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Topology and identification of critical residues of the O-acetyltransferase of serotype-converting bacteriophage, Sf6, of Shigella flexneri

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Thanweer, Farzaana
Tahiliani, Vikas
Korres, Haralambos
Verma, Naresh

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Academic Press

Abstract

The modification of the LPS O-antigen, seen in the diverse serotypes of Shigella flexneri is brought about by the glucosyltransferases (Gtr) and the O-acetyltransferase (Oac). In this study, we establish the membrane topology of Oac using the dual reporter PhoA-LacZα. We have determined that Oac is an integral membrane protein with 10 transmembrane regions. The hydrophilic N- and C-termini are oriented in the cytoplasm. Functionally important cytoplasmic and periplasmic loops have also been identified. Furthermore, cytoplasmic residues R73 and R75R76 were found to be critical to Oac function.

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Biochemical and Biophysical Research Communications

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Restricted until

2037-12-31