Substitution of conserved cysteine residues in wheat streak mosaic virus HC-Pro abolishes virus transmission by the wheat curl mite

• Published in: Archives of virology 2007-10, Vol.152 (11), p.2107-2111
• Main Authors: Young, B. A, Hein, G. L, French, R, Stenger, D. C
• Format: Article
• Language: English
• Subjects: Aceria tosichella; Alanine - chemistry; Amino Acid Sequence; Amino Acid Substitution; Amino acids; Animals; Arachnid Vectors - virology; Biological and medical sciences; Cloning; Cysteine - chemistry; Cysteine Endopeptidases - chemistry; Cysteine Endopeptidases - genetics; Cysteine Endopeptidases - metabolism; Experiments; Fundamental and applied biological sciences. Psychology; Infections; Microbiology; Miscellaneous; Mites - virology; Mutagenesis; Mutation; Potyviridae - physiology; Sequence Alignment; Triticum - virology; Triticum aestivum; Viral Proteins - chemistry; Viral Proteins - genetics; Viral Proteins - metabolism; Virology; Viruses; Wheat streak mosaic virus
• ISSN: 0304-8608; 1432-8798
• DOI: 10.1007/s00705-007-1034-x

Substitutions in the amino-proximal region of wheat streak mosaic virus (WSMV) HC-Pro were evaluated for effects on transmission by the wheat curl mite (Aceria tosichella Keifer). Alanine substitution at cysteine residues 16, 46 and 49 abolished vector transmission. Although alanine substitution at Cys₂₀ had no effect, substitution with arginine reduced vector transmission efficiency. Random substitutions at other positions (Lys₇ to Asn, Asn₁₉ to Ile, and Arg₄₅ to Lys) did not affect vector transmission. These results suggest that a zinc-finger-like motif (His₁₃-X2-Cys₁₆-X29-Cys₄₆-X2-Cys₄₉) in WSMV HC-Pro is essential for vector transmission.