TY  - JOUR
A1  - Andres, Dorothee
A1  - Baxa, Ulrich
A1  - Hanke, Christin
A1  - Seckler, Robert
A1  - Barbirz, Stefanie
T1  - Carbohydrate binding of Salmonella phage P22 tailspike protein and its role during host cell infection
N2  - TSPs (tailspike proteins) are essential infection organelles of bacteriophage P22. Upon infection, P22TSP binds to and cleaves the O-antigen moiety of the LPS (lipopolysaccharide) of its Salmonella host To elucidate the role of TSP during infection, we have studied binding to oligosaccharides and polysaccharides of Salmonella enteric Typhimurium and Enteritidis in vitro. P22TSP is a trimeric beta-helical protein with a carbohydrate-binding site on each subunit. Octasaccharide O-antigen fragments bind to P22TSP with micromolar dissociation constants. Moreover, P22TSP is an endorhamnosidase and cleaves the host O-antigen. Catalytic residues lie at the periphery of the high-affinity binding site, which enables unproductive binding modes, resulting in slow hydrolysis. However, the role of this hydrolysis function during infection remains unclear. Binding of polysaccharide to P22TSP is of high avidity with slow dissociation rates when compared with oligosaccharides. In vivo, the infection of Salmonella with phage P22 can be completely inhibited by the addition of LPS, indicating that binding of phage to its host via TSP is an essential step for infection.
Y1  - 2010
UR  - https://publishup.uni-potsdam.de/frontdoor/index/index/docId/32038
UR  - http://www.biochemsoctrans.org/
SN  - 0300-5127
ER  -