Structural and Functional Analysis of Moraxella catarrhalis Adhesins MCAP and OMPCD

 
 
 
 

Structural and Functional Analysis of Moraxella catarrhalis Adhesins MCAP and OMPCD

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dc.contributor.advisor Lafontaine, Eric en_US
dc.contributor.author Akimana, Christine en_US
dc.date.accessioned 2008-07-10T16:39:48Z
dc.date.available 2008-07-10T16:39:48Z
dc.date.created 2007 en_US
dc.date.issued 2008-07-10T16:39:48Z
dc.identifier.uri http://rave.ohiolink.edu/etdc/view?acc_num=mco1180025995 en_US
dc.identifier.uri http://hdl.handle.net/2374.OX/18132
dc.description Moraxella catarrhalis is a Gram-negative bacterium and is an important cause of otitis media in children and respiratory tract infections in adults with chronic obstructive pulmonary disease. Because of the emergence of antibiotic resistance among M. catarrhalis clinical isolates and the prevalence of M. catarrhalis infections, it is desirable to develop a vaccine for this organism. Most efforts towards designing a vaccine against M. catarrhalis infections are directed at studying surface antigens, especially outer membrane proteins. Adhesins are good vaccine candidates because they are often conserved within the bacterial species, and may contain conserved surface exposed epitope(s). In addition, targeting adhesins may interfere with adherence to mucosal surfaces, thus preventing bacteria from establishing an infection. The purpose of this dissertation research was to study the adherence mechanism of the Moraxella catarrhalis adhesin protein (McaP) and the outer membrane protein CD (OMPCD), and to define their vaccine potential. Our first set of studies demonstrated that McaP is an autotransporter protein containing a passenger domain, aa 51-336, that mediates adherence to human lung cells. In addition, we demonstrated that antibodies against McaP significantly reduce adherence to A549 human lung cells; thus, McaP is an important M. catarrhalis adhesin. This study also demonstrated that McaP protein is well conserved among the 16 clinical isolates tested, and contains surface exposed epitopes, which are all characteristics of a vaccine antigen. Our second set of studies demonstrated that OMPCD contains two domains specifying adherence to A549 human lung cells using three complementary approaches: E. coli cells expressing truncated OMPCD proteins, direct binding of recombinant His-tagged OMPCD proteins, and OMPCD polypeptides expressed on the surface of E. coli through the McaP display system. These cell-binding domains were delineated to aa 16-150 and aa 261-300 of O35E-OMPCD protein. These domains may be used as vaccine antigens in future studies. en_US
dc.format application/pdf en_US
dc.format 188p. en_US
dc.rights unrestricted en_US
dc.rights Copyright and permissions information available at the source archive en_US
dc.subject outer membrane protein CD en_US
dc.subject MCAP en_US
dc.subject surface display system en_US
dc.subject vaccine antigens en_US
dc.subject Adhesin of Moraxella catarrhalis en_US
dc.subject cell-binding domain en_US
dc.title Structural and Functional Analysis of Moraxella catarrhalis Adhesins MCAP and OMPCD en_US
dc.type Electronic Thesis or Dissertation en_US
dc.degree.name PhD en_US
dc.degree.level doctoral en_US
dc.degree.discipline Graduate Studies en_US
dc.degree.grantor University of Toledo Health Science Campus en_US
dc.contributor.publisher University of Toledo Health Science Campus / OhioLINK en_US

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