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. 2011 Nov;85(22):11809–11820. doi: 10.1128/JVI.00297-11

Fig. 8.

Fig. 8.

Yeast two-hybrid assay. (A) Mapping the interacting domains of VP1 and Anx2. Three overlapping cDNA fragments of VP1 (encoding amino acids 1 to 70, 40 to 180, and 140 to 297) and four cDNA fragments of Anx2 (encoding amino acids 36 to 107, 108 to 179, 192 to 264, and 268 to 339) were cloned into pBTM116 and the pACT2 vector, respectively, and were used in a yeast two-hybrid assay. Only cells cotransfected with VP1 (aa 40 to 180) and Anx2 (aa 268 to 339) grew colonies and showed positive β-galactosidase activity. His−, medium lacking His. (B) Fine mapping of the VP1 domain. The VP1 cDNA fragment encoding aa 40 to 180 was used as a PCR template for the generation of several VP1 cDNA deletion fragments, which were cloned into the pBTM116 vector for cotransfection with pACT2/Anx2268–339. The VP1 peptides that do (black lines) and do not (gray lines) interact with Anx2 (aa 268 to 339) are indicated by plus and minus signs, respectively, on the right.