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


    Carolan, James C. and Fitzroy, Carol I.J. and Ashton, Peter D. and Douglas, Angela E. and Wilkinson, Thomas L. (2009) The secreted salivary proteome of the pea aphid Acyrthosiphon pisum characterised by mass spectrometry. Proteomics, 9 (9). pp. 2457-2467. ISSN 1615-9853

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    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.

    Item Type: Article
    Additional Information: The definitive version of this article is available at 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
    Keywords: Acyrthosiphon pisum; Aphid; LC-MS/MS; Phloem sap; Saliva;
    Academic Unit: Faculty of Science and Engineering > Biology
    Item ID: 7173
    Identification Number: https://doi.org/10.1002/pmic.200800692
    Depositing User: James Carolan
    Date Deposited: 07 Jul 2016 11:41
    Journal or Publication Title: Proteomics
    Publisher: Wiley
    Refereed: Yes
    Funders: Science Foundation Ireland (SFI)
    URI:

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