Gain of virulence on Rsv1-genotype soybean by an avirulent Soybean mosaic virus requires concurrent mutations in both P3 and HC-Pro.
In soybean, Rsv1, a single dominant resistance gene, invokes extreme resistance (ER) against most Soybean mosaic virus (SMV) strains, including SMV-N, but not SMV-G7, which provokes a virulent lethal systemic hypersensitive response (LSHR). The elicitor functions of the two viruses provoking Rsv1-mediated ER and LSHR have been mapped to the N-terminal 271 amino acids of P3 from SMV-N and SMV-G7, respectively, which differ by nine residues between the two strains. To identify amino acids of P3 from SMV-N provoking Rsv1-mediated ER, the unique residues of SMV-G7 were substituted with those of SMV-N. Of the mutants tested on Rsv1-genotype soybean, only SMV-G7(I788R) and SMV-G7(T948A) lost virulence. However, substitution of amino acids of SMV-N, individually or in combination, with the reciprocal residues from SMV-G7 at these two positions failed to confer virulence to SMV-N. In the search for additional virulence determinants, a series of SMV-N chimeras was generated in which fragments within a region from near the middle of the helper-component proteinase (HC-Pro) cistron to the 5' end of the cytoplasmic inclusion cistron, nucleotides 1,605 to 3,787, were replaced with those of SMV-G7. Only SMV-N-derived chimeras harboring the 3' region of HC-Pro, at least from nucleotide 2,013, and the entire 5' end of P3 (nucleotides 2,430 to 3,237) from SMV-G7 were virulent whereas reciprocal exchanges resulted in loss of SMV-G7 virulence. This region of HC-Pro differs by three amino acids between SMV-N and SMV-G7. Analyses of SMV-G7-derived HC-Pro site-directed mutants showed that only SMV-G7(M683R) lost virulence on Rsv1-genotype soybean; however, SMV-N(R682M) failed to gain virulence. Nevertheless, an SMV-N derived mutant with three concurrent substitutions, R682M+R787I+A947T, gained virulence. The data indicate that both P3 and HC-Pro are involved in virulence of SMV on Rsv1-genotype soybean.
Eggenberger
A L
AL
Department of Plant Pathology, Iowa State University, Ames 50011, USA.
Hajimorad
M R
MR
Hill
J H
JH
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D002678:Chimera / Q000235:genetics; D003546:Cysteine Endopeptidases / Q000235:genetics; D017343:Genes, Plant; D005814:Genes, Viral; D005838:Genotype; D054884:Host-Pathogen Interactions / Q000235:genetics*; D008969:Molecular Sequence Data; D009154:Mutation; D010935:Plant Diseases / Q000235:genetics / Q000821:virology; D017800:Potyvirus / Q000235:genetics* / Q000502:physiology*; D017386:Sequence Homology, Amino Acid; D013025:Glycine max / Q000235:genetics* / Q000821:virology*; D014764:Viral Proteins / Q000235:genetics; D014774:Virulence / Q000235:genetics
D014764:Viral Proteins; D003546:Cysteine Endopeptidases; C072775:HC-Pro protein, potyvirus