In order to understand the molecular mechanisms underlying circulative transmission of potato leafroll virus (PLRV) by aphids, we screened proteins as putative PLRV binding molecules using a virus overlay assay of protein blots. In this way, we found that purified PLRV particles exhibited affinity for five aphid proteins. The one most readily detected has an of 63K, and was identified as symbionin. This is the predominant protein synthesized by the bacterial endosymbiont of the aphid and is released into the haemolymph. Since further studies clearly showed that PLRV particles also bind to native symbionin, it was envisaged that virus particles when acquired into the haemocoel of an aphid interact with symbionin. Inhibition of prokaryotic protein synthesis by feeding nymphs on an antibiotic-containing artificial diet prior to PLRV acquisition reduced virus transmission by more than 70%. The major coat protein of the virus was found to be degraded in the antibiotictreated aphids; this would obviously have resulted in an increased exposure of viral RNA to enzymic breakdown and concomitant loss of infectivity. For these reasons we conclude that endosymbiotic bacteria play a crucial role in determining the persistent nature of PLRV in the aphid haemolymph and that symbionin is probably the key protein in this interaction.


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