Bordetella Pertussis Research Paper

It is often thought that whooping cough is an outdated disease, due to the many ways we now have to combat the pathogen, but every year almost 400,000 people die due to infection with Bordetella pertussis (1, 41). Bordetella pertussis is a gram-negative coccobacillus bacterium, which causes whooping cough in humans (1, 41). The bacterium is spread by air borne particles or mucus droplets and is highly contagious. Although there is no known reservoir for the pathogen humans can often be asymptomatic, due to vaccination or immunity, and can easily spread the disease from person to person through coughing or sneezing (1, 41). Once inhaled the pathogen enters the respiratory tract and attaches to the ciliated respiratory epithelium. There
The pathogens genome encodes several proteins for the formation and secretion of virulence factors that aide in its effective attachment to these host cells such as filamentous hemagglutinin, fimbriae, and pertactin (2, 1512). Filamentous hemagglutinin is an adhesin. It has a monomeric rod like structure and consists of several beta sheet rich motifs (2, 1515). Specific amino acid sequences found in the filamentous hemmaglutinin allow the pathogen to specifically bind sulphated sugars on epithelial cells and CR3 integrins on macrophages and ciliary cells (2, 1515). Fimbriae, another virulence factor, are proteins located on the cell surface of the pathogen made up of two subunits, the major and the minor subunit (2, 1516). The minor subunit binds to monocytes at the Vla-5 subunit, and the major subunit attaches to sulphated sugars commonly found in the respiratory tract such as heparan sulphate ( 2, 1516). Although these two virulence factors have similar roles it has been shown that the filamenteous hemagglutinin plays a role in the pathogens attachment to the entire respiratory tract where as fimbriae play a more important role in attachment to laryngeal cells specifically ( 3, 1056). Pertactin is also an important virulence factor that aids in attachment of B. pertussis. It is a protein located on the outer membrane of the pathogen that has a very distinct beta helical conformation (2, 1518). The protein contains two very distinct arginine-glycine-aspartic acid sequences. These sequences are also found in proteins such as fibronectin, which mammals utilize to bind integrins (2, 1518). Therefore, this sequence allows the pathogen to specifically bind human integrins, and allows for better colonization of the