Open AccessThe capsular (K51) antigen of Escherichia coli 01:K51:H − , an O ‐acetylated poly‐ N ‐acetylglucosamine phosphate
Author(s) -
Jann Barbara,
Dengler Thomas,
Jann Klaus
Publication year - 1985
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1985.tb00872.x
Subject(s) - n acetylglucosamine , periodate , residue (chemistry) , acetylation , phosphate , hydrolysis , chemistry , escherichia coli , acetylglucosamine , biochemistry , antigen , nuclear chemistry , glucosamine , enzyme , biology , genetics , gene
The capsular K51 antigen of E.coli was isolated from a liquid culture of E.coli 01:K51:H − by Cetavlon precipitation. After purification it was obtained in a yield of about 80 mg/l. The polymer consisted of equimolar amounts of N ‐acetylglucosamine and phosphate and contained about 1.6 O ‐acetyl groups per N ‐acetylglucosamine residue. After de‐ O ‐acetylation it was resistant to periodate oxidation. Mild acid hydrolysis yielded N ‐acetylglucosamine‐3‐phosphate. With the aid of 13 C‐ and 31 P‐NMR spectroscopy it was ascertained that the K51 antigen is a poly‐ α ‐1.3‐ N ‐acetylglucosamine phosphate, in which most of the hydroxyl groups at C4 and C6 of the N ‐acetylglucosamine residue are acetylated.