Bangalore University, India
Dr. Uday Jayarmaiah has completed his PhD at the age of 30 years from Bangalore University and postdoctoral studies from Groningen University, Netherlands. He is the faculty of Department of Life Science ,Bangalore University a premier organization. He has published more than 5 papers in reputed journals and has been serving as an editorial board member of repute.
The research focused on intracellular bacteria Wolbachia, which are widespread symbionts of arthropods and filarial nematodes. This organism manipulates its hosts’ reproductive machinery and can also cause diseases. Recent research indicates its potential application in pest bio-control tool and as a target for arthropod disease transmitting vectors .The molecular mechanisms behind the Wolbachia-induced phenotypes are yet to be established. Outer membrane proteins (OMPs) of Gram-negative bacteria play a key role in bacterial-host interactions. Recent experimental studies have also shown that Wolbachia surface protein (WSP) an OMP can trigger host immune responses and control programmed cell death in humans. This suggests that WSP might play a key role during establishment and persistence of symbiotic associations in arthropods. However, while considerable attention has been given to OMPs of vertebrate pathogens, little is known about the role of these proteins in bacteria that primarily infect invertebrates. Since we were able to obtain WSP in a soluble form (through earlier work at our home university), further studies were taken up to determine the three-dimensional structure of WSP that will help to understand the function of the protein. This information could form the basis for development of drug targets and identification of inhibitors with antimicrobial activity. This would enable treatment of diseases by targeting Wolbachia endosymbionts in the vectors (as they required Wolbachia for their survival), such as the filarial nematode Brugia malayi, the causative agent of elephantiasis .Membrane protein crystallization holds specific challenges compared with soluble proteins both in obtaining initial crystals and significant effort is usually required to improve the resolution sufficiently to support structure solution. The diffraction data we obtained for WSP crystal is impressive, as there is absence of salt diffraction peaks. The mesh scans performed at ID30A-1, indicates the presence of a protein crystal. It may take multiple stages of optimization to obtain crystals that yield a diffraction pattern suitable for data collection and structure determination. The next steps in this project are to repeat our experiments with freshly prepared sample as it was challenging to improve (or even to reproduce) the diffraction quality of crystal obtained using a single sample.