A reinvestigation provides no evidence for sugar residues on structural proteins of poleroviruses and argues against a role for glycosylation of virus structural proteins in aphid transmission.

Date publication

juillet 2010

Auteurs

Membres identifiés du Cancéropôle Est :
Dr VAN DORSSELAER Alain

Tous les auteurs :
Revollon S, Strub JM, Fitchette AC, Wiss L, Gomord V, Van Dorsselaer A, Brault V

Lien Pubmed

https://www.ncbi.nlm.nih.gov/pubmed/20416918

Résumé

Poleroviruses are strictly transmitted by aphids. Glycosylation of Turnip yellows virus (TuYV) was previously reported and this modification was supposed to be required for aphid transmission. Using different approaches based on (i) a lectin-binding assay, (ii) use of specific complex glycan antibodies and (iii) mass spectrometry, we found no evidence that the structural proteins of TuYV and Cucurbit aphid-borne yellow virus (CABYV) carry glycan residues. Moreover, mutation of each of the four potential N-glycosylation sites of the structural protein sequences of CABYV indicated that, unless more than one site on the structural protein is glycosylated, N-glycosylation is not involved in aphid transmission. These results did not corroborate the previous hypothesis for the role of glycosylation in aphid transmission. They, however, revealed the presence of a glycosylated plant protein in purified polerovirus suspensions, whose function in aphid transmission should be further investigated.

Référence

Virology. 2010 Jul 5;402(2):303-14