|Moon, Jaeson - UNIV OF ILLINOIS|
Submitted to: Phytopathology
Publication Type: Abstract Only
Publication Acceptance Date: August 7, 1995
Publication Date: N/A
Technical Abstract: Barley yellow dwarf virus (BYDV) is a member of luteoviruses, aphid-transmitted in a persistent manner, and phloem-limited in host plants. The full-length BYDV-PAV-IL cDNA clone (pGP11) flanked by CaMV 35S promoter and nopaline synthase transcription terminator was constructed in pTZ19R. The mutant clone (pGP12) was constructed by site-directed mutagenesis in which the start condon of ORF4 was replaced b ACG without changing amino acid sequence of coat protein. When oat protoplasts were transfected with linearized pGP11 by electroporation and cultured 5 days, the 22 KSa coat protein accumulated to essentially to the same levels as in protoplasts transfected with purified BYDV RNA. To determine if the 17 KDA protein was necessary for replication, pGP12 was transfected with as described above. While pGP12 was infectious, the 22 KDa coat protein accumulated to lower levels in protoplasts transfected with pGP12 than in protoplasts transfected with pGP11. The result indicated that the 17 KDa protein was not essential for viral replication.