Submitted to: Virology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: April 4, 2001
Publication Date: July 15, 2001
Citation: LI, C., COX-FOSTER, D., GRAY, S.M., GILDOW, F.E. VECTOR-SPECIFICITY OF BARLEY YELLOW DWARF LUTEOVIRUS TRANSMISSION: IDENTIFICATION OF POTENTIAL CELLULAR RECEPTORS BINDING BYDV-MAV IN THE APHID SITOBION AVENAE. VIROLOGY. 2001.
Interpretive Summary: Barley yellow dwarf disease of cereals is caused by several related viruses and is the most significant virus disease of cereal crops worldwide. Each of the six viruses that cause BYD is transmitted by different aphid species because each virus and aphid has unique properties that must be compatible for transmission to occur. Our previous work has identified the path that a virus takes as it moves from the aphids stomach to the blood system and out through the salivary system. It is also known where in this route a virus not transmitted by a particular aphid species is blocked. In most instances when an aphid cannot transmit a virus it is because the virus cannot enter the salivary system and therefore cannot be spit back into a plant when the aphid feeds on a plant. This study has identified proteins present in the head of a vector aphid, but not in a non-vector aphid, that attach to virus particles. These are the first aphid proteins identified that interacts with virus. The proteins are thought to be receptors located on the surface of the salivary glands that allow virus to attach to, and move into, the aphids salivary system and ultimately allow the virus to be transmitted. Knowing what these receptor proteins are and how they function should allow the development of new methods to prevent or diminish the ability of aphids to transmit viruses between plants.
Two proteins (SaM35 and SaM50) isolated from head tissues of the aphid vector, Sitobion avenae, were identified as potential receptors for barley yellow dwarf virus-MAV (Luteoviridae) based on MAV virus overlay assays and immunoblots of urea SDA 2-D gels. An antiidiotypic antibody (MAV4 antiID) that mimics an epitope on MAV virions and competes with MAV in antibody binding assays, also bound to SaM50 and SaM35 and to six additional proteins including a GroEL homolog. No MAV-binding proteins were detected from the non-vector aphid, Rhopalosiphum maidis, although MAV4 Anti-ID did react with four proteins from R. maidis. It is hypothesized that SaM35 and SaM50 may be MAV receptors involved in MAV transmission based on their high affinity for MAV and their unique association with the vector, S. avenae. The additional aphid proteins binding the MAV4 antiID may represent less specific virus-binding proteins facilitating transmission through different taphid tissues.