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Gene Review

nanH  -  sialidase

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

 
 
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Disease relevance of nanH

  • Cloning, sequencing and distribution of the Salmonella typhimurium LT2 sialidase gene, nanH, provides evidence for interspecies gene transfer [1].
  • The complete nucleotide sequence of nanH, encoding a 41,300 dalton polypeptide, was determined and the derived primary structure was similar to sialidases from Clostridium perfringens, Clostridium sordellii, Bacteroides fragilis, and Trypanosoma cruzi [1].
  • Subclones containing the Salmonella typhimurium LT2 sialidase gene, nanH, were expressed in Escherichia coli from multicopy derivatives of pBR329 [2].
  • A phage released from strain LT2 and identified as phage Fels-1 carries the nanH gene and a novel sodC gene, which was named sodCIII [3].
  • The STNA structure is topologically identical to the previously reported influenza virus neuraminidase structures, although very different in detail; the root-mean-square (r.m.s) deviation for 210 C alpha positions considered equivalent is 2.28 angstroms (out of a total of 390 residues in influenza and 381 in STNA) [4].
 

High impact information on nanH

 

Biological context of nanH

  • The nt sequence in the 15-402 region had in vivo promoter activity in an Escherichia coli promoter probe plasmid pKK232-8, which suggested that the small nanH promoter is functional in E. coli [9].
  • Amino acid residues Arg37, Arg56, Asp62, His63, Asp100, Glu230, Asp247, Tyr347, and Glu362 located around the pocket of modeled C. perfringens small nanH were superimposed with the active-site pocket of S. typhimurium LT12, nanH [10].
 

Associations of nanH with chemical compounds

  • Four regions of amino acids demonstrated great similarity to the "Asp boxes" (-Ser-X-Asp-X-Gly-X-Thr-Trp-) of other bacterial nanH proteins [9].
  • N-acetyl neuraminic acid (NeuAc) is the substrate for NA, and analogues of this core structure have been commercialized as antiviral therapeutics [11].
  • Recent developments in antiviral research have established the viability of targeting viral neuraminidase (NA), an enzyme that cleaves sialic acid from the cell-surface-mediating passage of the virus in the respiratory tract [11].
 

Analytical, diagnostic and therapeutic context of nanH

References

  1. Cloning, sequencing and distribution of the Salmonella typhimurium LT2 sialidase gene, nanH, provides evidence for interspecies gene transfer. Hoyer, L.L., Hamilton, A.C., Steenbergen, S.M., Vimr, E.R. Mol. Microbiol. (1992) [Pubmed]
  2. Purification and properties of cloned Salmonella typhimurium LT2 sialidase with virus-typical kinetic preference for sialyl alpha 2----3 linkages. Hoyer, L.L., Roggentin, P., Schauer, R., Vimr, E.R. J. Biochem. (1991) [Pubmed]
  3. Variable assortment of prophages provides a transferable repertoire of pathogenic determinants in Salmonella. Figueroa-Bossi, N., Uzzau, S., Maloriol, D., Bossi, L. Mol. Microbiol. (2001) [Pubmed]
  4. The structures of Salmonella typhimurium LT2 neuraminidase and its complexes with three inhibitors at high resolution. Crennell, S.J., Garman, E.F., Philippon, C., Vasella, A., Laver, W.G., Vimr, E.R., Taylor, G.L. J. Mol. Biol. (1996) [Pubmed]
  5. Purification, crystallization and preliminary crystallographic study of neuraminidase from Vibrio cholerae and Salmonella typhimurium LT2. Taylor, G., Vimr, E., Garman, E., Laver, G. J. Mol. Biol. (1992) [Pubmed]
  6. Salmonella typhimurium neuraminidase acts with inversion of configuration. Guo, X., Sinnott, M.L. Biochem. J. (1993) [Pubmed]
  7. Cloning and characterization of genes involved in production of mannose-resistant, neuraminidase-susceptible (X) fimbriae from a uropathogenic O6:K15:H31 Escherichia coli strain. Hacker, J., Schmidt, G., Hughes, C., Knapp, S., Marget, M., Goebel, W. Infect. Immun. (1985) [Pubmed]
  8. P-antigen-recognizing fimbriae from human uropathogenic Escherichia coli strains. Korhonen, T.K., Väisänen, V., Saxén, H., Hultberg, H., Svenson, S.B. Infect. Immun. (1982) [Pubmed]
  9. Small neuraminidase gene of Clostridium perfringens ATCC 10543: cloning, nucleotide sequence, and production. Chien, C.H., Huang, Y.C., Chen, H.Y. Enzyme Microb. Technol. (1997) [Pubmed]
  10. Site-directed mutations of the catalytic and conserved amino acids of the neuraminidase gene, nanH, of Clostridium perfringens ATCC 10543. Chien, C.H., Shann, Y.J., Sheu, S.Y. Enzyme Microb. Technol. (1996) [Pubmed]
  11. One-bead-one-inhibitor-one-substrate screening of neuraminidase activity. Ying, L., Gervay-Hague, J. Chembiochem (2005) [Pubmed]
 
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