Avadhesha Surolia

Avadhesha Surolia (Born 3 December 1947, Kishangarh, Rajasthan)[1] is a Glycobiologist at Indian Institute of Science (IISc), Bangalore. Presently, he is an Honorary Professor at the Molecular Biophysics Unit (MBU), IISc[2] and holds the Bhatnagar fellowship of the Council of Scientific and Industrial Research (CSIR), India.[2] He is known for his work on lectin structure and interactions, orientation and dynamics of cell surface carbohydrate receptors and protein folding, diabetes, anti-malarials and anti-cancer agents based on curcumin, flavonoids, etc. In addition, neuropathic pain, neurodegenerative disorders and the link between immunity and obsessive compulsive disorder are areas of his current interest

Education and Career

Surolia obtained his bachelor's degree in Chemistry and Biology from University of Jodhpur, in 1970. He earned his master's degree in Biochemistry from Maharaja Sayajirao University, Baroda in 1972. He completed his Ph.D under the guidance of Prof. B. K. Bachhawat from Madras University in 1976. In 1978 he was awarded a D.Sc degree by Madras University. After his doctoral studies he joined Indian Institute of Chemical Biology (IICB), Calcutta, India as a scientist in 1977 till 1981. He further held the position of Assistant Professor at IICB till 1986 after which he joined Molecular Biophysics Unit (MBU) at IISc as an Associate Professor (1986-1991). He was Professor at MBU, IISc from 1991 to 2013 and served as its Chairman from 2000 to 2006. From 2006 to 2011 he held the Directorship of India’s prestigious research institute, National Institute of Immunology, New Delhi.[1][3] During his tenure NII was recognized by Thomson Reuters Innovation Award in 2010 as the most innovative research institute nationally.[4][5] He holds Honorary Professorship at Jawaharlal Nehru Centre for Advanced Scientific Research (JNCASR), Bangalore, India.[6] In recognition of his contributions to medicine and science he was conferred an Honorary D.Sc degree in 2013 by Queen’s University, Belfast, UK.[7][8][9][10]

Scientific Contributions

Surolia has elucidated the role of glycosphingolipids as biological receptors through studies on lectin-glycolipid interactions using liposomes.[11] He discovered novel blood group and tumor antigen specific lectins[12] and made original contribution towards elucidation of the energetics and mechanism of protein-sugar recognition. He genetically re-engineered carbohydrate specificities of lectins imparting exquisite T-antigen tumor recognizing ability to peanut agglutinin.[13] He delineated the molecular basis of carbohydrate recognition by legume lectins[14][15][16][17][18] and demonstrated the novel C-H…O/N hydrogen bond in protein-sugar interactions.[19] He studied thermal unfolding of lectins that led to the discovery of novel modes of oligomerization in them.[20][21] He found a molten globule monomeric intermediate during the folding of peanut agglutinin that retained its carbohydrate binding ability - establishing ‘wet’ molten globule as an “on pathway” folding intermediate and characterized other early intermediates.[21][22][23] His studies showed that the monomers of legume lectins have the necessary structural features for carbohydrate recognition and that oligomerization imparts them with topology necessary for their biologic activities such as agglutination, mitogenesis etc. He elucidated the molecular features of substrate recognition by endoplasmic reticulum chaperones calreticulin and Calnexin.[24][25] He discovered the unusual quaternary structure of peanut agglutinin[26] and a novel lectin fold in Jacalin[27] as well as the structural basis of inactivation of ribosomes by gelonin.[28] He enunciated that solvent reorganization in protein-ligand interactions modulates their specificities.[29][30] Showed the existence of co-operativity in lectin- multimeric sugar interactions. Surolia explained the enigmatic endotoxin neutralizing activity of polymyxin B to its specific ability to remove endotoxin from its assembly and attributed it to its unique amphiphilicity.[31][32][33][34] He popularized Protein A as a tool in immunology.[35][36] He discovered the broad substrate specificity of a key enzyme of biotin biosysnthesis from M. tuberculosis[37] and reported novel inhibitors for it. He has demonstrated the potential of common dietary components- curcumin and green tea catechins as anti-cancer and anti-malarial agents.[38][39][40] He has developed a rhodanine, BCFMT, as a potential therapeutic for cancer.[41] Surolia co-discovered the existence of the fatty acid synthesis (FAS) pathway in Plasmodium and demonstrated its remarkable distinction from that of its human host.[42] He co-identified triclosan, a widely used biocide, to compromise the growth of the parasite by inhibiting its enoyl-ACP reductase (FabI).[42] These apart, Surolia has also ventured into the field of chronic disease biology where he has developed a novel form of insulin Supramolecular Insulin Assembly-II (SIA-II) for long-lasting treatment of type I diabetes mellitus.[43][44][45] In addition to protein–sugar interactions his research is also focused on neuropathic pain, neurodegenerative disorders and the link between immunity and obsessive compulsive disorder. Curcumin and its designed analogs are being developed as experimental therapeutics for these diseases and cancer. His findings have been commercially exploited by a number of international companies such as Amersham-Pharmacia, Sigma Chemical Co., Pierce Corporation, Bangalore Genei, Datascope Corp., Shantha Biotechniques Pvt. Ltd. He has about 19 national and international patents.[46] Surolia has published about 360 scientific papers in peer-reviewed journals of high impact factor. He has an h-index of 41 and his publications have been cited over 5000 times.

Fellowships and Memberships

Surolia is a member of: Third World Academy of Sciences (TWAS), Trieste, Italy[47] and International Molecular Biologists Network.[48] He is a fellow of all the science academies in the country- National Science Academy, Indian National Science Academy and Indian Academy of Sciences.[1][49] He was a member of the Board of Trustees, Human Frontier Scientific Programme (HFSP, Strasbourg).[2][50][51] He is the only Indian member of the International Glycoconjugate Organization since 1998 and served as its president from 2001-2004.[3][52] He has been a visiting scientist at Massachusetts Institute of Technology, University of Maryland and University of Michigan, USA.[3] He has chaired a number of Study sections of Department of Biotechnology, Department of Science and Technology and CSIR (India) and continues to advise a number of Institutions and Academic bodies in India and abroad. He is currently Bhatnagar Fellow of CSIR (India), was a JC Bose Fellow of DST (India), Honorary Professor, Indian Institute of Science, and member Executive Committee of the International Union of Biochemistry and Molecular Biology (IUBMB).[2][53] He is in the editorial advisory board of IUBMB-Life and Plos One. He has served as an editor of the Proceedings of the Indian National Science Academy from 1998 to 2001. He is an editorial board member of the Proceedings of the National Academy of Sciences (India) and the Indian Journal of Biotechnology.

Awards

Jawaharlal Nehru Birth Centenary Lecture (2008).,[54] B.K. Bachhawat Memorial Award 2007, J.C.Bose Fellowship (2006),[55] Dr. B.R. Ambedkar Centenary Award for Excellence in Biomedical Research (2003),[56] Goyal Prize in the area of Life Sciences (2002),[1] Third World Academy of Sciences Prize in Biology (2001),[57] Professor GN Ramachandran 60th Birthday Commemoration Medal (2000),[54] Alumni Award (IISc, 1999),[1] Ranbaxy Science Foundation Award in Basic Medical Sciences (1995),[1] Shri Om Prakhash Bhasin Award for Biotechnology (1993),[58] FICCI award for outstanding research in Biological Sciences (1993), W.H. Stillmark Prize (Honorary) for outstanding research contributions on lectins (1990),[1] S.S. Bhatnagar Award for Outstanding Research in Biological Sciences (1987),[1] INSA Young Scientist Medal (1976)[1]

References

  1. 1 2 3 4 5 6 7 8 9 "Indian Fellow". insaindia.org. INSA. Retrieved 25 March 2014.
  2. 1 2 3 4 "Avadhesha Surolia" (PDF). ics2014bangalore.in. Retrieved 25 March 2014.
  3. 1 2 3 "Prof. Surolia's Lab". mbu.iisc.ernet.in. MBU. Retrieved 25 March 2014.
  4. ↑ "Intellectual Property and Science". ip-science.thomsonreuters.com. Thomson Reuters. Retrieved 25 March 2014.
  5. ↑ "THOMSON REUTERS AND CONFEDERATION OF INDIAN INDUSTRY (CII) RECOGNISE INDIA'S MOST INNOVATIVE ACADEMIC INSTITUTIONS AND ENTERPRISES". www.iii.gov.in. Retrieved 25 March 2014.
  6. ↑ "Honorary Faculty". www.jncasr.ac.in. JNCASR. Retrieved 25 March 2014.
  7. ↑ "Winter Graduation". www.qub.ac.uk. QUB. Retrieved 25 March 2014.
  8. ↑ www.mediator.qub.ac.uk. QUB http://www.mediator.qub.ac.uk/ms/graduations/summer2013/Hongrad13SH.wmv. Retrieved 25 March 2014. Missing or empty |title= (help)
  9. ↑ "Team GB mastermind and international leading scientists honoured at Queen's". www.qub.co.uk. QUB. Retrieved 25 March 2014.
  10. ↑ media.wix.com (PDF). QUB http://media.wix.com/ugd/896ed7_7e8d0bff8351cc0fbc9372e04576113a.pdf. Retrieved 25 March 2014. Missing or empty |title= (help)
  11. ↑ Satish P.R., Surolia A. (2002). "Preparation and characterization of glycolipid-bearing multilamellar and unilamellar liposomes.". Methods in molecular biology. 199: 193–202. PMID 12094570.
  12. ↑ Patanjali S.R., Sajjan S. U.; Surolia A. (1988). "Erythrocyte-binding studies on an acidic lectin from winged bean (Psophocarpus tetragonolobus)". Biochemistry Journal. 252 (3): 625–631. PMID 2458714.
  13. ↑ Sharma V, Vijayan M; Surolia A (1996). "Imparting exquisite specificity to peanut agglutinin for the tumor-associated Thomsen-Friedenreich antigen by redesign of its combining site.". Journal of Biological Chemistry. 271 (35): 21209–21213. PMID 8702892.
  14. ↑ Banerjee R, Das K, Ravishankar R, Suguna K, Surolia A; Vijayan M (1996). "Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex". Journal of Molecular Biology. 259 (2): 281–296. PMID 8656429.
  15. ↑ Sharma V, Surolia A (1997). "Analyses of carbohydrate recognition by legume lectins: size of the combining site loops and their primary specificity.". Journal of Molecular Biology. 267 (2): 433–445. PMID 9096236.
  16. ↑ Sharma V, Srinivas VR, Adhikari P, Vijayan M; Surolia A (1998). "Molecular basis of recognition by Gal/GalNAc specific legume lectins: influence of Glu 129 on the specificity of peanut agglutinin (PNA) towards C2-substituents of galactose.". Glycobiology. 8 (10): 1007–1012. PMID 9719681.
  17. ↑ Thomas CJ, Surolia A (2000). "Mode of molecular recognition of L-fucose by fucose-binding legume lectins". Biochemical and biophysical research communications. 268 (2): 262–267. PMID 10679191.
  18. ↑ Srinivas VR, Acharya S, Rawat S, Sharma V; Surolia A (2000). "The primary structure of the acidic lectin from winged bean (Psophocarpus tetragonolobus): insights in carbohydrate recognition, adenine binding and quaternary association.". FEBS Letters. 474 (1): 76–82. PMID 10828455.
  19. ↑ Ravishankar R, Ravindran M, Suguna K, Surolia A; Vijayan M (1997). "Crystal structure of the peanut lectin – T-antigen complex. Carbohydrate specificity generated by water bridges". Current Science. 72: 855–861.
  20. ↑ Reddy GB, Bharadwaj S; Surolia A (1999). "Thermal stability and mode of oligomerization of the tetrameric peanut agglutinin: a differential scanning calorimetry study.". Biochemistry. 38 (14): 4464–4470. PMID 10194368.
  21. 1 2 Reddy GB, Srinivas VR, Ahmad N; Surolia A (1999). "Molten globule-like state of peanut lectin monomer retains its carbohydrate specificity. Implications in protein folding and legume lectin oligomerization". Journal of Biological Chemistry. 274 (8): 4500–4503. PMID 9988681.
  22. ↑ Mitra N, Sinha S, Kini RM; Surolia A (2005). "Analysis of the peanut agglutinin molten globule-like intermediate by limited proteolysis". Biochimica et Biophysica Acta. 1725 (3): 283–289. PMID 16051441.
  23. ↑ Hansia P, Dev S, Surolia A; Vishveshwara S (2007). "Insight into the early stages of thermal unfolding of peanut agglutinin by molecular dynamics simulations.". Proteins. 69 (1): 32–42. PMID 17596827.
  24. ↑ Kapoor M, Srinivas H, Kandiah E, Gemma E, Ellgaard L, Oscarson S, Helenius A; Surolia A (2003). "Interactions of substrate with calreticulin, an endoplasmic reticulum chaperone.". Journal of Biological Chemistry. 278 (8): 6194–6200. PMID 12464625.
  25. ↑ Gopalakrishnapai J, Gupta G, Karthikeyan T, Sinha S, Kandiah E, Gemma E, Oscarson S; Surolia A (2006). "Isothermal titration calorimetric study defines the substrate binding residues of calreticulin.". Biochemical Biophysical Research Communications. 351 (1): 14–20. PMID 17049488.
  26. ↑ Banerjee R, Mande SC, Ganesh V, Das K, Dhanaraj V, Mahanta SK, Suguna K, Surolia A; Vijayan M (1994). "Crystal structure of peanut lectin, a protein with an unusual quaternary structure.". Proceedings of the National Academy of Sciences of the United States of America. 91 (1): 227–231. PMID 8278370.
  27. ↑ Sankaranarayanan R, Sekar K, Banerjee R, Sharma V, Surolia A; Vijayan M (1998). "A novel mode of carbohydrate recognition in jacalin, a Moraceae plant lectin with a beta-prism fold.". Nature Structural Biology. 3 (7): 596–603. PMID 8673603.
  28. ↑ Hosur MV, Nair B, Satyamurthy P, Misquith S, Surolia A; Kannan KK (1995). "X-ray structure of gelonin at 1.8 A resolution.". Journal of Molecular Biology. 258 (3): 368–380. PMID 7608981.
  29. ↑ Singha NC, Surolia N; Surolia A (1996). "On the relationship of thermodynamic parameters with the buried surface area in protein-ligand complex formation.". Bioscience Reports. 16 (1): 1–10. PMID 8861535.
  30. ↑ Swaminathan CP, Nandi A, Visweswariah SS; Surolia A (1999). "Thermodynamic analyses reveal role of water release in epitope recognition by a monoclonal antibody against the human guanylyl cyclase C receptor.". Journal of Biological Chemistry. 274 (44): 31272–31278. PMID 10531324.
  31. ↑ Srimal S, Surolia N, Balasubramanian S; Surolia A (1996). "Titration calorimetric studies to elucidate the specificity of the interactions of polymyxin B with lipopolysaccharides and lipid A.". Biochemical Journal. 315 (Pt2): 679–686. PMID 8615847.
  32. ↑ Thomas CJ, Surolia N; Surolia A. (1999). "Surface plasmon resonance studies resolve the enigmatic endotoxin neutralizing activity of polymyxin B.". Journal of Biological Chemistry. 274 (42): 29624–29627. PMID 10514430.
  33. ↑ Thomas CJ, Surolia A (1999). "Kinetics of the interaction of endotoxin with polymyxin B and its analogs: a surface plasmon resonance analysis.". FEBS Letters. 445 (2-3): 420–424. PMID 10094500.
  34. ↑ Bhor VM, Thomas CJ, Surolia N; Surolia A (2005). "Polymyxin B: an ode to an old antidote for endotoxic shock.". Molecular Biosystems. 1 (3): 213–222. PMID 16880985.
  35. ↑ Pain D, Surolia A (1981). "Preparation of protein A-peroxidase monoconjugate using a heterobifunctional reagent, and its use in enzyme immunoassays.". Journal of Immunological Methods. 40 (2): 219–230. PMID 6265559.
  36. ↑ Pain D, Surolia A (1979). "Protein A-enzyme monoconjugate as a versatile tool for enzyme immunoassays.". FEBS Letters. 107 (1): 73–76. PMID 387451.
  37. ↑ Bhor VM, Dev S, Vasanthakumar GR, Kumar P, Sinha S; Surolia A (2006). "Broad substrate stereospecificity of the Mycobacterium tuberculosis 7-keto-8-aminopelargonic acid synthase: Spectroscopic and kinetic studies.". Journal of Biological Chemistry. 281 (35): 25076–25088. PMID 16769720.
  38. ↑ Sharma SK, Parasuraman P, Kumar G, Surolia N; Surolia A (2007). "Green tea catechins potentiate triclosan binding to enoyl-ACP reductase from Plasmodium falciparum (PfENR).". Journal of Medicinal Chemistry. 50 (4): 765–775. PMID 17263522.
  39. ↑ Mishra S, Karmodiya K, Surolia N; Surolia A (2008). "Synthesis and exploration of novel curcumin analogues as anti-malarial agents.". Bioorganic and Medicinal Chemistry. 16 (6): 2894–2902. PMID 18194869.
  40. ↑ Chakraborti S, Das L, Kapoor N, Das A, Dwivedi V, Poddar A, Chakraborti G, Janik M, Basu G, Panda D, Chakrabarti P, Surolia A; Bhattacharyya B (2011). "Curcumin recognizes a unique binding site of tubulin.". Journal of Medicinal Chemistry. 54 (18): 6183–6196. PMID 21830815.
  41. ↑ Rai A, Surolia A; Panda D (2012). "An antitubulin agent BCFMT inhibits proliferation of cancer cells and induces cell death by inhibiting microtubule dynamics.". PLOS ONE. 7 (8). PMID 22952952.
  42. 1 2 Surolia N, Surolia A (2001). "Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum.". Nature Medicine. 7 (2): 167–173. PMID 11175846.
  43. ↑ Gupta S, Chattopadhyay T, Pal Singh M; Surolia A (2010). "Supramolecular insulin assembly II for a sustained treatment of type 1 diabetes mellitus.". Proceedings of National Academy of Sciences of the United States of America. 107 (30): 13246–13251. PMID 20628017.
  44. ↑ "Good tidings for diabetes patients". The Hindu. 13 July 2010. Retrieved 27 March 2014.
  45. ↑ "Alternative solution to fight diabetes proposed". The Hindu. 31 January 2012. Retrieved 27 March 2014.
  46. ↑ "Biodata of Prof. A. Surolia". mbu.iisc.ernet.in. MBU. Retrieved 27 March 2014.
  47. ↑ "Avadhesha Surolia". www.twas.org. TWAS. Retrieved 27 March 2014.
  48. ↑ "Member List". www.a-imbn.org. IMBN. Retrieved 27 March 2014.
  49. ↑ "Zone wise list of fellows and honorary fellows" (PDF). www.nasi.org.in. NASI. Retrieved 27 March 2014.
  50. ↑ "India joins elite life sciences group". Deccan Herald. 28 December 2006. Retrieved 27 March 2014.
  51. ↑ "India joins Human Frontier Science Program Organisation". www.docstoc.com. DOCSTOC. Retrieved 27 March 2014.
  52. ↑ "National Representatives". www.intl-glyco.org. Retrieved 27 March 2014.
  53. ↑ "The Members of the IUBMB Executive Committee". www.iubmb.org. IUBMB. Retrieved 27 March 2014.
  54. 1 2 "Awards Recipients". insaindia.org. INSA. Retrieved 27 March 2014.
  55. ↑ "JC Bose Fellows" (PDF). www.serb.gov.in. SERB. Retrieved 27 March 2014.
  56. ↑ "ICMR Awards and Prizes" (PDF). www.icmr.nic.in. ICMR. Retrieved 27 March 2014.
  57. ↑ "Recipients of TWAS Awards/Prizes". twas-old.ictp.it. TWAS. Retrieved 27 March 2014.
  58. ↑ "Shri Om Prakash Bhasin Awards". www.opbfawards.com. Retrieved 27 March 2014.
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