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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dc.contributor.authorSaldías, M. Soledad
dc.contributor.authorPatel, Kinnari
dc.contributor.authorMarolda, Cristina L.
dc.contributor.authorBittner, Mauricio
dc.contributor.authorContreras, Inés
dc.contributor.authorValvano, Miguel A.
dc.date.accessioned2024-04-05T16:07:26Z
dc.date.available2024-04-05T16:07:26Z
dc.date.issued2008-02
dc.descriptionINDEXACIÓN: SCOPUS.
dc.description.abstractWbaP is a membrane enzyme that initiates O antigen synthesis in Salmonella enterica by catalysing the transfer of galactose 1-phosphate (Gal-1-P) onto undecaprenyl phosphate (Und-P). WbaP possesses at least three predicted structural domains: an N-terminal region containing four transmembrane helices, 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 WbaP proteins and using them to complement O antigen synthesis in ΔwbaP mutants of S. enterica serovars Typhi and Typhimurium. Truncated forms of WbaP lacking the periplasmic loop exhibited altered chain-length distributions in O antigen polymerization, suggesting that this central domain is involved in modulating the chain-length distribution of the O polysaccharide. The N-terminal and periplasmic domains were dispensable for complementation of O antigen synthesis in vivo, 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 ΔwbaP mutant in vivo, membrane extracts containing WbaP derivatives without the N-terminal domain failed to transfer radioactive Gal from UDP-Gal into a lipid-rich fraction. 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 transfer of Gal-1-P to Und-P but also to establish critical interactions with additional proteins required for the correct assembly of O antigen in S. enterica. © 2008 SGM.
dc.identifier.citationMicrobiology, Volume 154, Issue 2, Pages 440 - 453, February 2008
dc.identifier.doi10.1099/mic.0.2007/013136-0
dc.identifier.issn1350-0872
dc.identifier.urihttps://repositorio.unab.cl/handle/ria/55692
dc.language.isoen
dc.publisherMicrobiology Society
dc.rights.licenseCC BY 4.0 DEED Atribución 4.0 Internacional
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/deed.es
dc.subjectAmino Acid Sequence
dc.subjectBacterial Proteins
dc.subjectBase Sequence
dc.subjectCloning, Molecular
dc.subjectConserved Sequence
dc.subjectEscherichia coli
dc.subjectMolecular Sequence Data
dc.subjectMutagenesis, Site-Directed
dc.subjectO Antigens
dc.subjectPeptides
dc.subjectPeriplasmic Proteins
dc.subjectProtein Structure, Tertiary
dc.subjectSalmonella enterica
dc.subjectSequence Analysis
dc.subjectTransferases
dc.titleDistinct 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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