Dr Ashish Sethi
Dr Ashish Sethi is a structural biologist and postdoctoral research fellow in biochemistry and molecular biology at Bio21 Molecular Science & Biotechnology Institute, at the University of Melbourne. Dr Sethi won the University’s 2020 Early Career Researcher Grant. The award included some funding for a new project on structure elucidation of HIV antigen in complex with bovine antibodies, in collaboration with Professor Damian Purcell at Peter Doherty Institute.
By Sasha Nimmo
‘Meet the Scientists’ Series
‘Meet the Scientists’ is a series of interviews with researchers working on ME and chronic fatigue syndrome. We ask them about their current research and get to meet the people working to improve our health. The series introduces early career researchers through to interviewing scientists and clinicians who have been working on the problems for decades.
Last year Dr Sethi spent time in Boston, USA, visiting a structural biology lab at Harvard Medical School, where a group has developed a new detection method to study intrinsically disordered proteins.
Dr Sethi became involved in ME research when Dr Chris Armstrong’s departure from Australia left a gap at Bio21.
How long have you been involved with ME and CFS research?
I got involved in the ME/CFS research about a year ago. Dr Chris Armstrong and I did our PhD in the same lab supervised by Associate Professor Paul Gooley at the University of Melbourne so when Chris decided to move to California in 2018, I got involved in the projects and have been thoroughly enjoying working in the field since then.
What are you working on at the moment?
Currently, I am working on understanding the host innate immunity antagonism by lyssavirus family which includes rabies and mokola virus. I visited a laboratory at Harvard Medical School in Boston to record a few experiments using an advanced solution Nuclear Magnetic Resonance (NMR) spectroscopic technique which we currently do not have at the University of Melbourne.
I spent three months in Associate Professor Haribabu Arthanari’s lab at the Dana Farber Cancer Institute, Harvard. His group has developed a new method of solution NMR called Direct 15N detection method which is incredible to study intrinsically disordered proteins. As I am working on the Phosphoprotein of rabies virus which is predicted to be 50% disordered, his methodology is best suited for it. I was fortunately successful in purifying P1 and P3 proteins and recording the data sets.
For ME/CFS, I am currently assisting Chris Armstrong and a team led by Professor Paul Fisher at La Trobe University in recording the solution NMR experiments which are used for metabolic profiling in the patients and the control subjects.
What were you working on previously?
I am a structural biologist and I love solving structures of proteins using solution NMR and other structural biology techniques such as Small-Angle X-ray Scattering (SAXS), Cross-link Mass Spectrometry & Cryo-Electron Microscopy. Currently, I am working on two major projects: one related to the negative sense single stranded RNA viruses such as rabies and mokola, and my second project is to study the AAA ATPase p97 enzyme in humans and various pathogens such as leishmania, trypanosoma and toxoplasma as this enzyme is essential for cell homeostasis and also plays a major role in a multiple cellular functions.
As you are looking at things on a nanoscale, is technology making a big difference?
Yes, I can’t agree more that the new technological advances have made a drastic improvement in the quality and depth of research and at the same time, have made it simple and fun to study complex biological systems.
Have you taken over Dr Armstrong’s work at Melbourne University, or are you working differently?
I am very new to ME/CFS research so I won’t say that I have taken over all of Chris’ work but I am definitely learning and growing in the field of ME/CFS research and working in collaboration with Chris.
What is the most exciting finding so far?
My most exciting finding so far is when we discovered an auxiliary binding site in the Relaxin Family Peptide Receptors which was my PhD work and we did that using the principle of paramagnetism in solution NMR. We were very fortunate to publish that finding in Nature Communication journal which I am really proud of.
Do you intend to continue working on ME?
Yes, I would like to keep working in the field of ME/CFS. In the last one year I have met so many extraordinary people and have closely seen the hardships and difficulties of people who are suffering from ME/CFS so I intend to keep working towards better understanding and ultimately finding a cure for this disease.
What are you most proud of in your career?
I love teaching part of my job as a postdoctoral researcher so whenever any of my students perform well either in their course or in the lab I feel very proud.
What would you still like to achieve in your career?
I dream about having my own laboratory one day where I could provide a respectful and diverse work environment and want to make sure that everyone feels supported, encouraged and looked after so I am working hard towards achieving that goal.
What do you enjoying doing outside work?
I am a big foodie and I love cooking so when I am at home I cook different kinds of food and enjoy it with my partner.