Lysogenic conversion of Salmonella typhimurium bacteriophages A3 and A4 consists of O-acetylation of rhamnose of the repeating unit of the O-antigenic polysaccharide chain.

Abstract:

:Lysogenization of Salmonella typhimurium with either of the bacteriophages A3 and A4 results in O-acetylation of the L-rhamnose residues of the O-polysaccharide chain of the lipopolysaccharide of the bacterial cell envelope. The O-acetyl group is found on both O-2 and O-3 of the L-rhamnosyl residues. This lysogenic conversion prevents the adsorption of the A3 and A4 phages and also greatly reduces the rate of adsorption of phage P22 to the O-polysaccharide chain as measured by binding studies with whole bacteria. Isolated lipopolysaccharide from A3- and A4-lysogenized bacteria was also inefficient in inactivating these phages: the concentration required for 50% inactivation was 10,000-fold higher than that for lipopolysaccharide from S. typhimurium not lysogenized by any A phage. Binding of phages A3 and A4 is accompanied by hydrolysis of the alpha-1,3 linkage between rhamnose and galactose in the tetrasaccharide repeating unit of the O-polysaccharide. Phage hydrolysis generates saccharides of various lengths, the majority being dodecasaccharides, i.e., equivalent to three repeating units. It is surmised that O-acetylation of the rhamnosyl residue interferes with phage A3, A4, and P22 infection by preventing binding to and hydrolysis of the O-polysaccharide chain, the initial step in the phage infection cycle. The new O-acetyl-rhamnose entities did not elicit specific antibodies in rabbits in accordance with earlier experiences. The O-acetylation of O-2 and O-3 of rhamnose is a new, hitherto unknown, modification of the O-polysaccharide chain of S. typhimurium.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Wollin R,Stocker BA,Lindberg AA

doi

10.1128/jb.169.3.1003-1009.1987

subject

Has Abstract

pub_date

1987-03-01 00:00:00

pages

1003-9

issue

3

eissn

0021-9193

issn

1098-5530

journal_volume

169

pub_type

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