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Gene Review

UTI89_C2660  -  bacteriophage HK620 gene R-like

Escherichia coli UTI89

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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


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


Anatomical context of UTI89_C2660


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


  1. Streptococcal M6 protein expressed in Escherichia coli. Localization, purification, and comparison with streptococcal-derived M protein. Fischetti, V.A., Jones, K.F., Manjula, B.N., Scott, J.R. J. Exp. Med. (1984) [Pubmed]
  2. Removal of group B streptococci colonizing the vagina and oropharynx of mice with a bacteriophage lytic enzyme. Cheng, Q., Nelson, D., Zhu, S., Fischetti, V.A. Antimicrob. Agents Chemother. (2005) [Pubmed]
  3. In vitro synthesis of the delta-lysin of Staphylococcus aureus. Lee, K.Y., Birkbeck, T.H. Infect. Immun. (1984) [Pubmed]
  4. Interaction of NK lysin, a peptide produced by cytolytic lymphocytes, with endotoxin. Andersson, M., Girard, R., Cazenave, P. Infect. Immun. (1999) [Pubmed]
  5. Granulysin, a T cell product, kills bacteria by altering membrane permeability. Ernst, W.A., Thoma-Uszynski, S., Teitelbaum, R., Ko, C., Hanson, D.A., Clayberger, C., Krensky, A.M., Leippe, M., Bloom, B.R., Ganz, T., Modlin, R.L. J. Immunol. (2000) [Pubmed]
  6. The two-step lysis system of pneumococcal bacteriophage EJ-1 is functional in gram-negative bacteria: triggering of the major pneumococcal autolysin in Escherichia coli. Diaz, E., Munthali, M., Lunsdorf, H., Holtje, J.V., Timmis, K.N. Mol. Microbiol. (1996) [Pubmed]
  7. Wild-type intracellular bacteria deliver DNA into mammalian cells. Grillot-Courvalin, C., Goussard, S., Courvalin, P. Cell. Microbiol. (2002) [Pubmed]
  8. Mur-LH, the broad-spectrum endolysin of Lactobacillus helveticus temperate bacteriophage phi-0303. Deutsch, S.M., Guezenec, S., Piot, M., Foster, S., Lortal, S. Appl. Environ. Microbiol. (2004) [Pubmed]
  9. Partial purification and some properties of phi C2(W) lysin, a lytic enzyme produced by phage-infected cells of Streptococcus lactis C2. Mullan, W.M., Crawford, R.J. J. Dairy Res. (1985) [Pubmed]
  10. Cloning, expression and sequence analysis of an endolysin-encoding gene of Lactobacillus bulgaricus bacteriophage mv1. Boizet, B., Lahbib-Mansais, Y., Dupont, L., Ritzenthaler, P., Mata, M. Gene (1990) [Pubmed]
  11. LysM domains of Medicago truncatula NFP protein involved in Nod factor perception. Glycosylation state, molecular modeling and docking of chitooligosaccharides and Nod factors. Mulder, L., Lefebvre, B., Cullimore, J., Imberty, A. Glycobiology (2006) [Pubmed]
  12. Controlled expression and structural organization of a Lactococcus lactis bacteriophage lysin encoded by two overlapping genes. Shearman, C.A., Jury, K.L., Gasson, M.J. Appl. Environ. Microbiol. (1994) [Pubmed]
  13. The bifunctional peptidoglycan lysin of Streptococcus agalactiae bacteriophage B30. Pritchard, D.G., Dong, S., Baker, J.R., Engler, J.A. Microbiology (Reading, Engl.) (2004) [Pubmed]
  14. Characterization of a lytic Lactobacillus plantarum bacteriophage and molecular cloning of a lysin gene in Escherichia coli. Yoon, S.S., Kim, J.W., Breidt, F., Fleming, H.P. Int. J. Food Microbiol. (2001) [Pubmed]
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