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Immunochemical Studies on Lipopolysaccharides from Wild-Type and Mutants of Escherichia coli K-12.

Authors :
Mayer, Hubert
Rapin, Anette M. C.
Schmidt, Günter
Boman, Hans G.
Source :
European Journal of Biochemistry. Jul76 Part 1, Vol. 66 Issue 2, p357-368. 12p.
Publication Year :
1976

Abstract

Lipopolysaccharides from a number of mutants of Escherichia coil K-12 were investigated by means of chemical and serological methods. Inhibition of passive hemagglutination and inhibition of precipitation show that L-rhamnose is the immunodominant sugar in the lipopolysaccharide from wild-type E. coli K-12. The disaccharide rhamnosyl-KDO (where KDO is 3-deoxy-D-manno-octulosonic acid) was isolated and characterized after mild acid hydrolysis of the lipopolysaccharide. It is concluded that rhamnose is present in the innermost part of the core as a side-chain substituent on KDO. From crosses between an E. coli K-12 donor and E. coil O8, hybrids were obtained which contained either one or both of the donor rfa and rfb clusters. Serum absorption studies with lipopolysaccharides from these hybrids indicated that the histidine-linked rfb cluster is responsible for the presence of rhamnose in the K-12 core oligosaccharide. Using paper chromatography of 32p-labelled lipopolysaccharides we have found heterogeneous lipopolysaccharide in two strains as well as some differences between two wild-type strains. The latter difference is believed to be due to varying contents of KDO-linked ethanolamine phosphate. The overall results presented together with those described in the companion paper clearly show that the core oligosaccharide in E. coil K-12 has a structure different from the types previously described for other strains of E. coli (designed coli R1 to coil R4). [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00142956
Volume :
66
Issue :
2
Database :
Academic Search Index
Journal :
European Journal of Biochemistry
Publication Type :
Academic Journal
Accession number :
13491784
Full Text :
https://doi.org/10.1111/j.1432-1033.1976.tb10525.x