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- W567556361 abstract "Capsular polysaccharide expression is an important virulence factor for many invasive bacterial pathogens of human. The capsule confers resistance to both specific and non-specific host defences. Escherichia coli offers a model system to study the mechanisms by which capsular polysaccharides are synthesised and exported out of the bacteria. Biosynthesis of the E. coli K5 capsular polysaccharide requires the KfiA, KfiB, KfiC, and KfiD proteins, which consists of the repeat structure -4)GlcA-(1,4)-GlcNAc-(1-. The effect of mutations in individual genes, involved in the biosynthesis and transport, on the localization of other protein was determined using anti-his and specific antisera. In this study the KfiB and KfiC were fused to a hexahistidine tag to facilitate protein purification. Both of the KfiB and KfiC fusion proteins with hexahistidine was successfully purified using Ni2+-NTA. Analysis of the location within the cell demonstrated that the association of KfiB with the cytoplasmic membrane is not dependent on either KfiA or KfiC but in the presence of these proteins, KfiB appears to be more stable. However the localization of KfiC with the cytoplasmic membrane was dependent to the presence of KfiB protein but not KfiA. Therefore KfiB protein appears to play a structural role in the assembly and maintenance of the biosynthetic complex on the inner membrane." @default.
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- W567556361 date "2003-01-01" @default.
- W567556361 modified "2023-09-29" @default.
- W567556361 title "The localization of KfiA, B and C proteins involved in the biosynthesis of the Escherichia coli K5 capsular polysaccharide" @default.
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