HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Eriksson, U. Articles by Lindberg, A. A. Search for Related Content PubMed PubMed Citation Articles by Eriksson, U. Articles by Lindberg, A. A. Agricola Articles by Eriksson, U. Articles by Lindberg, A. A.

Salmonella Phage Glycanases: Substrate Specificity of the Phage P22 Endo-rhamnosidase

Department of Bacteriology, National Bacteriological Laboratory, S-105 21 Stockholm, Sweden
^* Department of Organic Chemistry, Arrhenius Laboratory, University of Stockholm, S-104 05 Stockholm, Sweden

Interaction between phage P22 and phenol-water extracted lipopolysaccharides from sensitive Salmonella bacteria belonging to serogroups A, B and D1 results in hydrolysis of the -L-rhamnosyl linkages within the tetrasaccharide repeating unit of the O-antigenic polysaccharide chain. These O-antigens have identical structures except for the nature of the 3,6-dideoxy-hexosyl group linked to O-3 of the D-mannosyl residue. Removal of the dideoxysugar, or periodate oxidation followed by borohydride reduction of the L-rhamnosyl residue made the O chain resistant to the endo-rhamnosidase. Substitution of the D-galactosyl residue at O-4, but not at O-6, with an -D-glucosyl group was compatible with hydrolysis. A number of Klebsiella pneumoniae and Shigella flexneri lipo- or capsular polysaccharides containing chain L-rhamnosyl residues were tested but none was sensitive to the P22 endo-rhamnosidase. The substrate specificity of the endo-rhamnosidase parallels the lytic specificity of the phage which suggests that the initial step in phage P22 infection is a P22 tail enzyme O-antigen substrate interaction. The main product of the hydrolysate was octa-, dodeca- and hexadecasaccharides. Treatment of phage FO resistant smooth strains of S. typhimurium with P22 tails removed O polysaccharide chains and made previously ‘hidden’ FO receptors accessible to the phage.

Received 1 August 1978; accepted 24 November 1978.