Kamakshi Sureka

@jisiasr.org

Assistant Professor
JIS Institute of Advanced Studies and Research

Kamakshi Sureka

RESEARCH INTERESTS

Host-pathogen interaction, small molecule signaling
16

Scopus Publications

1366

Scholar Citations

11

Scholar h-index

11

Scholar i10-index

Scopus Publications

  • Cyclic dinucleotide signaling in mycobacteria: Roles of c-di-AMP and c-di-GMP in physiology and pathogenesis
    Somashree Mishra, Devshmita Das, Kamakshi Sureka
    Tuberculosis, 2026
  • Exploring the evolutionary divergence of cyclic di-nucleotide signaling in diverse mycobacterial species
    Sayantan Mitra, Sandip Paul, Kamakshi Sureka
    Archives of Microbiology, 2026
  • Enhanced active edge sites on MoSe2 nanostructures for stable electrocatalytic and photocatalytic hydrogen evolution reaction
    A. Gowrisankar, D. Subhashini, K. Sureka, T. Selvaraju
    Ionics, 2024
  • Hierarchical nanostructured functional materials for flexible supercapacitors
    A Gowrisankar, K Sureka, T Selvaraju
    Materials Technology for the Energy and Environmental Nexus, 2023
    In this chapter, we focus specifically on the recent advances in the fabrication of flexible supercapacitor devices and their electrochemical performance as supercapacitor materials. The synthesis approaches for HNFMs are categorized, and the electrochemical capacitive performances of various HNFMs are discussed. Finally, the challenges and the promising future of this particular material are discussed.
  • Spike protein mutational landscape in India during the complete lockdown phase: Could Muller's ratchet be a future game-changer for COVID-19?
    Rachana Banerjee, Kausik Basak, Anamika Ghosh, Vyshakh Rajachandran, Kamakshi Sureka, Debabani Ganguly, Sujay Chattopadhyay
    Infection Genetics and Evolution, 2021
    The dire need of effective preventive measures and treatment approaches against SARS-CoV-2 virus, causing COVID-19 pandemic, calls for an in-depth understanding of its evolutionary dynamics with attention to specific geographic locations, since lockdown and social distancing to prevent the virus spread could lead to distinct localized dynamics of virus evolution within and between countries owing to different environmental and host-specific selection pressures. To decipher any correlation between SARS-CoV-2 evolution and its epidemiology in India, we studied the mutational diversity of spike glycoprotein, the key player for the attachment, fusion and entry of virus to the host cell. For this, we analyzed the sequences of 630 Indian isolates as available in GISAID database till June 07, 2020 (during the time-period before the start of Unlock 1.0 in India on and from June 08, 2020), and detected the spike protein variants to emerge from two major ancestors – Wuhan-Hu-1/2019 and its D614G variant. Average stability of the docked spike protein – host receptor (S-R) complexes for these variants correlated strongly (R2 = 0.96) with the fatality rates across Indian states. However, while more than half of the variants were found unique to India, 67% of all variants showed lower stability of S-R complex than the respective ancestral variants, indicating a possible fitness loss in recently emerged variants, despite a continuous increase in mutation rate. These results conform to the sharply declining fatality rate countrywide (>7-fold during April 11 – June 28, 2020). Altogether, while we propose the potential of S-R complex stability to track disease severity, we urge an immediate need to explore if SARS-CoV-2 is approaching mutational meltdown in India.
  • Cyclic di-AMP targets the cystathionine beta-synthase domain of the osmolyte transporter OpuC
    TuAnh Ngoc Huynh, Philip H. Choi, Kamakshi Sureka, Hannah E. Ledvina, Julian Campillo, Liang Tong, Joshua J. Woodward
    Molecular Microbiology, 2016
    Cellular turgor is of fundamental importance to bacterial growth and survival. Changes in external osmolarity as a consequence of fluctuating environmental conditions and colonization of diverse environments can significantly impact cytoplasmic water content, resulting in cellular lysis or plasmolysis. To ensure maintenance of appropriate cellular turgor, bacteria import ions and small organic osmolytes, deemed compatible solutes, to equilibrate cytoplasmic osmolarity with the extracellular environment. Here, we show that elevated levels of c‐di‐AMP, a ubiquitous second messenger among bacteria, result in significant susceptibility to elevated osmotic stress in the bacterial pathogen Listeria monocytogenes. We found that levels of import of the compatible solute carnitine show an inverse correlation with intracellular c‐di‐AMP content and that c‐di‐AMP directly binds to the CBS domain of the ATPase subunit of the carnitine importer OpuC. Biochemical and structural studies identify conserved residues required for this interaction and transport activity in bacterial cells. Overall, these studies reveal a role for c‐di‐AMP mediated regulation of compatible solute import and provide new insight into the molecular mechanisms by which this essential second messenger impacts bacterial physiology and adaptation to changing environmental conditions.
  • Molecular basis for the recognition of cyclic-di-AMP by PstA, a PII-like signal transduction protein
    Philip H. Choi, Kamakshi Sureka, Joshua J. Woodward, Liang Tong
    Microbiologyopen, 2015
    Cyclic‐di‐AMP (c‐di‐AMP) is a broadly conserved bacterial second messenger that is of importance in bacterial physiology. The molecular receptors mediating the cellular responses to the c‐di‐AMP signal are just beginning to be discovered. PstA is a previously uncharacterized PII‐like protein which has been identified as a c‐di‐AMP receptor. PstA is widely distributed and conserved among Gram‐positive bacteria in the phylum Firmicutes. Here, we report the biochemical, structural, and functional characterization of PstA from Listeria monocytogenes. We have determined the crystal structures of PstA in the c‐di‐AMP‐bound and apo forms at 1.6 and 2.9 Å resolution, respectively, which provide the molecular basis for its specific recognition of c‐di‐AMP. PstA forms a homotrimer structure that has overall similarity to the PII protein family which binds ATP. However, PstA is markedly different from PII proteins in the loop regions, and these structural differences mediate the specific recognition of their respective nucleotide ligand. The residues composing the c‐di‐AMP binding pocket are conserved, suggesting that c‐di‐AMP recognition by PstA is of functional importance. Disruption of pstA in L. monocytogenes affected c‐di‐AMP‐mediated alterations in bacterial growth and lysis. Overall, we have defined the PstA family as a conserved and specific c‐di‐AMP receptor in bacteria.
  • The cyclic dinucleotide c-di-AMP is an allosteric regulator of metabolic enzyme function.
    Kamakshi Sureka, Philip H. Choi, Mimi Precit, Matthieu Delince, Daniel A. Pensinger, TuAnh Ngoc Huynh, Ashley R. Jurado, Young Ah Goo, Martin Sadilek, Anthony T. Iavarone, John-Demian Sauer, Liang Tong, Joshua J. Woodward
    Cell, 2014
    Cyclic di-adenosine monophosphate (c-di-AMP) is a broadly conserved second messenger required for bacterial growth and infection. However, the molecular mechanisms of c-di-AMP signaling are still poorly understood. Using a chemical proteomics screen for c-di-AMP-interacting proteins in the pathogen Listeria monocytogenes, we identified several broadly conserved protein receptors, including the central metabolic enzyme pyruvate carboxylase (LmPC). Biochemical and crystallographic studies of the LmPC-c-di-AMP interaction revealed a previously unrecognized allosteric regulatory site 25 Å from the active site. Mutations in this site disrupted c-di-AMP binding and affected catalytic activity of LmPC as well as PC from pathogenic Enterococcus faecalis. C-di-AMP depletion resulted in altered metabolic activity in L. monocytogenes. Correction of this metabolic imbalance rescued bacterial growth, reduced bacterial lysis, and resulted in enhanced bacterial burdens during infection. These findings greatly expand the c-di-AMP signaling repertoire and reveal a central metabolic regulatory role for a cyclic dinucleotide.
  • Phenotypic heterogeneity in mycobacterial stringent response
    Sayantari Ghosh, Kamakshi Sureka, Bhaswar Ghosh, Indrani Bose, Joyoti Basu, Manikuntala Kundu
    BMC Systems Biology, 2011
    Background A common survival strategy of microorganisms subjected to stress involves the generation of phenotypic heterogeneity in the isogenic microbial population enabling a subset of the population to survive under stress. In a recent study, a mycobacterial population of M. smegmatis was shown to develop phenotypic heterogeneity under nutrient depletion. The observed heterogeneity is in the form of a bimodal distribution of the expression levels of the Green Fluorescent Protein (GFP) as reporter with the gfp fused to the promoter of the rel gene. The stringent response pathway is initiated in the subpopulation with high rel activity. Results In the present study, we characterise quantitatively the single cell promoter activity of the three key genes, namely, mprA, sigE and rel, in the stringent response pathway with gfp as the reporter. The origin of bimodality in the GFP distribution lies in two stable expression states, i.e., bistability. We develop a theoretical model to study the dynamics of the stringent response pathway. The model incorporates a recently proposed mechanism of bistability based on positive feedback and cell growth retardation due to protein synthesis. Based on flow cytometry data, we establish that the distribution of GFP levels in the mycobacterial population at any point of time is a linear superposition of two invariant distributions, one Gaussian and the other lognormal, with only the coefficients in the linear combination depending on time. This allows us to use a binning algorithm and determine the time variation of the mean protein level, the fraction of cells in a subpopulation and also the coefficient of variation, a measure of gene expression noise. Conclusions The results of the theoretical model along with a comprehensive analysis of the flow cytometry data provide definitive evidence for the coexistence of two subpopulations with overlapping protein distributions.
  • An oligopeptide transporter of Mycobacterium tuberculosis regulates cytokine release and apoptosis of infected macrophages
    Arunava Dasgupta, Kamakshi Sureka, Devrani Mitra, Baisakhee Saha, Sourav Sanyal, Amit K. Das, Parul Chakrabarti, Mary Jackson, Brigitte Gicquel, Manikuntala Kundu, Joyoti Basu
    Plos One, 2010
    Background The Mycobacterium tuberculosis genome encodes two peptide transporters encoded by Rv3665c-Rv3662c and Rv1280c-Rv1283c. Both belong to the family of ABC transporters containing two nucleotide-binding subunits, two integral membrane proteins and one substrate-binding polypeptide. However, little is known about their functions in M. tuberculosis. Here we report functional characterization of the Rv1280c-Rv1283c-encoded transporter and its substrate-binding polypeptide OppAMTB. Methodology/Principal Findings OppAMTB was capable of binding the tripeptide glutathione and the nonapeptide bradykinin, indicative of a somewhat broad substrate specificity. Amino acid residues G109, N110, N230, D494 and F496, situated at the interface between domains I and III of OppA, were required for optimal peptide binding. Complementaton of an oppA knockout mutant of M. smegmatis with OppAMTB confirmed the role of this transporter in importing glutathione and the importance of the aforesaid amino acid residues in peptide transport. Interestingly, this transporter regulated the ability of M. tuberculosis to lower glutathione levels in infected compared to uninfected macrophages. This ability was partly offset by inactivation of oppD. Concomitantly, inactivation of oppD was associated with lowered levels of methyl glyoxal in infected macrophages and reduced apoptosis-inducing ability of the mutant. The ability to induce the production of the cytokines IL-1β, IL-6 and TNF-α was also compromised after inactivation of oppD. Conclusions Taken together, these studies uncover the novel observations that this peptide transporter modulates the innate immune response of macrophages infected with M. tuberculosis.
  • RseA, the SigE specific anti-sigma factor of Mycobacterium tuberculosis, is inactivated by phosphorylation-dependent ClpC1P2 proteolysis
    Subhasis Barik, Kamakshi Sureka, Partha Mukherjee, Joyoti Basu, Manikuntala Kundu
    Molecular Microbiology, 2010
  • Novel role of phosphorylation-dependent interaction between FtsZ and FipA in mycobacterial cell division
    Kamakshi Sureka, Tofajjen Hossain, Partha Mukherjee, Paramita Chatterjee, Pratik Datta, Manikuntala Kundu, Joyoti Basu
    Plos One, 2010
  • Polyphosphate kinase 2: A modulator of nucleoside diphosphate kinase activity in mycobacteria
    Kamakshi Sureka, Sourav Sanyal, Joyoti Basu, Manikuntala Kundu
    Molecular Microbiology, 2009
  • Novel role of Wag31 in protection of mycobacteria under oxidative stress
    Partha Mukherjee, Kamakshi Sureka, Pratik Datta, Tofajjen Hossain, Subhasis Barik, Kali P. Das, Manikuntala Kundu, Joyoti Basu
    Molecular Microbiology, 2009
  • Positive feedback and noise activate the stringent response regulator rel in mycobacteria
    Kamakshi Sureka, Bhaswar Ghosh, Arunava Dasgupta, Joyoti Basu, Manikuntala Kundu, Indrani Bose
    Plos One, 2008
  • Polyphosphate kinase is involved in stress-induced mprAB-sigE-rel signalling in mycobacteria
    Kamakshi Sureka, Supratim Dey, Pratik Datta, Anil Kumar Singh, Arunava Dasgupta, Sébastien Rodrigue, Joyoti Basu, Manikuntala Kundu
    Molecular Microbiology, 2007

RECENT SCHOLAR PUBLICATIONS

  • Cyclic Dinucleotide Signalling in Mycobacteria: Roles of c-di-AMP and c-di-GMP in Physiology and Pathogenesis
    S Mishra, D Das, K Sureka
    Tuberculosis, 102764 , 2026
    2026
  • Exploring the evolutionary divergence of cyclic di-nucleotide signaling in diverse mycobacterial species
    S Mitra, S Paul, K Sureka
    Archives of Microbiology 208 (2), 92 , 2026
    2026
    Citations: 1
  • Nested Multiplex Endpoint Polymerase Chain Reaction: An Alternative Method for Human Papilloma Virus Genotyping in Resource-limited Settings
    MC SYMEC Research Group (Kamakshi Sureka, Anusha Harishankar, Sudipto Mandal ...
    Journal of The Academy of Clinical Microbiologists 26 (1) , 2024
    2024
  • Spike protein mutational landscape in India during the complete lockdown phase: Could Muller's ratchet be a future game-changer for COVID-19?
    R Banerjee, K Basak, A Ghosh, V Rajachandran, K Sureka, D Ganguly, ...
    Infection, Genetics and Evolution, 104874 , 2021
    2021
    Citations: 1
  • Cyclic di‐AMP targets the cystathionine beta‐synthase domain of the osmolyte transporter OpuC
    TAN Huynh, PH Choi, K Sureka, HE Ledvina, J Campillo, L Tong, ...
    Molecular Microbiology 102 (2), 233-243 , 2016
    2016
    Citations: 123
  • Molecular basis for the recognition of cyclic‐di‐AMP by PstA, a PII‐like signal transduction protein
    PH Choi, K Sureka, JJ Woodward, L Tong
    Microbiologyopen 4 (3), 361-374 , 2015
    2015
    Citations: 65
  • The Cyclic Dinucleotide c-di-AMP Is an Allosteric Regulator of Metabolic Enzyme Function
    K Sureka, PH Choi, M Precit, M Delince, DA Pensinger, TAN Huynh, ...
    Cell 158 (6), 1389-1401 , 2014
    2014
    Citations: 266
  • Phenotypic heterogeneity in mycobacterial stringent response
    S Ghosh, K Sureka, B Ghosh, I Bose, J Basu, M Kundu
    BMC systems biology 5 (1), 1-13 , 2011
    2011
    Citations: 65
  • An oligopeptide transporter of Mycobacterium tuberculosis regulates cytokine release and apoptosis of infected macrophages
    A Dasgupta, K Sureka, D Mitra, B Saha, S Sanyal, AK Das, P Chakrabarti, ...
    PLoS One 5 (8), e12225 , 2010
    2010
    Citations: 74
  • RseA, the SigE specific anti‐sigma factor of Mycobacterium tuberculosis, is inactivated by phosphorylation‐dependent ClpC1P2 proteolysis
    S Barik, K Sureka, P Mukherjee, J Basu, M Kundu
    Molecular microbiology 75 (3), 592-606 , 2010
    2010
    Citations: 140
  • Novel role of phosphorylation-dependent interaction between FtsZ and FipA in mycobacterial cell division
    K Sureka, T Hossain, P Mukherjee, P Chatterjee, P Datta, M Kundu, ...
    PLOS one 5 (1), e8590 , 2010
    2010
    Citations: 111
  • Polyphosphate kinase 2: a modulator of nucleoside diphosphate kinase activity in mycobacteria
    K Sureka, S Sanyal, J Basu, M Kundu
    Molecular microbiology 74 (5), 1187-1197 , 2009
    2009
    Citations: 79
  • Novel role of Wag31 in protection of mycobacteria under oxidative stress
    P Mukherjee, K Sureka, P Datta, T Hossain, S Barik, KP Das, M Kundu, ...
    Molecular microbiology 73 (1), 103-119 , 2009
    2009
    Citations: 113
  • Positive feedback and noise activate the stringent response regulator rel in mycobacteria
    J Basu, A Dasgupta, I Bose, K Sureka, M Kundu, B Ghosh
    PUBLIC LIBRARY SCIENCE , 2008
    2008
  • Positive feedback and noise activate the stringent response regulator rel in mycobacteria
    K Sureka, B Ghosh, A Dasgupta, J Basu, M Kundu, I Bose
    PLoS One 3 (3), e1771 , 2008
    2008
    Citations: 139
  • Polyphosphate kinase is involved in stress‐induced mprAB‐sigE‐rel signalling in mycobacteria
    K Sureka, S Dey, P Datta, AK Singh, A Dasgupta, S Rodrigue, J Basu, ...
    Molecular microbiology 65 (2), 261-276 , 2007
    2007
    Citations: 189
  • O325 Characterisation of polyphosphate kinase 1 of mycobacteria and its role in persistence
    K Sureka, S Dey, P Datta, A Singh, A Dasgupta, J Basu, M Kundu
    International Journal of Antimicrobial Agents, S67-S68 , 2007
    2007

MOST CITED SCHOLAR PUBLICATIONS

  • The Cyclic Dinucleotide c-di-AMP Is an Allosteric Regulator of Metabolic Enzyme Function
    K Sureka, PH Choi, M Precit, M Delince, DA Pensinger, TAN Huynh, ...
    Cell 158 (6), 1389-1401 , 2014
    2014
    Citations: 266
  • Polyphosphate kinase is involved in stress‐induced mprAB‐sigE‐rel signalling in mycobacteria
    K Sureka, S Dey, P Datta, AK Singh, A Dasgupta, S Rodrigue, J Basu, ...
    Molecular microbiology 65 (2), 261-276 , 2007
    2007
    Citations: 189
  • RseA, the SigE specific anti‐sigma factor of Mycobacterium tuberculosis, is inactivated by phosphorylation‐dependent ClpC1P2 proteolysis
    S Barik, K Sureka, P Mukherjee, J Basu, M Kundu
    Molecular microbiology 75 (3), 592-606 , 2010
    2010
    Citations: 140
  • Positive feedback and noise activate the stringent response regulator rel in mycobacteria
    K Sureka, B Ghosh, A Dasgupta, J Basu, M Kundu, I Bose
    PLoS One 3 (3), e1771 , 2008
    2008
    Citations: 139
  • Cyclic di‐AMP targets the cystathionine beta‐synthase domain of the osmolyte transporter OpuC
    TAN Huynh, PH Choi, K Sureka, HE Ledvina, J Campillo, L Tong, ...
    Molecular Microbiology 102 (2), 233-243 , 2016
    2016
    Citations: 123
  • Novel role of Wag31 in protection of mycobacteria under oxidative stress
    P Mukherjee, K Sureka, P Datta, T Hossain, S Barik, KP Das, M Kundu, ...
    Molecular microbiology 73 (1), 103-119 , 2009
    2009
    Citations: 113
  • Novel role of phosphorylation-dependent interaction between FtsZ and FipA in mycobacterial cell division
    K Sureka, T Hossain, P Mukherjee, P Chatterjee, P Datta, M Kundu, ...
    PLOS one 5 (1), e8590 , 2010
    2010
    Citations: 111
  • Polyphosphate kinase 2: a modulator of nucleoside diphosphate kinase activity in mycobacteria
    K Sureka, S Sanyal, J Basu, M Kundu
    Molecular microbiology 74 (5), 1187-1197 , 2009
    2009
    Citations: 79
  • An oligopeptide transporter of Mycobacterium tuberculosis regulates cytokine release and apoptosis of infected macrophages
    A Dasgupta, K Sureka, D Mitra, B Saha, S Sanyal, AK Das, P Chakrabarti, ...
    PLoS One 5 (8), e12225 , 2010
    2010
    Citations: 74
  • Molecular basis for the recognition of cyclic‐di‐AMP by PstA, a PII‐like signal transduction protein
    PH Choi, K Sureka, JJ Woodward, L Tong
    Microbiologyopen 4 (3), 361-374 , 2015
    2015
    Citations: 65
  • Phenotypic heterogeneity in mycobacterial stringent response
    S Ghosh, K Sureka, B Ghosh, I Bose, J Basu, M Kundu
    BMC systems biology 5 (1), 1-13 , 2011
    2011
    Citations: 65
  • Exploring the evolutionary divergence of cyclic di-nucleotide signaling in diverse mycobacterial species
    S Mitra, S Paul, K Sureka
    Archives of Microbiology 208 (2), 92 , 2026
    2026
    Citations: 1
  • Spike protein mutational landscape in India during the complete lockdown phase: Could Muller's ratchet be a future game-changer for COVID-19?
    R Banerjee, K Basak, A Ghosh, V Rajachandran, K Sureka, D Ganguly, ...
    Infection, Genetics and Evolution, 104874 , 2021
    2021
    Citations: 1
  • Cyclic Dinucleotide Signalling in Mycobacteria: Roles of c-di-AMP and c-di-GMP in Physiology and Pathogenesis
    S Mishra, D Das, K Sureka
    Tuberculosis, 102764 , 2026
    2026
  • Nested Multiplex Endpoint Polymerase Chain Reaction: An Alternative Method for Human Papilloma Virus Genotyping in Resource-limited Settings
    MC SYMEC Research Group (Kamakshi Sureka, Anusha Harishankar, Sudipto Mandal ...
    Journal of The Academy of Clinical Microbiologists 26 (1) , 2024
    2024
  • Positive feedback and noise activate the stringent response regulator rel in mycobacteria
    J Basu, A Dasgupta, I Bose, K Sureka, M Kundu, B Ghosh
    PUBLIC LIBRARY SCIENCE , 2008
    2008
  • O325 Characterisation of polyphosphate kinase 1 of mycobacteria and its role in persistence
    K Sureka, S Dey, P Datta, A Singh, A Dasgupta, J Basu, M Kundu
    International Journal of Antimicrobial Agents, S67-S68 , 2007
    2007