Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors.

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Carbohydrate binding of Salmonella phage P22 tailspike protein and its role during host cell infection.

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 enterica Typhimurium and Enteritidis in vitro. P22TSP is a trimeric ...

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Interactions of phage P22 tailspike protein with GroE molecular chaperones during refolding in vitro.

Because efficient folding in vivo and reconstitution in vitro of phage P22 tailspike protein is temperature-sensitive, and because a chaperone function of the GroE proteins for tailspike folding in vivo has been suggested by genetic observations, the interactions of purified Escherichia coli GroE proteins with phage P22 tailspikes during refolding in vitro were investigated. At elevated tempera...

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Orally Administered P22 Phage Tailspike Protein Reduces Salmonella Colonization in Chickens: Prospects of a Novel Therapy against Bacterial Infections

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Stem Mutants in the N-terminal Domain of the Phage P22 Tailspike Protein

The P22 tailspike protein is an intensely studied protein whose structure and sequence has been described. However, a study, describing important protein interactions related to its function at the N-terminal domain, has been lacking. The P22 tailspike protein (TSP) consists of three identical polypeptide chains of 666aa. The first 108 of the 666aa in the P22 TSP form a trimeric N-terminal doma...

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Crystal Structure of ORF210 from E. coli O157:H1 Phage CBA120 (TSP1), a Putative Tailspike Protein

Bacteriophage tailspike proteins act as primary receptors, often possessing endoglycosidase activity toward bacterial lipopolysaccharides or other exopolysaccharides, which enable phage absorption and subsequent DNA injection into the host. Phage CBA120, a contractile long-tailed Viunalikevirus phage infects the virulent Escherichia coli O157:H7. This phage encodes four putative tailspike prote...

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ژورنال

عنوان ژورنال: Proceedings of the National Academy of Sciences

سال: 1996

ISSN: 0027-8424,1091-6490

DOI: 10.1073/pnas.93.20.10584