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.
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.
Revollon
S
S
INRA, Université de Strasbourg UMR SVQV, 28 rue de Herrlisheim BP 20507, 68021 Colmar, France.
Strub
J M
JM
Fitchette
A-C
AC
Wiss
L
L
Gomord
V
V
Van Dorsselaer
A
A
Brault
V
V
D000818:Animals; D000906:Antibodies / Q000378:metabolism; D001042:Aphids / Q000821:virology*; D029688:Brassica napus / Q000821:virology*; D002241:Carbohydrates / Q000032:analysis*; D006031:Glycosylation; D037102:Lectins / Q000378:metabolism; D052679:Luteoviridae / Q000737:chemistry*; D013058:Mass Spectrometry; D015678:Viral Structural Proteins / Q000737:chemistry*
D000906:Antibodies; D002241:Carbohydrates; D037102:Lectins; D015678:Viral Structural Proteins