Peer-Reviewed Journal Details
Mandatory Fields
Carolan J.;Fitzroy C.;Ashton P.;Douglas A.;Wilkinsonl T.
2009
May
Proteomics
The secreted salivary proteome of the pea aphid Acyrthosiphon pisum characterised by mass spectrometry
Published
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Optional Fields
Acyrthosiphon pisum Aphid LC-MS MS Phloem sap Saliva
9
9
2457
2467
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 metallopro- tease, 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 cys- teine 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 inactiva- tion of plant protein defences and inhibition of calcium-mediated occlusion of phloem sieve elements, respectively. The amino acid composition ofACYPI009881 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 allelo- chemicals. Further salivary proteins are expected to be identified as more sensitive MS technologies are developed. © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
1615-9853
10.1002/pmic.200800692
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