There is a paucity of tools to study vector biology and vectorvirus-host interactions at the molecular level; however, mass spectrometry technologies are emerging as one of the most powerful tools to develop a comprehensive understanding of virusvector-host interactions [9, 18, 22, 77, 78, 79, 80, 81, 82, 83] . We used mass spectrometry to describe several host proteins that associate with virions and to show they may even be ingested by aphids during feeding. The mounting body of evidence is that luteovirids commandeer their hosts and vectors to ensure their own survival and transmission. For instance, luteovirids move from companion cells into sieve elements but natural selection has favored their retention in the phloem of host plants and hence, dispersal by aphids. Luteovirid infection may also exert changes in the phloem proteome, changes that may also facilitate virus dispersal by aphids. A critical next experiment would have to distinguish between the following two hypotheses a) that virion-host protein complexes are internalized into aphids or b) that the virus manipulates the phloem to have a higher concentration of these proteins during infection. Due to the dynamic nature of protein trafficking in plants [61, 63, 84, 85, 86, 87] and cell-type specific transcriptional regulation [88] , the latter experiment is not a trivial undertaking. The current work has laid the groundwork for these future experiments. The virus-host interactome we describe in this study provides critical insights into the biochemical mechanisms that luteovirids use for movement in plants and aphids. These plant proteins (and associated biochemical pathways) are novel targets for developing host-resistance to luteovirid infection in cereals and other crops. Furthermore, the exciting, serendipitous discovery that sodium sulfite reduces transmissibility of virions provides biochemical evidence that intra or intermolecular disulfide bonding may be required for luteovirid entry into aphid cells and may also be exploited as part of a strategy to disrupt aphid-virus interactions and ultimately to mitigate virus transmission.