Arockiasamy Arulandu

Group Leader, Membrane Protein Biology
International Centre for Genetic Engineering and Biotechnology
Aruna Asaf Ali Marg
110 067 New Delhi, India
E-mail: sam@icgeb.res.in
Tel: +91-11-26741358 ext. 172
Fax: +91-11-26742316

Education

Madurai Kamarai University, Madurai, India, MSc, 1993
Madurai Kamarai University, Madurai, India, PhD, 2000

Career History

Since 2016, Group Leader, Membrane Protein Biology Group, International Centre for Genetic Engineering and Biotechnology (ICGEB) New Delhi, India
2006-2015, Staff Research Scientist, Structural and Computational Biology Group, ICGEB, New Delhi, India
2003-2006, Assistant Research Scientist, Texas A&M University, Texas, USA
2001-2003, Post-doctoral Research Associate, Texas A&M University
2000-2001, Post-doctoral Research Associate, University of Illinois at Chicago, USA
1994-2000, Junior and Senior Research Fellow (CSIR-NET), Madurai Kamaraj University, Tamil Nadu, India
1993-1994, Junior Research Fellow, Anna University, Chennai, Tamil Nadu, India

Scientific Activity

In Membrane Protein Biology we try to understand a few complex biological processes by basic research, using the tools of modern biology, and attempt to translate them for Atherosclerosis, Cancer and Sepsis therapy. Our research focus is on: 1) Dimorphic and bifunctional Dehydroascorbate reductases (DHARs)-cum-Chloride Intracellular Channels (CLICs) that recycle Vitamin-C as soluble enzymes and act as ion channels while membrane inserted, which are differently expressed in various cancers, 2) oxidized low density lipoprotein (ox-LDL) receptor LOX1 which is responsible for atherosclerosis, 3) plasmid fertility inhibition factors (FINs) that are involved in sexual conflicts among conjugative plasmids, 4) Outer membrane phospholipases (OmpLAs) from Gram negative pathogens that cause sepsis, and 5) Our new initiative is to define the molecular basis of how traditional Indian remedies used for cardio and cerebrovascular therapies work.

Selected publications

Babu, K., Arulandu, A., Sankaran, K. 2017. The structure of DLP12 endolysin exhibiting alternate loop conformation and comparative analysis with other endolysins. Proteins https://doi.org/10.1002/prot.25428

Pothineni, N.V.K., Karathanasis, S. K., Ding, Z., Arulandu, A., Varughese, K.I., Mehta, J.L. 2017. LOX-1 in Atherosclerosis and Myocardial Ischemia. Journal of the American College of Cardiology. https://doi.org/10.1016/j.jacc.2017.04.010

Krishna Das, B., Kumar, A., Maindola, P., Mahanty, S., Jain, S.K., Reddy, M.K., Arockiasamy, A. 2016. Non-native ligands define the active site of Pennisetum glaucum (L.) R. Br dehydroascorbate reductase. Biochemical and Biophysical Research Communications, 473. https://doi.org/10.1016/j.bbrc.2016.04.031

Verma, A., Chandele, A., Nayak, K., Kaja, M.K., Arulandu, A., Lodha, R., Ray, P. 2016. High yield expression and purification of Chikungunya virus E2 recombinant protein and its evaluation for serodiagnosis. Journal of Virological Methods, 235(July), 73–79. https://doi.org/10.1016/j.jviromet.2016.05.003

Maindola, P., Raina, R., Goyal, P., Atmakuri, K., Ojha, A., Gupta, S., Arockiasamy, A. 2014. Multiple enzymatic activities of ParB/Srx superfamily mediate sexual conflict among conjugative plasmids. Nature Communications, 5. https://doi.org/10.1038/ncomms6322

Balasubramaniam, D., Arockiasamy, A., Kumar, P.D., Sharma, A., Krishnaswamy, S. 2012. Asymmetric pore occupancy in crystal structure of OmpF porin from Salmonella typhi. Journal of Structural Biology, 178(3). https://doi.org/10.1016/j.jsb.2012.04.005

Kashyap, M., Jagga, Z., Das, B.K., Arockiasamy, A., Bhavesh, N.S. 2012. 1H, 13C and 15N NMR assignments of inactive form of P1 endolysin Lyz. Biomolecular NMR Assignments, 6(1). https://doi.org/10.1007/s12104-011-9331-4

Arockiasamy, A., Aggarwal, A., Savva, C.G., Holzenburg, A., Sacchettini, J.C. 2011. Crystal structure of calcium dodecin (Rv0379), from mycobacterium tuberculosis with a unique calcium-binding site. Protein Science, 20(5). https://doi.org/10.1002/pro.607

Sun, Q., Kuty, G. F., Arockiasamy, A., Xu, M., Young, R., Sacchettini, J. C. 2009. Regulation of a muralytic enzyme by dynamic membrane topology. Nature Structural and Molecular Biology, 16(11). https://doi.org/10.1038/nsmb.1681

Xu, M., Arulandu, A., Struck, D.K., Swanson, S., Sacchettini, J.C., Young, R. 2005. Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme. Science, 307(5706), 113–117. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/15637279

Arockiasamy, A., Murthy, G.S., Rukmini, M.R., Sundara Baalaji, N., Katpally, U.C., Krishnaswamy, S. 2004. Conformational epitope mapping of OmpC, a major cell surface antigen from Salmonella typhi. Journal of Structural Biology, 148(1). https://doi.org/10.1016/j.jsb.2004.03.011

Arockiasamy, A..Kumar, P.D., Sundara Baalaji, N., Rukmini, M.R., Krishnaswamy, S. 2004. Folding and structural stability of OmpC from Salmonella typhi: Role of LPS and environment. Curr. Sci. 87, 197-202

Sharma, V., Arockiasamy, A., Ronning, D.R., Savva, C.G., Holzenburg, A., Braunstein, M., Sacchettini, J.C. 2003. Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase. Proceedings of the National Academy of Sciences of the United States of America, 100(5). https://doi.org/10.1073/pnas.0538077100

Sujatha, S., Arockiasamy, A., Krishnaswamy, S.,Usha, R. 2001. Molecular modelling of epitope presentation using membrane protein OmpC. Indian J. Biochem. Biophys. 38, 294-297

Arockiasamy, S., Krishnaswamy, S. 2000. Homology model of major surface antigen OmpC from Salmonella typhi and its functional implications. J. Biomol. Struct. Dyn. 18, 261-271

Arockiasamy, A., Krishnaswamy, S. 2000. Purification of integral outermembrane protein OmpC, a surface antigen from Salmonella typhi for structure-function studies; a method applicable to Enterobacterial major outer membrane protein. Anal. Biochem. 283, 64-70

Gnanasekaran, T.V., Suraj Peri, A. Arockiasamy, A.,Krishnaswamy, S. 2000. Profiles from structure based sequence alignment of porins can identify b-stranded membrane proteins. Bioinformatics 16, 839-842

Arockiasamy, A., Krishnaswamy, S. 1999. Crystallization of the immunodominant outer membrane protein OmpC; the first protein crystals from Salmonella typhi, a human pathogen. FEBS Letters, 453(3). https://doi.org/10.1016/S0014-5793(99)00746-2

Arockiasamy, A., Krishnaswamy, S. 1995. Prediction of B-cell epitopes for Salmonella typhi OmpC. Journal of Biosciences, 20(2). https://doi.org/10.1007/BF02703271