Keehwan Kwon, PhD

Assistant Professor


301-795-7647

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Bio

Keehwan Kwon, Ph.D. is an assistant professor at the J. Craig Venter Institute working in the Infectious Diseases group. Dr. Keehwan Kwon received his B.S. degree from Korea University in Seoul, Korea and Ph.D. degree from the University of Maryland Baltimore County. He worked as a postdoctoral fellow at the Department of Pharmacology and Molecular Sciences, School of Medicine, Johns Hopkins University from 2001 to 2004. Over the past 13 years, he has directed proteomics research projects in the Pathogen Functional Genomics Resource Center (PFGRC) and cloning and protein expression projects in the Center for Structural Genomics of Infectious Disease (CSGID) at JCVI. He currently directs a multivalent human rhinovirus vaccine development. He has been involved in ‘multi-omics’ systems biology studies using microbiome profiling, cytokine profiling, and mass spectrometry-based proteomics to understand the interactions of gut microbiota, pathogens and human immune responses. He has extensive experience in bioanalytical chemistry and instrumentation used for protein analysis using mass spectrometry, spectroscopy, and imaging technologies.

Research Priorities

Vaccine development for human infectious diseases

  • Multivalent vaccine development for human rhinoviruses
  • Emphasis on screening of protein vaccine candidates S. pneumoniae

Applications of large scale cloning and protein production platforms

  • Characterization of inter- and intra-cellular protein-protein interactions
  • Screen antigenic proteins in pathogens

Depth assessment of inflammatory responses related diseases

  • Profiling of cytokines and chemokines released from selected model diseases
  • Correlation of the profiling of inflammatory factors and health problems including infectious diseases

Development of new methods and technology

  • High through assays to increase efficiency and numbers of combinations to determine protein-protein and protein-DNA interactions.

Patents

Assays for identification of topoisomerase inhibitors (Pat. No. US20080020973; WO2006015369)

New ligation independent cloning vectors for expression of recombinant proteins with a self-cleaving CPD/6xHis-tag.
BMC biotechnology. 2017-01-05; 17.1: 1.
PMID: 28056928
Characterization of Early-Phase Neutrophil Extracellular Traps in Urinary Tract Infections.
PLoS pathogens. 2017-01-01; 13.1: e1006151.
PMID: 28129394
Fluorescence-based thermal shift data on multidrug regulator AcrR from Salmonella enterica subsp. entrica serovar Typhimurium str. LT2.
Data in brief. 2016-06-01; 7.537-9.
PMID: 27054155
Loop-to-helix transition in the structure of multidrug regulator AcrR at the entrance of the drug-binding cavity.
Journal of structural biology. 2016-04-01; 194.1: 18-28.
PMID: 26796657
Using host-pathogen protein interactions to identify and characterize Francisella tularensis virulence factors.
BMC genomics. 2015-12-29; 16.1106.
PMID: 26714771
Mining host-pathogen protein interactions to characterize Burkholderia mallei infectivity mechanisms.
PLoS computational biology. 2015-03-01; 11.3: e1004088.
PMID: 25738731
Urine sample preparation in 96-well filter plates for quantitative clinical proteomics.
Analytical chemistry. 2014-06-03; 86.11: 5470-7.
PMID: 24797144
A structurally distinct human mycoplasma protein that generically blocks antigen-antibody union.
Science (New York, N.Y.). 2014-02-07; 343.6171: 656-661.
PMID: 24503852
Expression and solubility testing in a high-throughput environment.
Methods in molecular biology (Clifton, N.J.). 2014-01-01; 1140.75-88.
PMID: 24590710
High-throughput cloning for biophysical applications.
Methods in molecular biology (Clifton, N.J.). 2014-01-01; 1140.61-74.
PMID: 24590709
Novel Burkholderia mallei virulence factors linked to specific host-pathogen protein interactions.
Molecular & cellular proteomics : MCP. 2013-11-01; 12.11: 3036-51.
PMID: 23800426
Structural characterization and comparison of three acyl-carrier-protein synthases from pathogenic bacteria.
Acta crystallographica. Section D, Biological crystallography. 2012-10-01; 68.Pt 10: 1359-70.
PMID: 22993090
Structural and functional characterization of microcin C resistance peptidase MccF from Bacillus anthracis.
Journal of molecular biology. 2012-07-20; 420.4-5: 366-83.
PMID: 22516613
The HaloTag: Improving Soluble Expression and Applications in Protein Functional Analysis.
Current chemical genomics. 2012-01-01; 6.8-17.
PMID: 23115610
Recombinant expression and functional analysis of proteases from Streptococcus pneumoniae, Bacillus anthracis, and Yersinia pestis.
BMC biochemistry. 2011-05-05; 12.17.
PMID: 21545736
High quality protein microarray using in situ protein purification.
BMC biotechnology. 2009-08-23; 9.72.
PMID: 19698181
A correlation analysis of protein characteristics associated with genome-wide high throughput expression and solubility of Streptococcus pneumoniae proteins.
Protein expression and purification. 2007-10-01; 55.2: 368-78.
PMID: 17703947
Catalytic phosphoryl interactions of topoisomerase IB.
Biochemistry. 2005-08-30; 44.34: 11476-85.
PMID: 16114884
Ribonuclease activity of vaccinia DNA topoisomerase IB: kinetic and high-throughput inhibition studies using a robust continuous fluorescence assay.
Biochemistry. 2004-11-30; 43.47: 14994-5004.
PMID: 15554707
Solution structure and base perturbation studies reveal a novel mode of alkylated base recognition by 3-methyladenine DNA glycosylase I.
The Journal of biological chemistry. 2003-11-28; 278.48: 48012-20.
PMID: 13129925
A novel zinc snap motif conveys structural stability to 3-methyladenine DNA glycosylase I.
The Journal of biological chemistry. 2003-05-23; 278.21: 19442-6.
PMID: 12654914
Rational engineering of a DNA glycosylase specific for an unnatural cytosine:pyrene base pair.
Chemistry & biology. 2003-04-01; 10.4: 351-9.
PMID: 12725863
3-Methyladenine DNA glycosylase I is an unexpected helix-hairpin-helix superfamily member.
Nature structural biology. 2002-09-01; 9.9: 659-64.
PMID: 12161745
Binding specificity and the ligand dissociation process in the E. coli biotin holoenzyme synthetase.
Protein science : a publication of the Protein Society. 2002-03-01; 11.3: 558-70.
PMID: 11847279
Fluorescence spectroscopy studies of vaccinia type IB DNA topoisomerase. Closing of the enzyme clamp is faster than DNA cleavage.
The Journal of biological chemistry. 2002-01-04; 277.1: 345-52.
PMID: 11689572
19F NMR studies of vaccinia type IB topoisomerase. Conformational dynamics of the bound DNA substrate.
The Journal of biological chemistry. 2002-01-04; 277.1: 353-8.
PMID: 11689573
Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor.
Protein science : a publication of the Protein Society. 2001-12-01; 10.12: 2618-22.
PMID: 11714930
Turning On uracil-DNA glycosylase using a pyrene nucleotide switch.
The Journal of biological chemistry. 2001-11-09; 276.45: 42347-54.
PMID: 11551943
Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator.
Proceedings of the National Academy of Sciences of the United States of America. 2001-05-22; 98.11: 6045-50.
PMID: 11353844
Multiple disordered loops function in corepressor-induced dimerization of the biotin repressor.
Journal of molecular biology. 2000-12-15; 304.5: 821-33.
PMID: 11124029
Function of a conserved sequence motif in biotin holoenzyme synthetases.
Protein science : a publication of the Protein Society. 2000-08-01; 9.8: 1530-9.
PMID: 10975574