is partitioned such that all endo- and exocytosis is directed through a specific membrane region, the flagellar pocket, in which it is thought the majority of invariant surface proteins reside. However, very few of these proteins have been identified, severely limiting functional studies, and hampering the development of potential treatments. Here we used an integrated biochemical, proteomic and bioinformatic strategy to identify surface components of the human parasite Trypanosoma brucei. This surface proteome contains previously known flagellar pocket proteins as well as multiple novel components, and is significantly enriched in proteins that are essential for parasite survival. Molecules with receptor-like properties are almost exclusively parasite-specific, whereas transporter-like proteins are conserved in model organisms. Validation shows that the majority of surface proteome constituents are bona fide surface-associated proteins, and as expected, the majority present at the flagellar pocket. Moreover, the largest systematic analysis of trypanosome surface molecules to date provides evidence that the cell surface is compartmentalized into three distinct domains with free diffusion of molecules in each, but selective, asymmetric traffic between. This work provides a paradigm for the compartmentalization of a cell surface and a resource for its analysis.
HostingRepository	PRIDE
AnnounceDate	2015-06-15
AnnouncementXML	Submission_2015-06-15_02:33:48.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Catarina Gadelha
SpeciesList	scientific name: Trypanosoma brucei; NCBI TaxID: 5691;
ModificationList	deamidated residue; monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	LTQ Orbitrap Velos

Revision	Datetime	Status	ChangeLog Entry
0	2015-05-13 01:38:00	ID requested
⏵ 1	2015-06-15 02:33:50	announced

Gadelha C, Zhang W, Chamberlain JW, Chait BT, Wickstead B, Field MC, Architecture of a Host-Parasite Interface: Complex Targeting Mechanisms Revealed Through Proteomics. Mol Cell Proteomics, 14(7):1911-26(2015) [pubmed]

curator keyword: Biological

submitter keyword: Trypanosoma brucei, surfeome, cell surface proteome, plasma membrane, VSG, ESAG

Catarina Gadelha
contact affiliation	School of Life Sciences, University of Nottingham, UK
contact email	catarina.gadelha@nottingham.ac.uk
lab head
Catarina Gadelha
contact affiliation	University of Nottingham
contact email	catarina.gadelha@nottingham.ac.uk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD002180
     1. Label: PRIDE project
     2. Name: Architecture of a host-parasite interface: complex targeting mechanisms revealed through proteomics