Directories

Helen Wing

Associate Professor
School of Life Sciences
Office: 
WHI 314A
Mail Code: 
4004
Phone: 
702-895-5382
Fax: 
702-895-3956

Biography

My team primarily studies the biology and pathogenesis of Shigella flexneri, a gram-negative intracellular bacterial pathogen that causes dysentery in humans. It is estimated that Shigella spp. cause approx. 1 million deaths in the world every year. Symptoms of Shigellosis include fever, stomach cramps and bloody diarrhea. Our research focuses on bacterial proteins that cause this disease, mechanisms of virulence gene expression and the environmental cues encountered in the human host that trigger Shigella virulence gene expression.

In a second, collaborative project, my team is studying antimicrobial peptide resistance in the honey bee pathogen Paenibacillus larvae.

Expertise

Bacterial Pathogenesis, Bacterial Gene Regulation, Antimicrobial Compounds, Bacterial Genetics

Degrees

Ph.D. University of Birmigham, Edgbaston, United Kingdom

Publications

  • Hensley CT, Kamneva OK, Levy KM, Labahn SK, Africa LA, Wing HJ. 2011. Two promoters and two translation start sites control the expression of the Shigella flexneri outer membrane protease IcsP. Arch Microbiol. Jan 12. [Epub ahead of print]
  • Castellanos MI, Harrison DJ, Smith JM, Levy KM, Labahn SK and Wing HJ. 2009. VirB alleviates H-NS repression of the icsP promoter in Shigella flexneri from sites over 1 kb upstream of the transcription start site. J Bacteriol. 191: 4047-4050
  • Wing HJ, Yan AW, Goldman SR and Goldberg MB. 2004. Regulation of IcsP, the outer membrane protease of the Shigella actin tail assembly protein IcsA, by virulence plasmid regulators VirF and VirB. J. Bacteriol. 186: 699-705.
  • Wing HJ, Goldman SR, Ally S, Goldberg MB. 2005. Modulation of an outer membrane protease contributes to the virulence defect of Shigella flexneri strains carrying a mutation in the virK locus. Inf Immun. 73:1217-1220.
  • Lee DJ, Wing HJ, Savery NJ, Busby SJW. 2000. Analysis of interactions between activating region 1 of Escherichia coli FNR protein and the C-terminal domain of the RNA polymerase alpha subunit: use of alanine scanning and suppression genetics. Mol. Microbiol. 37: 1032-1040.
  • Wing HJ, Green J, Guest JR, Busby SJW. 2000. Role of activating region 1 of Escherichia coli FNR protein in transcription activation at class II promoters. J. Biol. Chem. 275: 29061-29065.
  • Williams SM, Wing HJ, Busby SJW. 1998. Repression of transcription initiation by Escherichia coli FNR protein: repression by FNR can be simple. FEMS Microbiol. Letts, 163: 203-208.
  • Li B, Wing HJ, Lee D, Wu HC, Busby SJW. 1998. Transcription activation by Escherichia coli FNR protein: similarities to, and differences from, the CRP paradigm. Nucl. Acid Res. 26: 2075-2081.
  • Williams SM, Savery NJ, Busby SJW, Wing HJ. 1997 Transcription activation at Class I FNR-dependent promoters: identification of the activating surface of FNR and the corresponding contact site in the C-terminal domain of the RNA polymerase alpha subunit. Nucl. Acid Res. 25: 4028-4034.
  • Wing HJ, Williams SM, Busby SJW. 1995. "Spacing requirements for transcription activation by Escherichia coli FNR protein." J. Bacteriol. 177: 6704-6710.
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