Department of Biology and Biochemistry
Office: Houston Science Center, 448
Contact: email@example.com - (713) 743-8377
Education: Ph.D., Université Montpellier II
Google Scholar Profile
Structural Molecular Biology; X-ray Crystallography
Dr. Hye-Jeong Yeo’s research interests center on the structure determination of bacterial virulence factor proteins by X-ray crystallography and functional analysis of these proteins using a combination of biochemical and biophysical methods. Her lab studies proteins involved in bacterial secretion systems and bacterial lipoproteins, as possible vaccine and drug targets against infectious diseases.
One ongoing project is to study three fascinating proteins (HMW1, HMW1B and HMW1C) of the HMW1 adhesin secretion pathway in Haemophilus influenzae, a common cause of localized respiratory tract diseases. Bacterial attachment to the respiratory epithelium plays an important role in infection and is influenced by adhesive proteins called adhesins. The HMW1 adhesin is a key virulence exoprotein secreted via the Two-Partner Secretion pathway. A detailed structural and functional understanding of the HMW1 secretion strategies cooperated with HMW1B (outer membrane protein) and HMW1C (N-glycosyltransferase) should provide insights into one of the major bacterial secretion mechanisms.
Another project is to investigate a variety of novel virulence factor proteins from Campylobacter jejuni, a leading cause of human gastrointestinal infections. Bacterial lipoproteins are universal components of the membranes and have diverse functions. Some of the lipoproteins that are upregulated, once inside the mammalian host, undergo antigenic variations as a strategy of evading the host immune response. Lipoproteins are also involved in disease pathogenesis through their ability to trigger the host inflammatory response. Surface-exposed lipoproteins are often implicated in essential roles in the interaction with mammalian host cells. Yeo seeks to discover novel lipoproteins of C. jejuni and explore their potential as vaccine candidates.
- Pflughoeft KJ, Swick MC, Engler DA, Yeo HJ, Koehler TM (2014). Modulation of the Bacillus anthracis Secretome by the Immune Inhibitor A1 Protease. J Bacteriol. 196, 424-435.
- Paek S, Kawai F, Choi KJ, Yeo HJ (2012). Crystal structure of the Campylobacter jejuni Cj0090 protein reveals a novel variant of the immunoglobulin fold among bacterial lipoproteins. Proteins. 80, 2804-2809.
- Li F, Alvarez-Martinez C, Chen Y, Choi KJ, Yeo HJ, Christie PJ (2012). Enterococcus faecalis PrgJ, a VirB4-like ATPase, mediates pCF10 conjugative transfer through substrate binding. J Bacteriol. 194, 4041-4051.
- Kawai F, Paek S, Choi KJ, Prouty M, Kanipes MI, Guerry P, Yeo HJ (2012). Crystal structure of JlpA, a surface-exposed lipoprotein adhesin of Campylobacter jejuni. J Struct Biol. 177, 583-588.
- Kawai F, Grass S, Kim Y, Choi KJ, St Geme JW III, Yeo HJ (2011). Structural insights into the glycosyltransferase activity of the Actinobacillus pleuropneumoniae HMW1C-like protein. J Biol Chem. 286, 38546-38557.
- Choi KJ, Grass S, Paek SH, St. Geme JW III, Yeo HJ (2010). The Actinobacillus pleuropneumoniae HMW1C-like glycosyltransferase mediates N-linked glycosylation of the Haemophilus influenzae HMW1 adhesin. PLoS ONE. 5, e15888.
- St. Geme JW III, Yeo HJ (2009). A prototype two-partner secretion pathway: The Haemophilus influenzae HMW1 and HMW2 adhesin systems. Trends in Microbiol. 17, 355-360.
- Yokoyama T, Choi K, Bosch AM, Yeo HJ (2009). Structure and Function of a Campylobacter jejuni thioesterase Cj0915, a hexameric Hot Dog fold enzyme. Biochim Biophys Acta. 1794, 1073-1081.
- Kirkpatrick AS, Yokoyama T, Choi K, Yeo HJ (2009). Campylobacter jejuni Fatty Acid Synthase II: structural and functional analysis of -hydroxyacyl-ACP dehydratase (FabZ). Biochem Biophys Res Commun. 380, 407-412.
- Yokoyama T, Paek SH, Ewing, CP, Guerry P, Yeo HJ (2008). Structure of a sigma28-regulated Nonflagellar Virulence Protein from Campylobacter jejuni. J Mol Biol. 384, 364-376.
- Duret G, Szymanski M, Choi K, Yeo HJ, Delcour AH (2008). The TpsB Translocator HMW1B of Haemophilus influenzae Forms a Large-Conductance Channel. J Biol Chem. 283, 15771-15778.
- Chen Y, Zhang X, Manias D, Yeo HJ, Dunny GM, Christie PJ (2008). Enterococcus faecalis PcfC, a Spatially-Localized Substrate Receptor for Type IV Secretion of the pCF10 Transfer Intermediate. J Bacteriol. 190, 3632-3645.
- Yeo HJ, Yokoyama T, Walkiewicz K, Kim Y, Grass S, St Geme JW III (2007). The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretion J Biol Chem. 282, 31076-31084.
- Sexton JA, Yeo HJ, Vogel JP (2005). Genetic analysis of the Legionella pneumophila DotB ATPase reveals a role in type IV secretion system protein export. Mol Microbiol. 57, 70-84.
- Yeo HJ, Cotter S, Laarmann S, St Geme JW III, Waksman G (2004). Structural basis for host recognition by the Haemophilus influenzae Hia autotransporter. EMBO J. 23, 1245-1256.
- Yeo HJ, Waksman G (2004). Unveiling molecular scaffolds of the type IV secretion system. J bacteriol, 186, 1919-1926.
- Yeo HJ, Yuan Q, Beck MR, Baron C, Waksman G (2003). Structural and functional characterization of the VirB5 protein from the type IV secretion system encoded by the conjugative plasmid pKM101. Proc Natl Acad Sci 100, 15947-15952.
- Savvides SN, Yeo HJ, Beck MR, Blaesing F, Lurz R, Lanka E, Buhrdorf R, Fischer W, Haas R, Waksman G (2003). VirB11 ATPases are dynamic hexameric assemblies: new insights into bacterial type IV secretion. EMBO J. 22, 1969-1080.
- Yeo HJ, Zieglin G, Korolev S, Calendar R, Lanka E, Waksman G (2002). Phage P4 origin-binding domain structure reveals a mechanism for regulation of DNA-binding activity by homo- and heterodimerization of winged helix protein. Mol Microbiol. 43, 855-867.
- Yeo HJ, Savvides SN, Herr AB, Lanka E, Waksman G. (2000). Crystal structure of the hexameric traffic ATPase of the Helicobacter pylori type IV secretion system. Mol Cell. 6, 1461-1472.
- Yeo HJ, Larvor MP, Ancelin ML, Vial HJ (1997). Plasmodium falciparum CTP:phosphocholine cytidylyltransferase expressed in E. coli : purification, characterization and lipid regulation. Biochem J. 342, 303-310.
- Yeo HJ, Sri Widada J, Mercereau-Puijalon O, Vial HJ (1995). Molecular Cloning of CTP:Phosphocholine Cytidylyltransferase from Plasmodium falciparum. Eur J Biochem. 233, 62-72.
Organizations, Outreach, Boards, Memberships:
American Association for the Advancement of Science
American Chemical Society
American Crystallographic Association
Houston Area Molecular Biophysics Program