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Location: Home > People > Faculty > Lafontaine ERIC R. LAFONTAINE Dr. Lafontaine's research program consists of identifying and characterizing surface antigens that are expressed by the gram negative bacteria Moraxella catarrhalis, Burkholderia pseudomallei, and Burkholderia mallei, with emphasis on molecules functioning as adherence factors. Our lab's hypothesis is that these molecules, or fragments thereof, are potential vaccine antigens. Furthermore, adherence is an important step in pathogenesis by most infectious agents and we believe that studying this process will shed some light on the means by which the organisms cause disease. M. catarrhalis is a major causative agent of otitis media, sinusitis, as well as respiratory infections in patients with chronic obstructive pulmonary disease. Very little is known about pathogenesis by M. catarrhalis and there is currently no vaccine for this bacterium. B. pseudomallei causes melioidosis whereas B. mallei causes glanders. These two closely related bacteria are potential bioterrorism agents and there is an urgent need to understand their biology as well as develop vaccines. Once identified, adhesins are tested for their vaccinogenic potential (e.g., Do antibodies to these molecules bind to the surface of bacteria, block adherence, and/or have bactericidal activity? Is immunization with the adhesins protective in animal models?). RECENT PUBLICATIONS Lafontaine, E.R., L.D. Cope, C. Aebi, J.L. Latimer, G.H. McCracken JR, and E.J. Hansen. The UspA1 and a second type of UspA2 protein mediate adherence of Moraxella catarrhalis to human epithelial cells in vitro. J. Bacteriol. 182:1364-1373 (2000).
Lafontaine, E.R., N.J. Wagner, and E.J. Hansen. Expression of the Moraxella catarrhalis UspA1 protein undergoes phase variation and is regulated at the transcriptional level. J. Bacteriol. 183: 1540-1551 (2001).
Pearson, M.M., E.R. Lafontaine, N.J. Wagner, J.W. St. Geme III, and E.J. Hansen. A hag mutant of Moraxella catarrhalis strain O35E is deficient in hemagglutination, autoagglutination, and IgD-binding activities. Infect. Immun. 70:4523-4533 (2002).
Timpe, J.M., M. M. Holm, S. L. Vanlerberg, V. Basrur, and E.R. Lafontaine. Identification of a Moraxella catarrhalis outer membrane protein exhibiting both adhesin and lipolytic activities. Infect. Immun. 71: 4341-4350 (2003).
Holm, M.M, S.L. Vanlerberg, D. D. Sledjeski and E.R. Lafontaine. The Hag protein of Moraxella catarrhalis strain O35E is associated with adherence to human lung and middle ear cells. Infect. Immun. 71: 4977-4984 (2003).
Holm, M.M., S.L. Valenberg, I. M. Foley D.D. Sledjeski and E.R. Lafontaine. The Moraxella catarrhalis porin-like outer membrane protein CD is an adhesin for human lung cells. Infect. Immun. 72: 1906-1913 (2004).
Lafontaine, E. R., D. Wall, S. L. Vanlerberg, H. Donabedian and D. D. Sledjeski. Moraxella catarrhalis coaggregates with Streptococcus pyogenes and modulates its interactions with human epithelial cells. Infect. Immun. 72: 6689-6693 (2004)
Attia, A.S, E. R. Lafontaine, J.L Latimer, C. Aebi, G. A. Syrogiannopoulos, and E.J Hansen. The UspA2 protein of Moraxella catarrhalis is directly involved in the expression of serum resistance. Infect. Immun. 73: 2400-2410 (2005).
Bullard, B., S. L. Lipski, and E.R. Lafontaine. Hag directly mediates the adherence of Moraxella catarrhalis to human middle ear cells. Infect Immun 73:5127-36 (2005).
Melillo, A, D. D. Sledjeski, S. Lipski, R. M. Wooten, V. Basrur and E. R. Lafontaine. Identification of a Francisella tularensis LVS outer membrane protein that confers adherence to A549 human lung cells. FEMS Microbiology Letters 263:102-108 (2006).
Lipski, S. L., M. M. Holm, and E. R. Lafontaine. Identification of a Moraxella catarrhalis Gene that Confers Adherence to Various Human Epithelial Cell Lines In Vitro. FEMS Microbiology Letters 267: 207-213 (2007).
Lipski, S. L., C. Akimana, J. M. Timpe, R.M. Wooten, and E. R. Lafontaine. The Moraxella catarrhalis Autotransporter McaP is a Conserved Surface Protein That Mediates Adherence to Human Epithelial Cells through Its N-terminal Passenger Domain. Infect. Immun. 75: 314-324 (2007). |
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