Potyvirus Helper Component-Proteinase Self-Interaction in the Yeast Two-Hybrid System and Delineation of the Interaction Domain Involved

• Published in: Virology (New York, N.Y.) Vol. 258; no. 1; pp. 95 - 99
• Main Authors: Urcuqui-Inchima, Silvio, Walter, Jocelyne, Drugeon, Gabrièle, German-Retana, Sylvie, Haenni, Anne-Lise, Candresse, Thierry, Bernardi, Françoise, Le Gall, Olivier
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 25-05-1999; Elsevier
• Subjects: Binding Sites; Cloning, Molecular; Cysteine Endopeptidases - genetics; Cysteine Endopeptidases - metabolism; Lettuce mosaic virus; Life Sciences; Potato virus Y; Potyvirus - enzymology; Saccharomyces cerevisiae; Viral Proteins - genetics; Viral Proteins - metabolism; HC-PRO; VIROLOGIE; VIRUS DE LA MOSAIQUE JAUNE-CHROME DE A VIGNE; INSECTE
• ISSN: 0042-6822; 1096-0341
• DOI: 10.1006/viro.1999.9725

Using the yeast two-hybrid system, a screen was performed for possible interactions between the proteins encoded by the 5′ region of potyviral genomes [P1, helper component-proteinase (HC-Pro), and P3]. A positive self-interaction involving HC-Pro was detected with lettuce mosaic virus (LMV) and potato virus Y (PVY). The possibility of heterologous interaction between the HC-Pro of LMV and of PVY was also demonstrated. No interaction involving either the P1 or the P3 proteins was detected. A series of ordered deletions from either the N- or C-terminal end of the LMV HC-Pro was used to map the domain involved in interaction to the 72 N-terminal amino acids of the protein, a region known to be dispensable for virus viability but necessary for aphid transmission. A similar but less detailed analysis mapped the interacting domain to the N-terminal half of the PVY HC-Pro.