Pertactin sandbox1: Difference between revisions
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== Function== | == Function== | ||
C-terminal beta helix function: | |||
The last step of secretion in autotransporters is C→ N terminal threading of the passenger domain through the outer membrane-spanning portion of the protein. After this step, the original structure of pertactin is formed. Interestingly, this translocation process does not depend on the consumption of ATP nor the presence of a proton gradient. (Junker et al., 2006). | |||
== Relevance== | == Relevance== | ||
Immunization Potential: | |||
P.69 has recently been shown to be an agglutinogen, an antigen that produces agglutinin which causes particles to coagulate(Charles et al. 1989). Due to agglutinogen properties as well as the ability to kill B. pertussis, P.69 has the potential for use in an acellular vaccine as an antigen for whooping cough (Gotto et al.1993). | |||
==Pertactin vs Pertussis Toxin: Virulence Factors== | ==Pertactin vs Pertussis Toxin: Virulence Factors== | ||
