About: Interactions of phage P22 tails with their cellular receptor, Salmonella O-antigen polysaccharide.

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About: Interactions of phage P22 tails with their cellular receptor, Salmonella O-antigen polysaccharide. Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Interactions of phage P22 tails with their cellular receptor, Salmonella O-antigen polysaccharide.
Creator	Baxa, Ulrich Huber, Robert Miller, Stefan Seckler, Robert Steinbacher, Stefan Weintraub, Andrej
Source	PMC
abstract	Bacteriophage P22 binds to its cell surface receptor, the repetitive O-antigen structure in Salmonella lipopolysaccharide, by its six homotrimeric tailspikes. Receptor binding by soluble tailspikes and the receptor-inactivating endorhamnosidase activity of the tailspike protein were studied using octa- and dodecasaccharides comprising two and three O-antigen repeats of Salmonella enteritidis and Salmonella typhimurium lipopolysaccharides. Wild-type tailspike protein and three mutants (D392N, D395N, and E359Q) with defective endorhamnosidase activity were used. Oligosaccharide binding to all three subunits, measured by a tryptophan fluorescence quench or by fluorescence depolarization of a coumarin label attached to the reducing end of the dodecasaccharide, occurs independently. At 10 degrees C, the binding affinities of all four proteins to oligosaccharides from both bacterial strains are identical within experimental error, and the binding constants for octa- and dodecasaccharides are 1 x 10(6) M(-1) and 2 x 10(6) M(-1), proving that two O-antigen repeats are sufficient for lipopolysaccharide recognition by the tailspike. Equilibration with the oligosaccharides occurs rapidly, but the endorhamnosidase produces only one cleavage every 100 s at 10 degrees C or about 2 min(-1) at the bacterial growth temperature. Thus, movement of virions in the lipopolysaccharide layer before DNA injection may involve the release and rebinding of individual tailspikes rather than hydrolysis of the O-antigen.
has issue date	1996-10-01(xsd:dateTime)
bibo:pmid	8889178
has license	no-cc
sha1sum (hex)	b1d5e48dbb2f37918b0d8007a8197f465b54845c
resource representing a document's title	Interactions of phage P22 tails with their cellular receptor, Salmonella O-antigen polysaccharide.
has PubMed Central identifier	PMC1233670
has PubMed identifier	8889178
schema:publication	Biophys J
resource representing a document's body	covid:b1d5e48dbb2f37918b0d8007a8197f465b54845c#body_text
is schema:about of	named entity 'cleavage' named entity 'lipopolysaccharide' named entity 'release' named entity 'binding' named entity 'structure' named entity 'M-1' named entity 'binding' named entity 'M-1' named entity 'subunits' named entity 'defective' named entity 'repeats' named entity 'independently' named entity 'fluorescence' named entity 'O-Antigen' named entity 'mutants' named entity 'virions' named entity 'endorhamnosidase' named entity 'Receptor binding' named entity 'oligosaccharides' named entity 'lipopolysaccharide' named entity 'Salmonella enteritidis' named entity 'bacterial growth' named entity 'antigen' named entity 'antigen' named entity 'bacterial strains' named entity 'lipopolysaccharide' named entity 'endorhamnosidase' named entity 'endorhamnosidase' named entity 'M-1' named entity 'dissociation constant' named entity 'HPLC' named entity 'protein expression' named entity 'bacteriophage' named entity 'oligosaccharide' named entity 'mutant proteins' named entity 'right-handed' named entity 'tryptophan fluorescence' named entity 'protein' named entity 'wild-type' named entity 'carbohydrate' named entity 'protein' named entity 'antigen' named entity 'enzymatic mechanism' named entity 'oligosaccharide' named entity 'adhesin' named entity 'fluorescence' named entity 'polysaccharide' named entity 'biophysical' named entity 'polysaccharide' named entity 'helix' named entity '1 mM' named entity '16.8' named entity 'kcat' named entity 'fluorescence' named entity 'Oligosaccharide' named entity 'binding affinities' named entity 'free energy' named entity 'Bayer' named entity 'bacteriophages' named entity 'binding domain' named entity 'accessible to solvent' named entity 'absorbance' named entity 'amino-terminal' named entity 'protein complex' named entity 'heat capacity' named entity 'Salmonella' named entity 'supernatant' named entity 'antigen' named entity 'carboxy-terminal' named entity 'substrate' named entity 'x-ray' named entity 'cooperativity' named entity 'oligosaccharide' named entity 'protein' named entity 'nonlinear regression' named entity 'x-ray crystallography' named entity 'titration' named entity 'polypeptide'

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