Pertactin sandbox1: Difference between revisions

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Kimberly Eldridge, Melissa Gray, Rachel Korba, Claire Gormley, Zackary Zayakosky

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 == Function==
-The closely related organisms ''B. pertussis, B. parapertussis, and B. bronchiseptica'' all produce slightly different forms of pertactin, which differ in the passenger domain (p.69, P.70, P.68 respectively). Specifically, the difference in size is due to the number of internal  repeats within the passenger domain. These different forms of pertactin all share two RGD motifs that are thought to be relevant to cell binding. One is found in the passenger domain and one in the transporter domain. There is further evidence that pertactin functions in adhesion, however, the data is contradictory. ''In vitro'' adhesion assays show that pertactin allows for adhesion to general cell lines such as CHO and HeLa cells, however, no evidence for was found to convey that pertactin aids in adhesion of bacterial cells to either bronchial or laryngeal cells. Furthermore, no receptor has been identified for pertactin <ref name= "HEN">Henderson, I., & Nataro, J. (2001). Virulence Functions of Autotransporter Proteins. Infection and Immunity, 1231-1243.</ref>. This data supports the conflict of whether or not the function of pertactin is adhesion to host cells.
+The closely related organisms ''B. pertussis, B. parapertussis, and B. bronchiseptica'' all produce slightly different forms of pertactin, which differ in the passenger domain (P.69, P.70, P.68 respectively). Specifically, the difference in size is due to the number of internal  repeats of (GGXXP) in a proline rich region within the passenger domain. These different forms of pertactin all share two RGD motifs that are thought to be relevant to cell binding. One is found in the passenger domain and one in the transporter domain. There is further evidence that pertactin functions in adhesion, however, the data is contradictory. ''In vitro'' adhesion assays show that pertactin allows for adhesion to general cell lines such as CHO and HeLa cells, however, no evidence for was found to convey that pertactin aids in adhesion of bacterial cells to either bronchial or laryngeal cells. Furthermore, no receptor has been identified for pertactin <ref name= "HEN">Henderson, I., & Nataro, J. (2001). Virulence Functions of Autotransporter Proteins. Infection and Immunity, 1231-1243.</ref>. This data supports the conflict of whether or not the function of pertactin is adhesion to host cells.
 In ''B. bronchiseptica'', pertactin seemed to be involved in the cytotoxicity of mononuclear phagocytic cells. A possible explanation is that pertactin promoted stable adhesion of the bacterium to the phagocyte. Researchers also found that pertactin is produced ''in vitro'' at an intermediate time in ''B. pertussis'' growth: after another virulence factor, FHA, but before pertussis toxin. This occurrence supports the idea that pertactin is involved in a closer adhesion to mammalian cells but prior to toxin release <ref name="HEN" />. If pertactin truly is an adhesion molecule, it would be a huge contribution to the overall pathogenesis of the species.