SUNIL KUMAR TEWARY

Post Doc at University of Kansas

ab9yk9@r.postjobfree.com

Summary

Scientific

Experience

Post Doc Research Scientist at University of Kansas

April 2011 - Present (2 years 7 months)

Currently working on the structural details of assembly and packaging of parvo virus and herpesvirus

(KSHV). I am also working on understanding the genome packaging mechanism of the Sf6 bacteriophage

using the X-ray crystallography technique.

PhD. at National University of Singapore

August 2006 - December 2010 (4 years 5 months)

PhD. in X-ray fiber diffraction from National University of Singapore (2006-2010).

Topic: Structure determination of Hibiscus latent Singapore virus by fiber diffraction

Abstract:

Hibiscus latent Singapore virus (HLSV) is a new member of the Tobamovirus family. The HLSV genome

contains a unique poly(A) tract in its 3'-UTR which is absent in other Tobamoviruses. The virion is composed

of a monomeric coat protein (CP) of 18 kDa. We have determined the HLSV structure at 3.5 A by X-ray fiber

diffraction with R factor of 0.096. The structure of HLSV CP resembles that of other Tobamoviruses, with a

few unique differences. In other Tobamoviruse structure, CP sequence at position 122 contains a conserved

Arg residue, while the HLSV and SHMV contain His residue. Also, His122 is followed by another positively

charged amino acid residue Lys which is uncharged residue in other Tobamoviruses. There is a kink observed

for the first time in the LR helix of HLSV due to the presence of the unique His122, which produces a bend in

the helix in the non-Pro non-Gly bends. Also, the adjacent Lys123 may destabilize the helix by positive

charge repulsion, making the kink more pronounced. In the HLSV structure, we are able to see Lys123

stabilizing the phosphate 1, hence balancing the protein-nucleic acid interactions. Another residue Arg92

from the Subunit -17 is believed to be involved in stabilizing the remaining phosphate 2 and phosphate 3.

Arg122 is believed to regulate the guanine 1 recognition during assembly for all other existing structures of

the Tobamovirus. Uniquely, His122 at this position showed a very strong salt bridge with the neighboring

Asp88 from subunit -1, hence significantly stabilizing the loop adjacent to RR helix. The

carboxyl-carboxylate interactions that drive viral disassembly are also seem to be different in HLSV. The

nucleotide recognition mechanism for virus assembly is similar between HLSV and RMV but different from

that of TMV and CGMMV.

Research Assistant at National University of Singapore

August 2010 - November 2010 (4 months)

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Worked as research assistant in Dept of Biological Scineces in the Lab of Dr. K. Swaminathan a famous

protein X-ray crystallographer. Worked on several projects and involved in maintaining the lab and training

the undergrad students.

Volunteer Experience

Structure biology research at The University of Kansas

Projects

Crystal structure determination of HBoV NS1 N-terminal nuclease domain

January 2012 to Present

Members:SUNIL KUMAR TEWARY, Liang Tang

We are the first to solve the structure of Parvovirus called human bocavirus (HBoV) which infects the host

without any helper virus infection such as adeno associated virus (AAV). HBoV belongs to genus Bocavirus

of the family Parvoviridae. This work is very significant because we have found a subdomain in the structure

which is highly negatively charged surface and is completely novel and is missing in the AAV.

Structure determination of Hibiscus latent Singapore virus by Fiber diffraction

June 2007 to Present

Members:SUNIL KUMAR TEWARY, Sek-Man Wong, Kunchitpadam Swaminathan, Gerald Stubbs

This structure shows the significant bend in the RNA binding helix when compared to other Tobamoviruses.

In vitro characterization of the B19V origin of replication DNA interaction with the non-structural

protein 1.

January 2012 to Present

Members:SUNIL KUMAR TEWARY, Liang Tang

Honors and Awards

SBPR travel grant for NUS-Vanderbilt University, USA, collaboration work from Dept. of Biological

Sciences, NUS, Singapore

Structure biology and proteomics lab, Singapore

July 2008

Graduate Aptitude Test in Engineering (GATE)

Indian Institute of Technology, India

March 2004

All india rank 44 (99.08 precentile)

Indian Council of Medical Research (ICMR)

ICMR, India

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January 2004

Junior Research Fellowship (JRF) for pursuing PhD. in India

National Eligibility Test

CSIR, India

June 2003

Eligibility for the Lectureship/Professorship

Poster presentation won prize

NUS, Singapore

December 2008

Poster presentation at Biological Science Graduate Congress, National Univ., of Singapore, 15-17 Dec,2008,

Singapore

Publications

Structure of hibiscus latent Singapore virus by fiber diffraction: a non-conserved His122 contributes to

coat protein stability

Journal of Molecular Biology February 25, 2011

Authors: SUNIL KUMAR TEWARY, Sek-Man Wong, K Swaminathan and Gerald Stubbs

Sunil Kumar Tewary, Toshiro Oda, Amy Kendall, Wen Bian, Gerald Stubbs, Sek-Man Wong and

Kunchithapadam Swaminathan

Abstract:Hibiscus latent Singapore virus (HLSV) is a rigid rod-shaped plant virus and a new member of the

Tobamovirus family. Unlike all other Tobamoviruses, the HLSV genome contains a unique poly(A) tract in

its 3# untranslated region. The virion is composed of a monomeric coat protein (CP) unit of 18 kDa, arranged

as a right-handed helix around the virus axis. We have determined the structure of HLSV at 3.5 Å by X-ray

fiber diffraction and refined it to an R-factor of 0.096. While the overall structure of the HLSV CP resembles

that of other Tobamoviruses, there are a few unique differences. There is a kink in the LR helix due to the

presence of His122. Also, the adjacent Lys123 may further destabilize the helix by positive charge repulsion,

making the kink more pronounced. The His122-Asp88 salt bridge provides significant stability to the loop

adjacent to the RR helix. Carboxyl–carboxylate interactions that drive viral disassembly are also different in

HLSV. The nucleotide recognition mechanisms for virus assembly between HLSV and ribgrass mosaic virus

are similar, but different between tobacco mosaic virus and cucumber green mottle mosaic virus.

Structure of the NS1 protein N-terminal origin-recognition/nickase domain from the emerging human

bocavirus

Journal of Virology August 21, 2013

Authors: SUNIL KUMAR TEWARY, Haiyan Zhao, Liang Tang, Weiran Shen, Jianming Qiu

Sunil Kumar Tewary,Haiyan Zhao, Weiran Shen, Jianming Qiu and Liang Tang

Abstract:Human bocavirus is a newly identified, globally prevalent, parvovirus that is associated with

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respiratory infection in infant and young children. Parvoviruses encode a large non-structural protein 1 (NS1)

that is essential for replication of the viral single-stranded DNA genome and DNA packaging and may play

versatile roles in virus:host interaction. Here we report the structure of the human parvovirus NS1 N-terminal

domain, the first for any autonomous parvovirus. The structure shows an overall fold that is canonical to the

histidine-hydrophobic-histidine superfamily of nucleases, which integrates two distinct DNA-binding sites: a

positively charged region mediated by a surface hairpin (residues 190-198) that is responsible for recognition

of the viral origin of replication of the double-stranded DNA nature; and the nickase active site that binds to

the single-stranded DNA substrate for site-specific cleavage. The structure reveals an acidic-residue-rich

sub-domain that is present in bocavirus NS1 proteins but not in the NS1 orthologs in erythrovirus or

dependovirus, which may mediate bocavirus-specific interaction with DNA or potential host factors. These

results provide insights into recognition of the origin of replication and nicking of DNA during bocavirus

genome replication. Mapping of variable amino acid residues of NS1s from four HBoV species onto the

structure shows a scattered pattern, but the origin-recognition site and the nuclease active site are invariable,

suggesting potential targets for antivirals against this clade of highly diverse human viruses.

Test Scores

National Univ of Singapore course work

April 2011 Score:4.10/5 (A)

M.Tech (IIT, Kharagpur) course work

June 2006 Score:8.63/10 (A)

M.Sc Biotechnology course work

June 2004 Score:71%

Courses

Masters of Science, Biotechnology

University of Calicut

Cell biology MBY101

Chemistry of biomolecules MBY102

Microbiology MBY103

Cell biology practical MBY104

Chemistry of biomolecules practical MBY105

Microbiology practicle MBY106

Biophyscics biostatistics & bioinformatics MBY201

Cellular biochemistry & enzymology MBY201

IPR MBY203

Molecular biology & genetics MBY204

Cellular biochemistry & enzymology practicle MBY205

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Molecular biology & molecular genetics practicle MBY206

Bioprocess technology MBY301

RDT MBY302

Immunology & immuno technology MBY303

Tissue culture technology MBY304

Bioprocess technology practical MBY305

RDT practical MBY306

Immunology & immuno tech practical MBY307

Tissue culture tech practical MBY308

Project work MBY401

Genetic engg. in plants MBY402

Recent advances in biotechnology MBY403

Practical- Genetic engg. in plants MBY404

M.Tech., Biotechnology & Biochemical Engg.

Indian Institute of Technology, Kharagpur

New separation process in biotechnology BT60001

Immunotechnology BT60003

Aspects of biochemical engineering BT60011

Secondary metabolism in plants & microbes BT60015

Seminar-I BT69001

Cell culture & hybridoma tech. lab BT69003

New separation process laboratory BT69005

Statistical technique & computer programming MA60061

Recombinant DNA technology BT60002

Biotechnology of plant metabolites BT60004

Bioprocess plant & equipment design BT60012

Protein engineering BT61030

Comprehensive viva voce BT68002

Seminar-II BT60002

Plant biotechnology laboratory BT69012

Genetic engg. & strain improvement lab BT69014

Industrial relations HS60004

Project-I BT67001

Project-II BT67002

PhD.

National University of Singapore

Structural Biology & proteomics BL5210

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Current trends in Biotechnology BL5204

Graduate seminar module in biological sciences BL5198

Macromolecular X-ray crystallography BL5215

Special topics in biological sciences:bioimaging BL5224

Stem cell biology GS6003

Languages

English (Full professional proficiency)

Hindi (Native or bilingual proficiency)

Bhojpuri (Native or bilingual proficiency)

Skills & Expertise

Protein Chemistry

Cell Biology

SDS-PAGE

Research

Cell Culture

Protein Purification

Matlab

Fluorescence Microscopy

Confocal Microscopy

X-ray crystallography

Teaching

Molecular Biology

Biochemistry

Protein Expression

RT-PCR

Biotechnology

Western Blotting

Molecular Cloning

Immunology

Vaccines

Transfection

PCR

Bioinformatics

Electrophoresis

recombinant DNA technology

Cancer

Purification

Proteomics

Cell

Microscopy

Site-directed Mutagenesis

DNA

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Flow Cytometry

ELISA

Education

Indian Institute of Technology, Kharagpur

M.Tech., Biotechnology & Biochemical Engg., 2004 - 2006

Grade: A

University of Calicut

Masters of Science, Biotechnology, 2002 - 2004

Grade: A

Interests

I am interested in understanding the structure and function of proteins and structural details of

packaging and assembly of viruses using the methods of macromolecular X-ray crystallography. I am also

interested in structure based drug design against pathogens that cause disease in humans. My long-term goal is

to extend research to diseases like cancer, AIDS, Alzheimer etc.

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SUNIL KUMAR TEWARY

Post Doc at University of Kansas

ab9yk9@r.postjobfree.com

Contact SUNIL KUMAR on LinkedIn

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