Professional Education

  • Doctor of Philosophy, Ludwig Maximilian Universitat Munchen (2010)

Stanford Advisors


  • Venkata Raveendra Pothineni. "United States Patent US 621079,537 INHIBITORS OF BORRELIA METAL TRANSPORTER FOR TREATMENT OF LYME DISEASE", stanford, Nov 28, 2014

Current Research and Scholarly Interests

high throughput screening new drugs for borrelia burgdorferi

Journal Articles

  • Varicella Zoster Virus ORF25 Gene Product: An Essential Hub Protein Linking Encapsidation Proteins and the Nuclear Egress Complex JOURNAL OF PROTEOME RESEARCH Pinto, M. G., Pothineni, V. R., Haase, R., Woidy, M., Lotz-Havla, A. S., Gersting, S. W., Muntau, A. C., Haas, J., Sommer, M., Arvin, A. M., Baiker, A. 2011; 10 (12): 5374-5382


    Varicella zoster virus (VZV) ORF25 is a 156 amino acid protein belonging to the approximately 40 core proteins that are conserved throughout the Herpesviridae. By analogy to its functional orthologue UL33 in Herpes simplex virus 1 (HSV-1), ORF25 is thought to be a component of the terminase complex. To investigate how cleavage and encapsidation of viral DNA links to the nuclear egress of mature capsids in VZV, we tested 10 VZV proteins that are predicted to be involved in either of the two processes for protein interactions against each other using three independent protein-protein interaction (PPI) detection systems: the yeast-two-hybrid (Y2H) system, a luminescence based MBP pull-down interaction screening assay (LuMPIS), and a bioluminescence resonance energy transfer (BRET) assay. A set of 20 interactions was consistently detected by at least 2 methods and resulted in a dense interaction network between proteins associated in encapsidation and nuclear egress. The results indicate that the terminase complex in VZV consists of ORF25, ORF30, and ORF45/42 and support a model in which both processes are closely linked to each other. Consistent with its role as a central hub for protein interactions, ORF25 is shown to be essential for VZV replication.

    View details for DOI 10.1021/pr200628s

    View details for Web of Science ID 000297537200010

    View details for PubMedID 21988664