Sushil Kumar - ICGEB  - ICGEB

Sushil Kumar

ICGEB

ICGEB

New Delhi, Delhi | India

Additional Specialties: RGP

Sushil Kumar - ICGEB  - ICGEB

Sushil Kumar

Introduction

Primary Affiliation: ICGEB - New Delhi, Delhi , India

Additional Specialties:

Research Interests:

Publications

9Publications

79Reads

636Profile Views

14PubMed Central Citations

Host ICAMs play a role in cell invasion by Mycobacterium tuberculosis and Plasmodium falciparum.

Nat Commun 2015 Jan 14;6:6049. Epub 2015 Jan 14.

Recombinant Gene Products Group, International Centre for Genetic Engineering and Biotechnology, ICGEB, Aruna Asaf Ali Marg, New Delhi 110067, India.

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http://dx.doi.org/10.1038/ncomms7049DOI Listing
January 2015
15 Reads
6 Citations
10.742 Impact Factor

A novel peptide interferes with Mycobacterium tuberculosis virulence and survival.

FEBS Open Bio 2014 7;4:735-40. Epub 2014 Aug 7.

Recombinant Gene Products Group, International Centre for Genetic Engineering and Biotechnology, ICGEB, Aruna Asaf Ali Marg, New Delhi 110067, India.

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http://dx.doi.org/10.1016/j.fob.2014.08.001DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4208091PMC
October 2014
14 Reads
1 Citation

Europium nanoparticle-based high performing immunoassay for the screening of treponemal antibodies.

PLoS One 2013 26;8(12):e84050. Epub 2013 Dec 26.

Department of Biotechnology, University of Turku, Turku, Finland.

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http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0084050PLOS
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3873409PMC
August 2014
3 Reads
1 Citation
3.234 Impact Factor

Expression of the ARPC4 subunit of human Arp2/3 severely affects mycobacterium tuberculosis growth and suppresses immunogenic response in murine macrophages.

PLoS One 2013 22;8(7):e69949. Epub 2013 Jul 22.

Recombinant Gene Products Group, International Centre for Genetic Engineering and Biotechnology, ICGEB Campus, Aruna Asaf Ali Marg, New Delhi, India.

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http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0069949PLOS
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3718739PMC
February 2014
12 Reads
3 Citations
3.234 Impact Factor

Escherichia coli-expressed near full length HIV-1 envelope glycoprotein is a highly sensitive and specific diagnostic antigen.

BMC Infect Dis 2012 Nov 27;12:325. Epub 2012 Nov 27.

Department of Biotechnology, University of Turku, 20520 Turku, Finland.

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http://dx.doi.org/10.1186/1471-2334-12-325DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3519745PMC
November 2012
6 Reads
1 Citation
2.613 Impact Factor

A three-hybrid system to probe in vivo protein-protein interactions: application to the essential proteins of the RD1 complex of M. tuberculosis.

6(11):e27503

PLoS ONE

Protein-protein interactions play a crucial role in enabling a pathogen to survive within a host. In many cases the interactions involve a complex of proteins rather than just two given proteins. This is especially true for pathogens like M. tuberculosis that are able to successfully survive the inhospitable environment of the macrophage. Studying such interactions in detail may help in developing small molecules that either disrupt or augment the interactions. Here, we describe the development of an E. coli based bacterial three-hybrid system that can be used effectively to study ternary protein complexes. The protein-protein interactions involved in M. tuberculosis pathogenesis have been used as a model for the validation of the three-hybrid system. Using the M. tuberculosis RD1 encoded proteins CFP10, ESAT6 and Rv3871 for our proof-of-concept studies, we show that the interaction between the proteins CFP10 and Rv3871 is strengthened and stabilized in the presence of ESAT6, the known heterodimeric partner of CFP10. Isolating peptide candidates that can disrupt crucial protein-protein interactions is another application that the system offers. We demonstrate this by using CFP10 protein as a disruptor of a previously established interaction between ESAT6 and a small peptide HCL1; at the same time we also show that CFP10 is not able to disrupt the strong interaction between ESAT6 and another peptide SL3. The validation of the three-hybrid system paves the way for finding new peptides that are stronger binders of ESAT6 compared even to its natural partner CFP10. Additionally, we believe that the system offers an opportunity to study tri-protein complexes and also perform a screening of protein/peptide binders to known interacting proteins so as to elucidate novel tri-protein complexes.

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January 2011
3 Reads

Phenylalanine-rich peptides potently bind ESAT6, a virulence determinant of Mycobacterium tuberculosis, and concurrently affect the pathogen's growth.

4(11):e7615

PLoS ONE

ABSTRACT: The secretory proteins of Mycobacterium tuberculosis (M. tuberculosis) have been known to be involved in the virulence, pathogenesis as well as proliferation of the pathogen. Among this set, many proteins have been hypothesized to play a critical role at the genesis of the onset of infection, the primary site of which is invariably the human lung. During our efforts to isolate potential binding partners of key secretory proteins of M. tuberculosis from a human lung protein library, we isolated peptides that strongly bound the virulence determinant protein Esat6. All peptides were less than fifty amino acids in length and the binding was confirmed by in vivo as well as in vitro studies. Curiously, we found all three binders to be unusually rich in phenylalanine, with one of the three peptides a short fragment of the human cytochrome c oxidase-3 (Cox-3). The most accessible of the three binders, named Hcl1, was shown also to bind to the Mycobacterium smegmatis (M. smegmatis) Esat6 homologue. Expression of hcl1 in M. tuberculosis H37Rv led to considerable reduction in growth. Microarray analysis showed that Hcl1 affects a host of key cellular pathways in M. tuberculosis. In a macrophage infection model, the sets expressing hcl1 were shown to clear off M. tuberculosis in much greater numbers than those infected macrophages wherein the M. tuberculosis was not expressing the peptide. Transmission electron microscopy studies of hcl1 expressing M. tuberculosis showed prominent expulsion of cellular material into the matrix, hinting at cell wall damage. While the debilitating effects of Hcl1 on M. tuberculosis are unrelated and not because of the peptide's binding to Esat6-as the latter is not an essential protein of M. tuberculosis-nonetheless, further studies with this peptide, as well as a closer inspection of the microarray data may shed important light on the suitability of such small phenylalanine-rich peptides as potential drug-like molecules against this pathogen.

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January 2009
7 Reads

Hydrogen and polyhydroxybutyrate producing abilities of microbes from diverse habitats by dark fermentative process.

99(13):5444-51

Bioresource Technology

ABSTRACT: Thirty five bacterial isolates from diverse environmental sources such as contaminated food, nitrogen rich soil, activated sludges from pesticide and oil refineries effluent treatment plants were found to belong to Bacillus, Bordetella, Enterobacter, Proteus, and Pseudomonas sp. on the basis of 16S rRNA gene sequence analysis. Under dark fermentative conditions, maximum hydrogen (H(2)) yields (mol/mol of glucose added) were recorded to be 0.68 with Enterobacter aerogenes EGU16 followed by 0.63 with Bacillus cereus EGU43 and Bacillus thuringiensis EGU45. H(2) constituted 63-69% of the total biogas evolved. Out of these 35 microbes, 18 isolates had the ability to produce polyhydroxybutyrate (PHB), which varied up to 500 mg/l of medium, equivalent to a yield of 66.6%. The highest PHB yield was recorded with B. cereus strain EGU3. Nine strains had high hydrolytic activities (zone of hydrolysis): lipase (34-38 mm) -Bacillus sphaericus strains EGU385, EGU399 and EGU542; protease (56-62 mm) -Bacillus sp. strains EGU444, EGU447 and EGU445; amylase (23 mm) -B. thuringiensis EGU378, marine bacterium strain EGU409 and Pseudomonas sp. strain EGU448. These strains with high hydrolytic activities had relatively low H(2) producing abilities in the range of 0.26-0.42 mol/mol of glucose added and only B. thuringiensis strain EGU378 had the ability to produce PHB. This is the first report among the non-photosynthetic microbes, where the same organism(s) -B. cereus strain EGU43 and B. thuringiensis strain EGU45, have been shown to produce H(2) - 0.63 mol/mol of glucose added and PHB - 420-435 mg/l medium.

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October 2008
10 Reads

Top co-authors

Prem Prakash
Prem Prakash

CSIR-Central Drug Research Institute

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Sultan Tousif
Sultan Tousif

National Institute of Malaria Research

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Gobardhan Das
Gobardhan Das

Robert Wood Johnson Medical School

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Anand Ranganathan
Anand Ranganathan

Recombinant Gene Products Group

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Sachin Kumar Samuchiwal
Sachin Kumar Samuchiwal

Recombinant Gene Products Group

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Anamika Ghosh
Anamika Ghosh

Recombinant Gene Products Group

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Kim Pettersson
Kim Pettersson

University of Turku

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