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Architecture of a Host-Parasite Interface: Complex Targeting Mechanisms Revealed Through Proteomics.

Gadelha C, Zhang W, Chamberlain JW, Chait BT, Wickstead B, Field MC - Mol. Cell Proteomics (2015)

Bottom Line: 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.Validation shows that the majority of surface proteome constituents are bona fide surface-associated proteins and, as expected, most present at the flagellar pocket.This work provides a paradigm for the compartmentalization of a cell surface and a resource for its analysis.

View Article: PubMed Central - PubMed

Affiliation: From the ‡School of Life Sciences, University of Nottingham, Nottingham, UK, NG2 7UH; §Department of Pathology, University of Cambridge, Cambridge, UK, CB2 1QP; catarina.gadelha@nottingham.ac.uk.

No MeSH data available.


Related in: MedlinePlus

Enrichment analysis showing proteins of unknown function taken for validation by localization. Dataset as in Fig. 2, with points representing 25 ESPs highlighted according to predicted protein architecture.
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Figure 3: Enrichment analysis showing proteins of unknown function taken for validation by localization. Dataset as in Fig. 2, with points representing 25 ESPs highlighted according to predicted protein architecture.

Mentions: Having demonstrated an efficient enrichment of known FP proteins and related annotation in the labeled dataset, we next sought to robustly test our TbBSP by directly interrogating the cellular location of multiple protein hits of unknown localization, and looking for specific signal at the FP. A set of 25 candidates were selected from the high-confidence sets for further characterization using the following criteria: (1) they were annotated as “hypothetical” proteins for which no functional data had been previously reported for T. brucei at the start of this work; (2) they represented the range of general protein topologies detected, e.g. predicted GPI-anchored proteins, type I and type II TM proteins, and multipass TM proteins; and (3) they included proteins with enrichment ranging from 5 to >6000 times and spanning >3 orders of magnitude of mass spectrometry signal intensity. Fig. 3 shows the enrichment and architectures of these candidates, and supplemental Table S3 provides their accession numbers and predicted features.


Architecture of a Host-Parasite Interface: Complex Targeting Mechanisms Revealed Through Proteomics.

Gadelha C, Zhang W, Chamberlain JW, Chait BT, Wickstead B, Field MC - Mol. Cell Proteomics (2015)

Enrichment analysis showing proteins of unknown function taken for validation by localization. Dataset as in Fig. 2, with points representing 25 ESPs highlighted according to predicted protein architecture.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4587319&req=5

Figure 3: Enrichment analysis showing proteins of unknown function taken for validation by localization. Dataset as in Fig. 2, with points representing 25 ESPs highlighted according to predicted protein architecture.
Mentions: Having demonstrated an efficient enrichment of known FP proteins and related annotation in the labeled dataset, we next sought to robustly test our TbBSP by directly interrogating the cellular location of multiple protein hits of unknown localization, and looking for specific signal at the FP. A set of 25 candidates were selected from the high-confidence sets for further characterization using the following criteria: (1) they were annotated as “hypothetical” proteins for which no functional data had been previously reported for T. brucei at the start of this work; (2) they represented the range of general protein topologies detected, e.g. predicted GPI-anchored proteins, type I and type II TM proteins, and multipass TM proteins; and (3) they included proteins with enrichment ranging from 5 to >6000 times and spanning >3 orders of magnitude of mass spectrometry signal intensity. Fig. 3 shows the enrichment and architectures of these candidates, and supplemental Table S3 provides their accession numbers and predicted features.

Bottom Line: 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.Validation shows that the majority of surface proteome constituents are bona fide surface-associated proteins and, as expected, most present at the flagellar pocket.This work provides a paradigm for the compartmentalization of a cell surface and a resource for its analysis.

View Article: PubMed Central - PubMed

Affiliation: From the ‡School of Life Sciences, University of Nottingham, Nottingham, UK, NG2 7UH; §Department of Pathology, University of Cambridge, Cambridge, UK, CB2 1QP; catarina.gadelha@nottingham.ac.uk.

No MeSH data available.


Related in: MedlinePlus