ISSN:
0952-3499
Keywords:
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Medicine
Notes:
The interaction between phage G13 and different bacterial and synthetic oligosaccharides has been studied using equilibrium dialysis inhibition. The results, and conformational analysis of the oligosaccharides, make us conclude that the phage G13 carbohydrate receptor is a conformational domain involving three sugar residues. The following trisaccharide elements contain in domain: α-D-Galp-(1→3)-[α-D-Galp-(1→6)]-α-D-Glcp, α-D-Manp-(1→3)-[α-D-Manp-(1→6)]-α-D-Manp, and α-D-Glcp-(1→3)-[L-gly-α-D-man-Hepp-(1→7)]-L-gly-α-D-man-Hepp. Thus two structures, either a hexose substituted with α-D-glycopyranosyl groups in the 3- and 6-positions, or a heptose substituted with such groups in the 3- and 7-positions are functional G13 binding sites. Such domains are present in several cores of lipopolysaccharides from Salmonella and Escherichia coli species. Some cores, e.g. those from S. typhimurium chemotypes Ra, Rb1 and Rb2, contain two such domains. The identification of two G13 receptor domains within different core saccharides could explain the broad host range this phage.
Additional Material:
6 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/jmr.300020106
