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pmid:31991085

Cuticular Structure Proteomics in the Pea Aphid Acyrthosiphon pisum Reveals New Plant Virus Receptor Candidates at the Tip of Maxillary Stylets.

Maëlle Deshoux · Victor Masson · Karim Arafah · Sébastien Voisin · Natalia Guschinskaya · Manuella van Munster · Bastien Cayrol · Craig G Webster · Yvan Rahbé · Stéphane Blanc · Philippe Bulet · Marilyne Uzest

Journal of proteome research · 2020 doi:10.1021/acs.jproteome.9b00851

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Experiment

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Data

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Analysis

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Record details sci_version · id · kind · revision · content_hash · schema · created_at · updated_at · generator
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title
Cuticular Structure Proteomics in the Pea Aphid Acyrthosiphon pisum Reveals New Plant Virus Receptor Candidates at the Tip of Maxillary Stylets.
doi
10.1021/acs.jproteome.9b00851
pmid
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[0]
Maëlle Deshoux
[1]
Victor Masson
[2]
Karim Arafah
[3]
Sébastien Voisin
[4]
Natalia Guschinskaya
[5]
Manuella van Munster
[6]
Bastien Cayrol
[7]
Craig G Webster
[8]
Yvan Rahbé
[9]
Stéphane Blanc
[10]
Philippe Bulet
[11]
Marilyne Uzest
journal
Journal of proteome research
year
2020
abstract
Aphids are phloem-feeding insects known as major pests in agriculture that are able to transmit hundreds of plant viruses. The majority of these viruses, classified as noncirculative, are retained and transported on the inner surface of the cuticle of the needle-like mouthparts while the aphids move from plant to plant. Identification of receptors of viruses within insect vectors is a key challenge because they are promising targets for alternative control strategies. The acrostyle, an organ discovered earlier within the common food/salivary canal at the tip of aphid maxillary stylets, displays proteins at the cuticle-fluid interface, some of which are receptors of noncirculative viruses. To assess the presence of stylet- and acrostyle-specific proteins and identify putative receptors, we have developed a comprehensive comparative analysis of the proteomes of four cuticular anatomical structures of the pea aphid, stylets, antennae, legs, and wings. In addition, we performed systematic immunolabeling detection of the cuticular proteins identified by mass spectrometry in dissected stylets. We thereby establish the first proteome of stylets of an insect and determine the minimal repertoire of the cuticular proteins composing the acrostyle. Most importantly, we propose a short list of plant virus receptor candidates, among which RR-1 proteins are remarkably predominant. The data are available via ProteomeXchange (PXD016517).
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Cuticular structure proteomics analyses of the pea aphid Acyrthosiphon pisum
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Summary of Proteins Identified in Acyrthosiphon pisum Cuticular Structures: (A) All Peptides and Proteins Recovered from LC-MS/MS Analyses; (B) Peptides and Proteins Assigned to A. pisum Proteome (A. pisum ID) Recovered from LC-MS/MS Analysis; (C) Cuticular Proteins (CPs) Assigned to A. pisum Recovered from LC-MS/MS Analysisa
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Comparative Analyses of the Proteome of Four Cuticular Structures of the Pea Aphid A. Pisum
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Summary of Proteins Identified in Acyrthosiphon pisum Cuticular Structures: (A) All Peptides and Proteins Recovered from LC-MS/MS Analyses; (B) Peptides and Proteins Assigned to A. pisum Proteome (A. pisum ID) Recovered from LC-MS/MS Analysis; (C) Cuticular Proteins (CPs) Assigned to A. pisum Recovered from LC-MS/MS Analysisa
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[5]
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927
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6924
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1055
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41
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4.5
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10.6
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Distribution of the Identified CPs in the Different Investigated Cuticular Anatomical Structures
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Exhaustive List of Cuticular Proteins Identified in the Four Cuticular Structuresa
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Distribution of the Identified CPs in the Different Investigated Cuticular Anatomical Structures
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Classification of Cuticular Proteins of the Different Structuresa
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Localization of RR-1 Proteins in the Stylets
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Correspondence between Peptides/Proteins Identified in A. pisum Stylets by MS Analysis and Peptides Used for Antibody Productiona
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Cuticular Structure Proteomics in the Pea Aphid Acyrthosiphon pisum Reveals
[1]
1. Experimental workflow to characterize the proteomics composition of the acrostyle and identify pl
[2]
tion of the cuticular proteins identified by mass spectrometry in dissected stylets. We thereby establish t
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esuspended in 2% ACN/0.1% TFA (v/v) prior to mass spectrometry (MS) analysis. Supplementary Material pr9b00
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Complete file
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The majority of these viruses, classified as noncirculative, are retained and transported on the inner surface of the cuticle of the needle-like mouthparts while the aphids move from plant to plant. Identification of receptors of viruses within insect vectors is a key challenge because they are promising targets for alternative control strategies. The acrostyle, an organ discovered earlier within the common food/salivary canal at the tip of aphid maxillary stylets, displays proteins at the cuticle-fluid interface, some of which are receptors of noncirculative viruses. To assess the presence of stylet- and acrostyle-specific proteins and identify putative receptors, we have developed a comprehensive comparative analysis of the proteomes of four cuticular anatomical structures of the pea aphid, stylets, antennae, legs, and wings. In addition, we performed systematic immunolabeling detection of the cuticular proteins identified by mass spectrometry in dissected stylets. We thereby establish the first proteome of stylets of an insect and determine the minimal repertoire of the cuticular proteins composing the acrostyle. Most importantly, we propose a short list of plant virus receptor candidates, among which RR-1 proteins are remarkably predominant. 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"table": {"label": "Table 2", "caption": "Exhaustive List of Cuticular Proteins Identified in the Four Cuticular Structuresa", "rows": [], "row_count": 0, "column_count": 0, "numeric_cells": 0, "header_rows": 0, "locator": "section[18]/table-wrap[1]#tbl2"}}, {"id": "asset:table:pmid:31991085:3", "role": "table", "format": "jats-table", "media_type": "application/vnd.jats.table+json", "uri": null, "sha256": "sha256:dc43ec6dc7bcb3b8c071d2c8e4001cc359fd3cdc7310529215686701e787e7df", "bytes": 535, "access": "open", "state": "verified", "reader": "read_table", "reader_status": "available", "identifier": "section[18]/table-wrap[2]#tbl3", "version": null, "note": "Classification of Cuticular Proteins of the Different Structuresa", "structure": {"pmcid": "PMC7063574", "section_index": 18, "section_title": "Distribution of the Identified CPs in the Different Investigated Cuticular Anatomical Structures", "row_count": 6, "column_count": 7}, "table": {"label": "Table 3", "caption": "Classification of Cuticular Proteins of the Different Structuresa", "rows": [["", "CPAP1", "CPAP3", "CPR_RR1b", "CPR_RR-2b", "TWDLb", "Totalb"], ["Antennae", "1", "6", "(8)-10", "(22)-59", "2", "(39)-78"], ["Legs", "2", "5", "(6)-7", "(22)-61", "(1)-2", "(36)-77"], ["Wings", "2", "6", "(8)-9", "(24)-58", "(1)-2", "(41)-77"], ["Stylets", "0", "3", "(4)-5", "(8)-30", "0", "(15)-38"], ["Whole genome", "11", "8", "15", "110", "3", "147"]], "row_count": 6, "column_count": 7, "numeric_cells": 31, "header_rows": 1, "locator": "section[18]/table-wrap[2]#tbl3"}}, {"id": "asset:table:pmid:31991085:4", "role": "table", "format": "jats-table", "media_type": "application/vnd.jats.table+json", "uri": null, "sha256": "sha256:19e19439353de1ff041f1429669c47d5fc818861126b22ab790d67598d8030fc", "bytes": 279, "access": "open", "state": "verified", "reader": "read_table", "reader_status": "available", "identifier": "section[19]/table-wrap[1]#tbl4", "version": null, "note": "Correspondence between 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