• Identification of the CBP60g protein orthologue of Arabidopsis thaliana in human genome
  • Mohammad Sadegh Abbasi,1,* Dr. Mahdi Safaeizadeh,2 Yeganeh altafi,3 Ali Akbar Ghotbi-Ravandi,4
    1. Department of Cell and Molecular Biology, Faculty of Life Sciences and Biotechnology, Shahid Beheshti University, Tehran, Iran
    2. Department of Cell and Molecular Biology, Faculty of Life Sciences and Biotechnology, Shahid Beheshti University, Tehran, Iran
    3. Department of Plant Sciences and Plant Biology, Faculty of Life Sciences and Biotechnology, Shahid Beheshti University, Tehran, Iran
    4. Department of Plant Sciences and Plant Biology, Faculty of Life Sciences and Biotechnology, Shahid Beheshti University, Tehran, Iran


  • Introduction: Orthologue identification is a critical aspect of bioinformatics and medical biotechnology that allow inferring gene function, estimating species phylogeny, and constructing phylogenetic profiles. CBP60 protein plays an important role in mediating immune responses and disease resistance in plants. CBP60g lacks the C-terminal CaM interaction, with a N-terminal CaM interaction instead. Previous studies have shown that most of the members of the CBP60 family play roles in pathogen and drought resistance. CBP60g acts synergistically with SARD1 in the pathogen resistance, while antagonistically with CBP60a. In this research, the aim was to identify an Arabidopsis thaliana CBP60 protein orthologue in humans.
  • Methods: In this research, the CBP60g protein sequences were obtained from the National Center for Biotechnology Information (NCBI) database. Then, to find the orthologue of this protein in humans, the sequence of this protein was analyzed using Ensembl database and BLAST. Furthermore, the physicochemical characteristics of CBP60 protein and its identified orthologue were used from Uniprot and ExPASy databases. In the next step, we used different bioinformatics program to dissect the orthlogue of CBP60g in the human genome.
  • Results: Through bioinformatics analysis, an orthologue for CBP60 in humans named OPN1MW protein was identified with a similarity percentage of over 60%. The isoelectric point and molecular weight of CBP60g protein are 8.48 and 63067.6 daltons, respectively. The isoelectric point and molecular weight of OPN1MW protein are 8.79 and 40630.40 daltons, orderly.
  • Conclusion: CBP60g, a member of the CBP60 protein family, interacts with calmodulin and is involved in disease resistance and salicylic acid (SA) accumulation. This interaction highlights the potential role of calmodulin in mediating immune responses in plants. Research conducted to identify a human orthologue for CBP60g, which led to the discovery of its human orthologue, OPN1, is of considerable importance in the field of molecular biology and genetics. Both CBP60g and OPN1MW are involved in biological processes related to immunity and disease resistance. CBP60g is a lipase-like protein that forms complexes with other proteins to regulate immune responses and anthocyanin accumulation in plants. Similarly, OPN1MW is a protein involved in the immune response and disease resistance in humans, suggesting a functional similarity between the two proteins. CBP60g has been identified as a transcriptional activator of immune genes in Arabidopsis thaliana. Understanding the role of CBP60g and its human orthologue, OPN1, in regulating the immune response could provide insight into immune defense mechanisms in plants and potentially in humans. Overall, research conducted to identify CBP60g orthologs in humans and their functional implications in immunity is of great importance in advancing our understanding of molecular processes in plants and humans. It opens avenues for further research and potential applications in various fields including agriculture, medicine and biotechnology.
  • Keywords: CBP60, Orthologue, OPN1MW, human disease