Disease relevance of UTI89_C2660

• The amino acid composition of the ColiM6 protein was nearly identical to that of M protein isolated from streptococci with phage lysin (LysM6) [1].
• The lysin (named PlyGBS) was recombinantly expressed in Escherichia coli, and purified PlyGBS efficiently killed all tested GBS serotypes in vitro [2].
• The stability of mRNA for the delta-lysin of Staphylococcus aureus was determined by measuring the residual lysin synthesis after inhibition of DNA-dependent RNA polymerase activity with rifampin [3].
• Chromium-labeled lymphoma cells were lysed by NK lysin, and LPS dose-dependently inhibited the cytolysis at equimolar amounts [4].
• A lysin cloned from a phage infecting GBS was found to contain two putative catalytic domains and one putative binding domain, which is similar to the domain organization of some staphylococcal phage lysins [2].

High impact information on UTI89_C2660

• A predicted model generated from the nuclear magnetic resonance structure of a related protein, NK lysin, suggested that granulysin contains a four alpha helical bundle motif, with the alpha helices enriched for positively charged amino acids, including arginine and lysine residues [5].
• Remarkably, the Ejl lysin was able to attack murein from bacteria lacking choline in their sacculi, which suggests that pneumococcal lysins have a broader substrate specificity than previously assumed [6].
• The bacteria used as DNA delivery vectors were engineered to lyze upon entry in the cell due to impaired cell wall synthesis for Shigella flexneri and invasive Escherichia coli, or production of a phage lysin for Listeria mono- cytogenes [7].
• Here we report the binding of NK lysin to lipopolysaccharide (LPS) and its anti-LPS activity [4].
• Interaction of NK lysin, a peptide produced by cytolytic lymphocytes, with endotoxin [4].

Chemical compound and disease context of UTI89_C2660

• The lysin-encoding lys gene was verified by PCR amplification from the total phage DNA and subcloned [8].
• Partial purification and some properties of phi C2(W) lysin, a lytic enzyme produced by phage-infected cells of Streptococcus lactis C2 [9].

Biological context of UTI89_C2660

• The nucleotide sequence of a 1150-bp fragment coding for an active lysin was determined [10].
• The lysin gene was within a 4.1-kb DNA fragment of phi-0303 containing six open reading frames (ORFs) and two truncated ORFs [8].
• The deduced amino acid sequence of the mv1 lysin (LysA) was compared to that of other known lytic enzymes [10].
• The extracellular region of this protein contains three tandem lysin motifs (LysMs), a short peptide domain that is implicated in peptidoglycan or chitin binding in various bacterial or eukaryotic proteins, respectively [11].
• Controlled expression and structural organization of a Lactococcus lactis bacteriophage lysin encoded by two overlapping genes [12].

Anatomical context of UTI89_C2660

• In the same manner, NK lysin inhibited certain LPS-stimulated effects on mouse bone marrow cells as well as LPS binding to mouse granulocytes [4].
• Reevaluation of homology between the lysin and Bacillus subtilis PZA protein 15 led to the identification of a new potential ribosome binding site (RBS) [12].

Associations of UTI89_C2660 with chemical compounds

• Lipid A and polymyxin B inhibited the binding, demonstrating a preferential interaction of NK lysin with the lipid part of LPS [4].
• The translational start of the lysin gene was identified as an isoleucine codon, and this may lead to a low translation rate [12].
• The smaller lysin protein was isolated, and the N terminus was sequenced, confirming that one methionine codon acted as the start of a second gene [12].
• The generation of both reducing activity and N-terminal alanine residues during lysis indicated that the lysin is a bifunctional enzyme, possessing both glycosidase and endopeptidase activities [13].

Analytical, diagnostic and therapeutic context of UTI89_C2660

• Characterization of a lytic Lactobacillus plantarum bacteriophage and molecular cloning of a lysin gene in Escherichia coli [14].

References