Publication: Salivary proteins of aphids identified by mass spectrometry

May 5th, 2009

Carolan JC, Fitzroy CF, Ashton PD, Douglas AE and Wilkinson TL, 2009. The proteome of the pea aphid saliva characterized by LC/MS-MS. Proteomics 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 metalloprotease,
* a glucose-methanol-choline (GMC)-oxidoreductase
* a homolog to regucalcin (also known as senescence marker protein 30).

One of the five proteins without homologous to any previously described sequence (ACYPI009881) has the amino acid composition (high serine, tyrosine and cysteine content) predicted of the salivary sheath protein that protects the aphid mouthparts from plant defences. The oxidoreductase may promote gelling of the sheath protein or mediate oxidative detoxification of plant allelochemicals.