Disease relevance of 9

• The tailspike protein (TSP) of Salmonella typhimurium phage P22 is a part of the apparatus by which the phage attaches to the bacterial host and hydrolyzes the O antigen [1].
• Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors [2].
• The classical example is the family including four families of pectinases without obviously related primary sequences, the phage P22 tailspike endorhamnosidase, chrondroitinase B and possibly pertactin from Bordetella pertusis [3].
• Characterization of bacteriophage P22 tailspike mutant proteins with altered endorhamnosidase and capsid assembly activities [4].
• We have introduced 19 different single amino acid substitutions at the two global suppressor sites independently and examined the effects on the tailspike formation in Escherichia coli [5].

High impact information on 9

• In this report, nine alpha-tailspike antibody binding epitopes were characterized by measuring the binding of these monoclonal antibodies to tailspike variants bearing surface point mutations [6].
• The major, central part of P22 tailspike protein, which forms a parallel beta-helix and is responsible for saccharide binding and hydrolysis, lacks detectable sequence homology to the Sf6 protein [7].
• The specific endorhamnosidase activities of Sf6 tailspike protein toward fluorescence-labeled dodeca-, deca-, and octasaccharide fragments of Shigella O-antigen suggest a similar active site topology of both proteins [7].
• Bacteriophage Sf6 tailspike protein is functionally equivalent to the well characterized tailspike of Salmonella phage P22, mediating attachment of the viral particle to host cell-surface polysaccharide [7].
• We have used a pair of monoclonal antibodies to probe the conformational features of full-length, newly synthesized tailspike chains recovered on ribosomes from phage-infected cells [8].

Chemical compound and disease context of 9

• Intracellular trapping of a cytoplasmic folding intermediate of the phage P22 tailspike using iodoacetamide [9].
• Tailspike protein binds and hydrolyzes the repetitive O-antigen structure in Salmonella lipopolysaccharide [10].
• The 666 residue subunit of the Salmonella typhimurium bacteriophage P22 tailspike contains eight cysteine residues distributed through the elongated structure [11].
• The suppressors were selected for their ability to correct the defects of missense tailspike polypeptide chains, generated by growth of gene 9 amber mutants on Salmonella host strains inserting either tyrosine, serine, glutamine or leucine at the nonsense codons [12].
• Each of the eight cysteines was replaced with serine by site-specific mutagenesis of the cloned P22 tailspike gene and the mutant genes expressed in Escherichia coli [13].

Biological context of 9

• The kinetics of appearance of the immunoreactive forms during the in vitro refolding of the protein in crude extracts of phage-infected cells was similar to that observed with the pure tailspike [14].
• The proteins made from 15 mutant tailspike structural genes carried on high level expression plasmids have been analyzed with respect to their in vivo stability, quaternary structure, capsid assembly activity, and enzymatic activity [4].
• Phage tailspike protein. A fishy tale of protein folding [15].
• In the assembly pathway of the trimeric P22 tailspike protein, the protein conformation critical for the partitioning between productive folding and off-pathway aggregation is a monomeric folding intermediate [16].
• We investigated the influence of the suppressor mutations on tailspike refolding in vitro, on its maturation at high expression levels in vivo, and on the rates of thermal unfolding of the native protein [17].

Anatomical context of 9

• The in vivo and in vitro folding, assembly and misfolding of an elongated protein, the thermostable tailspike adhesin of phage P22, reveals important aspects of the sequence control of chain folding as well as its failure mode, inclusion body formation [18].
• The gene and protein for the phage P22 tailspike, which is the phage adsorption organelle, have been intensively studied [19].

Associations of 9 with chemical compounds

• The tailspike protein was reconstituted from polypeptide chains unfolded by urea as described by Fuchs et al [14].
• Iodoacetamide also reacted with a folding intermediate during the refolding of purified tailspike chains in vitro, inhibiting further folding [9].
• The diverse cysteine states may be an outcome of the folding and assembly pathway of the tailspike, which though lacking disulfide bonds in the native state, utilizes transient disulfide bonds in the maturation pathway [11].
• The gene 9 mutation hmH3034 synthesizes a tailspike protein with a change at amino acid 100 from Asp to Asn [20].
• In contrast, these conformational features are greatly altered by chemical denaturation of the tailspike with lithium halide and guanidine hydrochloride [21].

Analytical, diagnostic and therapeutic context of 9

• As shown by circular dichroism and Fourier transform infrared spectroscopy, the secondary structure contents of Sf6 and P22 tailspike proteins are very similar [7].
• Monoclonal antibody epitope mapping describes tailspike beta-helix folding and aggregation intermediates [6].
• The tailspike protein of phage P22 is a model system for which genetic analysis has permitted mutational dissection of the role of amino acid positions in the polypeptide chain in directing its in vivo folding [22].
• The tailspike protein was denatured to unfolded polypeptide chains in 6 M urea, pH 3, as disclosed by analytical ultracentrifugation, fluorescence, and circular dichroism [23].
• Secondary structure and thermostability of the phage P22 tailspike. XX. Analysis by Raman spectroscopy of the wild-type protein and a temperature-sensitive folding mutant [24].

References