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Distinct functional domains of the Salmonella enterica WbaP transferase that is involved in the initiation reaction for synthesis of the O antigen subunit

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Keywords
  • Wbap Is A Membrane Enzyme That Initiates O Antigen Synthesis In Salmonella Enterica By Catalysing Th
  • Wbap Possesses At Least Three Predicted Structural Domains: An N-Terminal Region Containing Four Tra
  • A Large Central Periplasmic Loop
  • And A C-Terminal Domain Containing The Last Transmembrane Helix And A Large Cytoplasmic Tail
  • In This Work
  • We Investigated The Contribution Of Each Region To Wbap Function By Constructing A Series Of Mutant
  • Enterica Serovars Typhi And Typhimurium
  • Truncated Forms Of Wbap Lacking The Periplasmic Loop Exhibited Altered Chain-Length Distributions In
  • Suggesting That This Central Domain Is Involved In Modulating The Chain-Length Distribution Of The O
  • The N-Terminal And Periplasmic Domains Were Dispensable For Complementation Of O Antigen Synthesis I
  • Suggesting That The C-Terminal Domain Carries The Sugar-Phosphate Transferase Activity
  • However
  • Despite The Fact That They Complemented The Synthesis Of O Antigen In The Deltawbap Mutant In Vivo
  • Membrane Extracts Containing Wbap Derivatives Without The N-Terminal Domain Failed To Transfer Radio
  • These Results Suggest That The N-Terminal Region Of Wbap
  • Which Contains Four Transmembrane Domains
  • Is Essential For The Insertion Or Stability Of The Protein In The Bacterial Membrane
  • We Propose That The Domain Structure Of Wbap Enables This Protein Not Only To Function In The Transf
  • Enterica
Disciplines
  • Ecology
  • Medicine

Abstract

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