Functional characterization of Vibrio cholerae O1 WbeW enzyme responsible for initial reaction in O antigen biosynthesis

• Published in: Biotechnology and bioprocess engineering Vol. 20; no. 6; pp. 980 - 987
• Main Authors: Kim, Chang Sup, Seo, Jeong Hyun, Cha, Hyung Joon
• Format: Journal Article
• Language: English
• Published: Seoul The Korean Society for Biotechnology and Bioengineering 01.11.2015; Springer Nature B.V; 한국생물공학회
• Subjects: ABC transporters; Antigen presentation; Antigens; Biosynthesis; Biotechnology; Chemical engineering; Chemistry; Chemistry and Materials Science; E coli; Enzymes; Escherichia coli; Exports; Glycerol; Industrial and Production Engineering; Klebsiella pneumoniae; Localization; O-antigens; Protein expression; Protein synthesis; Proteins; Research Paper; Studies; Vibrio cholerae; Vibrio cholerae O1; 생물공학; South Korea; membrane protein; O1; undecaprenyl phosphate galactose-1-phosphate transferase; WbeW enzyme
• ISSN: 1226-8372; 1976-3816
• DOI: 10.1007/s12257-015-0677-9

Vibrio cholerae O1 employs the ATP-binding cassette (ABC) transporter-dependent pathway for O antigen biosynthesis. Different from highly studied Klebsiella pneumoniae and Escherichia coli, it was reported that initial reaction of O antigen biosynthesis in V. cholerae O1 may be involved in WbeW protein, which is predicted to be a galactosyltransferase. In this work, we report expression and characterization of WbeW enzyme. WbeW was expressed as membrane-associated form in E. coli and it was obtained with high purity. The enzyme had a function of transferring Gal-1-P from UDP-Gal to Und-P, implying that initial glycan of O antigen in V. cholerae O1 can be composed of a Gal residue.