Abstract:
:Coli surface antigen 6, CS6, is one of the most prevalent colonization factors (CFs) associated with Enterotoxigenic Escherichia coli (ETEC) bacteria, the most common cause of diarrhea among infants and children in developing countries. The CS6 operon encodes two structural subunit proteins, CssA and CssB, a chaperon, CssC, and an usher, CssD. Since little is known about the relationship of the genes and their role in expression and surface assembly of CS6, the operon was cloned into a laboratory E. coli strain, and mutants were constructed by creating deletions in each of the genes. Examination of protein expression by different methods, using monoclonal antibodies with specificities for the individual CS6 structural proteins, suggested that the usher (CssD) was not involved in assembly or surface expression of CS6 whereas deletion of the chaperon (CssC) significantly reduced levels of CssA, but not of CssB. Binding studies with CaCo-2 cells demonstrated that there is a combined effect of CssC and CssD on receptor binding, presumably associated with their activities in assembly and transport of the structural subunits. These findings may have important implications for the construction of strains expressing high levels of CS6 on the surface for eventual use in an ETEC vaccine.
journal_name
Vaccinejournal_title
Vaccineauthors
Tobias J,Lebens M,Källgård S,Nicklasson M,Svennerholm AMdoi
10.1016/j.vaccine.2008.07.091subject
Has Abstractpub_date
2008-10-03 00:00:00pages
5373-80issue
42eissn
0264-410Xissn
1873-2518pii
S0264-410X(08)01054-2journal_volume
26pub_type
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