In:
Canadian Journal of Microbiology, Canadian Science Publishing, Vol. 42, No. 10 ( 1996-10-01), p. 983-988
Abstract:
We determined whether Arg13, Met31, and Ser95 of the heat-labile enterotoxin B subunit (LT-B) might be involved in Lt-B binding to oligosaccharides, which did not bind to the B subunit of the cholera toxin (CT-B). Three LT-B mutants, R13H, M31L, and S95A were prepared by substituting three amino acid residues that differ in CT-B. These mutants formed a pentamer and exhibited the same binding ability to the G M1 ganglioside as native LT-B. Although these mutants did not bind to Bio-Gel A-5m, they did bind to the glycoprotein from mouse intestinal cells in the order R13H 〉 M31L 〉 S95A. These data suggest that Ser95, Met31, and Arg13 are important for LT-B binding to Bio-Gel A-5m, and that although Ser95 is also partially responsible for LT-B binding to the glycoprotein, Arg13 has no significant involvement in it.Key words: heat-labile enterotoxin, cholera toxin, Bio-Gel A-5m, glycoprotein.
Type of Medium:
Online Resource
ISSN:
0008-4166
,
1480-3275
Language:
English
Publisher:
Canadian Science Publishing
Publication Date:
1996
detail.hit.zdb_id:
280534-0
detail.hit.zdb_id:
1481972-7
SSG:
12
