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Arabidopsis thaliana’s  VirE2-Interacting Protein 1 (VIP1) interacts with  Agrobacterium tumefaciens  VirE2 protein and regulates stress responses and plant immunity signaling occurring downstream of the Mitogen-Activated Protein Kinase (MPK3) signal transduction pathway. In this study, a full-length cDNA of 972bp encoding  HvVIP1  was obtained from barley ( Hordeum vulgare  L.) leaves. A corresponding 323 amino acid poly-peptide was shown to carry the conserved bZIP (Basic Leucine Zipper) domain within its 157 th  and 223 rd  amino acid residue. 13 non-synonymous SNPs were spotted within the  HvVIP1  bZIP domain sequence when compared with  AtVIP1 . Moreover, minor differences in the bZIP domain locations and lengths were noted when comparing  Arabidopsis thaliana  and  Hordeum vulgare  VIP1 proteins through the 3D models, structural domain predictions and disorder prediction profiling. The expression of  HvVIP1  was stable in barley tissues infected by pathogen (whether  Agrobacterium tumefaciens  or  Fusarium culmorum ), but was induced at specific time points. We found a strong correlation between the transcript accumulation of  HvVIP1  and barley PR- genes  HvPR1 ,  HvPR4  and  HvPR10 , but not with  HvPR3  and  HvPR5 , probably due to low induction of those particular genes. In addition, a gene encoding for a member of the barley MAPK family,  HvMPK1 , showed significantly higher expression after pathogenic infection of barley cells. Collectively, our results might suggest that early expression of PR genes upon infection in barley cells play a pivotal role in the  Agrobacterium -resistance of this plant.

Characterisation of HvVIP1 and expression profile analysis of stress response regulators in barley under Agrobacterium and Fusarium infections