Skip to navigation Skip to content


#IAmScience Gangadhar Vadla

Gangadhar Vadla IamScience.jpg

By Sarah Kiefer | Bond LSC

Sunlight is where it starts for a daffodil. As rays cascade upon the plant, photosynthesis begins and this carbon dioxide and oxygen exchange gives the flower what it needs to survive. For Gangadhar Vadla, he drew a picture of this vibrant process in his head in high school.

“When my teacher was explaining photosynthesis I was in a hallucination of how that was happening in a colorful picture form, and that’s how I got interested in the science,” Vadla said.

Vadla’s passion for processes that fuel our planet’s ecosystem shows in his research as a postdoctoral fellow in the Chris Lorson lab. His work deals with the rare neurodegenerative diseases like spinal muscular atrophy (SMA) and spinal muscular atrophy with respiratory distress (SMARD1), specifically studying protein-to-protein interactions of IGHMBP2 and the modifier ABT1. IGHMBP2, when mutated, leads to SMARD1 or CMT2S.

The biochemical aspect of this work drew Vadla to this work, as well as the prospect to help individuals with the disease. SMARD1 is an extremely rare, inherited nervous system condition that is often fatal in babies. Test animals fair equally poor.

“The animals die in sixteen to eighteen days,” Vadlar said.

SMARD1 results in muscle weakness and respiratory failure when motor neurons — anterior horn cells — in the spinal cord that control muscle movement are damaged and die. A mutated gene causes this nerve decline by creating a faulty protein that affects DNA copying, but it is unknown how this happens. Vadla’s science hopes to help researchers “understand why the mutation relationship is pathogenic,” essential to finding a root protein responsible for the disease.

The IGMHBP2 enzyme is involved in copying DNA in relation to neurodegenerative disorders SMARD1 and the Charcot-Marie-Tooth type 2S disease. The protein ABT1 that Vadla studies is the first protein identified that binds this important enzyme in SMARD1 disease. When ABT1 binds to IGHMBP2, the protein’s ability to breakdown energy, as well as unwind the DNA, increases significantly.

The severity of the SMARD1 disease is directly linked to this biochemical activity, demonstrated, for the first time in the Lorson lab. This discovery exposed the ABT1 modifier as part of the SMARD1 pathology. That is one step closer to finding a cure for the disease.

Vadla earned his bachelors, masters, and Ph.D. degrees, all in biochemistry, at the University of Madras in Chennai, India, his home country. He finds the work environment at Bond LSC to be encouraging because of the frequent conversations he has with his supervisors, namely Dr. Lorson, Dr. Monique Lorson, and collaborator Dr. Singh, sharing thoughts and having intellectual discussions surrounding research topics.

“I want to thank my PI’s and lab members for being a great support system,” Vadla said.

Outside of the long hours Vadla spends in the lab, he comes home to his wife and children. He is currently trying to teach his children how to play chess, cricket, and badminton, games of both strategy and tactic. It is not uncommon on weekends for them to do all of the above.
When not playing with his kids or watching family movies, Vadla devotes time to another passion. Writing short stories and movie scripts is a hobby that Vadla has taken up, brainstorming new characters or narratives along the way. He recently finished a two-hour-long movie script in his native language, Telegu, India, of which he frequently writes in. He balances his family life activities and hobbies with his lab work each day.
Vadla is intrigued with the “organization of the reactions within the cell and nucleus,” that he works with every day, and hopes to continue his work in protein-to-protein interactions and relationships even after the completion of the research he is doing in the Lorson lab.

Article originally published on Decoding Science.