Alok Kumar Datta obtained his BSc (Hons) and MSc in Chemistry and Biochemistry, respectively, from the Calcutta University, and earned his PhD degree (1974) under the guidance of Professor DP Burma. He then joined the laboratory of Dr SK Niyogi at the Oak Ridge National Laboratory, USA as a post-doctoral Investigator. After returning in 1984, Datta joined the Indian Institute of Chemical Biology (IICB), Kolkata.
Academic and Research Achievements: During his PhD work Datta was able to reconstitute biologically functional ribosomes from the ribosomal RNA and its split proteins, which, later set the stage for subsequent ribosome research in this country. Datta's work at Oak ridge National Lab (USA) along with Dr Niyogi led to discovery of a novel ribonuclease activity, which was termed as 'Oligoribounclease' based on its substrate specificity. Mechanistic characterization of the enzyme led them to implicate it to be a part of the messenger RNA processing component. Subsequent work by others supported their proposal and led to understanding of the enigmatic problem of mRNA decay mechanism. The work of Datta at the University of North Carolina, Chapel Hill, USA on the mechanism of action of antiherpetic drug, 'Acyclovir' on Epstein-Barr virus, also had significant impact on the treatment of infection caused due to herpes virus. At IICB, he developed a new area of research on purine salvage enzyme system of the parasitic protozoa. He was the first to establish that adenosine kinase (AdK) of purine auxotrophic parasites could be an exploitable chemotherapeutic target. His laboratory's work on cloning of the enzyme from Leishmania donovani, delineation of its active site, mechanistic aspects of the reaction and eventual structural analysis have been internationally acclaimed. Elucidation of an old unsolved riddle, as to why L donovani as opposed to most other parasites is refractory to cyclosporin A (CsA) inhibitions, is another significant finding of his laboratory. His laboratory was the first to clone and characterize an endoplasmic reticulum-located cyclophilin (LdCyP) gene from the parasite. The LdCyP acts as a chaperone by binding to proteins rather than as the mediator of calcineurin inhibition, the target for CsA actions. Using newly identified inactive soluble AdK aggregate as the substrate, his laboratory demonstrated that LdCyP alone, in presence of CsA, could disaggregate and reactivate the enzyme. Studies indicated that ADP, one of the products of the reaction, is responsible for aggregation of the enzyme during reaction. This ATP-independent and CsA-insensitive chaperone function of CyP, hitherto unknown in chaperone literature, raises a possibility that under in vivo conditions, LdCyP may regulate the activity of aggregation prone proteins by ensuring their disaggregation. He has published several research and review articles, mostly in high impact journals and mentored a large number of PhD students.
Other Contributions: Datta was on the Editorial Board of the Journal of Biosciences. He has served as member in various academic and scientific committees.
Awards and Honours: Datta is a recipient of Professor IS Bhatia Memorial Award by the Society of Biological Chemists, India. He is a Fellow of the Indian Academy of Sciences, Bangalore; National Academy of Sciences (India), Allahabad.