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Research Article

The secreted salivary proteome of the pea aphid Acyrthosiphon pisum characterised by mass spectrometry

  1. James C. Carolan Dr.1,*,
  2. Carol I. J. Fitzroy1,
  3. Peter D. Ashton2,
  4. Angela E. Douglas2,3,
  5. Thomas L. Wilkinson1

Article first published online: 28 APR 2009

DOI: 10.1002/pmic.200800692

Issue

PROTEOMICS

PROTEOMICS

Volume 9, Issue 9, pages 2457–2467, No. 9 May 2009

Additional Information

How to Cite

Carolan, J. C., Fitzroy, C. I. J., Ashton, P. D., Douglas, A. E. and Wilkinson, T. L. (2009), The secreted salivary proteome of the pea aphid Acyrthosiphon pisum characterised by mass spectrometry. Proteomics, 9: 2457–2467. doi: 10.1002/pmic.200800692

Author Information

  1. 1

    UCD School of Biology and Environmental Science, University College Dublin, Dublin, Ireland

  2. 2

    Department of Biology, University of York, York, UK

  3. 3

    Present address: Department of Entomology, Comstock Hall, Cornell University, Ithaca, NY14850, USA

*UCD School of Biology and Environmental Science, University College Dublin, Belfield, Dublin 4, Ireland Fax: +353-1-716-1152

Publication History

  1. Issue published online: 28 APR 2009
  2. Article first published online: 28 APR 2009
  3. Manuscript Received: 31 AUG 2008

Funded by

  • Science Foundation Ireland. Grant Numbers: 03/IN3/B381, BB/C520898

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Keywords:

  • Acyrthosiphon pisum;
  • Aphid;
  • LC-MS/MS;
  • Phloem sap;
  • Saliva

Abstract

Nine proteins secreted in the saliva of the pea aphid Acyrthosiphon pisum were identified by a proteomics approach using GE-LC-MS/MS and LC-MS/MS, with reference to EST and genomic sequence data for A. pisum. Four proteins were identified by their sequences: a homolog of angiotensin-converting enzyme (an M2 metalloprotease), an M1 zinc-dependant metalloprotease, a glucose-methanol-choline (GMC)-oxidoreductase and a homolog to regucalcin (also known as senescence marker protein 30). The other five proteins are not homologous to any previously described sequence and included an abundant salivary protein (represented by ACYPI009881), with a predicted length of 1161 amino acids and high serine, tyrosine and cysteine content. A. pisum feeds on plant phloem sap and the metalloproteases and regucalcin (a putative calcium-binding protein) are predicted determinants of sustained feeding, by inactivation of plant protein defences and inhibition of calcium-mediated occlusion of phloem sieve elements, respectively. The amino acid composition of ACYPI009881 suggests a role in the aphid salivary sheath that protects the aphid mouthparts from plant defences, and the oxidoreductase may promote gelling of the sheath protein or mediate oxidative detoxification of plant allelochemicals. Further salivary proteins are expected to be identified as more sensitive MS technologies are developed.

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