Joseph W. St. Geme, III, MD

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Professor of Pediatrics
Department: Pediatrics
Graduate Group Affiliations

Contact information
The Children’s Hospital of Philadelphia
Physician-in-Chief Suite, Room 9NW67
34th St. and Civic Center Blvd.

1205D Abramson Research Center
3615 Civic Center Blvd.
Philadelphia, PA 19104-4399
Office: 215-590-2766
Lab: 267-426-8374
Stanford University, Stanford, CA, 1979.
M.D. (Medicine)
Harvard Medical School, Boston, MA, 1984.
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Description of Research Expertise

The St. Geme laboratory is interested in understanding the molecular and cellular determinants of bacterial pathogenicity, with a particular focus on Haemophilus influenzae and Kingella kingae. H. influenzae is a common commensal in the nasopharynx and represents the leading cause of otitis media and sinusitis in children and exacerbations of chronic obstructive pulmonary disease in adults. K. kingae is a common commensal in the posterior pharynx and has emerged as a major cause of bone and joint infections in young children. We are using a combination of genetic methods, protein chemistry, X-ray crystallography, high-resolution microscopy, and animal models to study H. influenzae and K. kingae as model mucosal pathogens, aiming to understand how these organisms: 1) initiate infection; 2) establish a state of commensalism; and 3) transition from a state of commensalism to produce disease.

Selected Publications

Dawid S, Barenkamp SJ, St. Geme JWIII: Variation in expression of the Haemophilus influenzae HMW adhesins: a prokaryotic system reminiscent of eukaryotes. Proceedings of the National Academy of Sciences, USA 96: 1077-1082, 1999.

Laarmann S, Cutter D, Juehne T, Barenkamp SJ, St. Geme JWIII: The Haemophilus influenzae Hia autotransporter harbors two adhesive pockets that reside in the passenger domain and recognize the same host cell receptor. Molecular Microbiology 46: 731-743, 2002.

Surana NK, Grass S, Hardy GG, Li H, Thanassi DG, St. Geme JWIII: Evidence for conserved architecture and physical properties of Omp85-like proteins throughout evolution. Proceedings of the National Academy of Sciences USA 101: 14497-14502, 2004.

Yeo H-J, Cotter SE, Laarmann S, Juehne T, St. Geme JWIII, Waksman G: Structural basis for host recognition by the Haemophilus influenzae Hia autotransporter. EMBO Journal 23: 1245-1256, 2004.

Meng G, Surana NK, St. Geme JWIII, Waksman G: Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter. EMBO Journal 25: 2297-2304, 2006.

Yeo H-J, Yokoyama T, Walkiewicz K, Kim Y, Grass S, St. Geme JWIII: The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain that is essential for bacterial two-partner secretion. Journal of Biological Chemistry 42: 31076-31084, 2007.

Gross J, Grass S, Davis AE, Gilmore-P, Townsend RR, St. Geme JWIII: The Haemophilus influenzae HMW1 adhesin is a glycoprotein with an unusual N-linked carbohydrate modification. Journal of Biological Chemistry 283: 26010-26015, 2008.

Grass S, Lichti C, Townsend RR, Gross J, St. Geme JWIII: The Haemophilus HMW1C protein is a glycosyltransferase that transfers hexose residues to asparagine sites in the HMW1 adhesin. PLoS Pathogens 6: e1000919, 2010.

Meng G, Spahich N, Kenjale R, Waksman G, St. Geme JWIII: Crystal structure of the Haemophilus influenzae Hap adhesin reveals an intercellular oligomerization mechanism for bacterial aggregation. EMBO Journal 30: 3864-3874, 2011

Porsch EA, Kehl-Fie TE, St. Geme JWIII: Modulation of Kingella kingae adherence to human epithelial cells by type IV pili, capsule, and a novel trimeric autotransporter. mBio 3(5): 00372, 2012.

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Last updated: 04/19/2018
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