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. 1991 Sep 1;88(17):7887–7891. doi: 10.1073/pnas.88.17.7887

Amino acid substitutions in the coat protein result in loss of insect transmissibility of a plant virus.

P L Atreya 1, C D Atreya 1, T P Pirone 1
PMCID: PMC52409  PMID: 1881922

Abstract

Amino acids near the N terminus of the coat protein of tobacco vein mottling virus were deleted or altered by site-directed mutagenesis to determine the effect on aphid transmissibility of the virus. Deletion of a three amino acid sequence Asp-Ala-Gly, which is conserved in aphid-transmissible potyvirus isolates, abolished transmission. The mutation Ala----Thr in this triplet drastically reduced transmission, whereas the mutation Asp----Asn had no effect, and the mutation Asp----Lys consistently reverted to the wild-type residue. The mutation Lys----Glu, in the residue adjacent to the glycine of the triplet, drastically reduced transmission, whereas the mutation Gln----Pro, seven residues downstream from the glycine had no effect. Comparison of the sequences of other potyviruses suggests that the presence of a glycine residue at the third position of the Asp-Ala-Gly triplet is critical for aphid transmissibility and that certain changes in the residues adjacent to this position abolish or greatly reduce aphid transmissibility.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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