Sialidases cloning

Chang, Y. K., and Chein, C. H. (1998). Simple two step procedure for purification of cloned small sialidase from unclaridied E. coli feedstocks, lnt. Conf. Expanded Bed Adsorption, 2nd, Napa Valley, CA, 1998, Abstr., p. 8.2. 

In the first primary structures of microbial sialidases, obtained by cloning and sequencing of the respective genes from Clostridium perfringens [769], Vibrio cholerae [770], Clostridium sordellii [77 ] and Salmonella typhimurium [772], an amino acid sequence motif was detected, which is repeated four-fold in each protein S-X-D-X-G-X-T-W [773]. This motif, named the Asp-box, was found in all 16 sialidases of animals, trypanosomes, and bacteria, which have so far been sequenced (see refs. [660,768] and Table 18). In viral sialidases, however, the motif was rarely detectable (e.g. only the sialidase from N9 influenza A virus strain exhibits the complete motif [786] and has probably undergone mutational alterations). 

Cloned sialidases and /rawi-sialidases with Asp-boxes ... 

NEU2 was the first vertebrate sialidase characterized using the recombinant DNA techniques. The enzyme was first cloned from rat skeletal muscle in 1993, and subsequently a highly similar protein was cloned from CHO cells.Overexpression... 

B. Rothe, P. Roggentin, and R. Schauer, The sialidase gene from Clostridium septicum Cloning, sequencing, expression in Escherichia coli and identification of conserved sequences in sialidases and other proteins, Mol Gen. Genet., 226 (1991) 190-197. 

T. Miyagi, K. Konno, Y. Emori, H. Kawasaki, K. Suzuki, A. Yasui, and S. Tsuik, Molecular cloning and expression of cDNA encoding rat skeletal muscle cytosolic sialidase, J. Biol. Chem., 268 (1993) 26435-26440. 

J. Ferrari, R. Harris, and T. G. Warner, Cloning and expression of a soluble sialidase fi om Chinese hamster ovary cells Sequence alignment similarities to bacterial sialidases, Glycobiology, 4 (1994) 367-373. 

E. Monti, M. T. Bassi, R. Bresciani, S. Civini, G. L. Croci, N. Papini, M. Riboni, G. Zanchetti, A. Ballabio, A. Preti, G. Tettamanti, B. Venerando, and G. Borsani, Molecular cloning and characterization of NEU4, the fourth member of the human sialidase gene family. Genomics, 83 (2004) 445-453. 

M. Manzoni, P. Colombi, N. Papini, L. Rubaga, N. Tiso, A. Preti, B. Venerando, G. Tettamanti, R. Bresciani, F. Argenton, G. Borsani, and E. Monti, Molecular cloning and biochemical characterization of sialidases from zebrafish (Danio rerio), Biochem. J., 408 (2007) 395—406. 

L.L. Hoyer, P. Roggentin, R. Schauer and E.R. Vimr, Purification and properties of cloned Salmonella typhimurium LT2 sialidase with virus-typical kinetic preference for sialyl a 2,3 linkages. J. Biochem. (Tokyo), 1991, llO, 462-467. 

Carrillo, M.B. Milner, C.M. Ball, S.T. Snoek, M. Campbell, R.D. Cloning and Characterization of a Sialidase from the Murine Histocompatibility-2 Complex Low Levels of mRNA and a Single Amino Acid Mutation are Responsible for Reduced Sialidase Activity in Mice Carrying the Neul a Allele. Glycobiology, 19, 7, 975-986. 

Summary of Cloned and Sequenced Sialidases from Eukarya and Bacteria... 

Henningsen, M., Roggentin, P., and Schauer, R., 1991, Cloning, sequencing and expression of the sialidase gene from Actinomyces viscosus DSM 43798, Biol. Chem. Hoppe-Seyler 372 1065- 012. 

Hoyer, L. L., Hamilton, A. C., Steenbergen, S. M., and Vimr, E. R., 1992, Cloning, sequencing and distribution of the Salmonella typhimurium LT-2 sialidase gene, nanH, provides evidence for interspecies gene transfer. Mol. Microbiol. 6 873-884. 

Roggentin, P., Rothe, B., Lottspeich, F., and Schauer, R., 1988, Cloning and sequencing of a Clostridium perfringens sialidase gene, FEBS Lett. 238 31-34. 

Recently, sialidase genes have been cloned from several bacterial and fungal strains, including Clostridiumperfringens (Roggentin et al., 1988a, 1992), Clos-... 

Recently, a cDNA clone encoding the cytosolic sialidase of rat skeletal muscle was prepared and expressed in Escherichia coli (Miyagi et al., 1993). The nucleotide sequence encodes 379 amino acid residues with a calculated molecular mass of 42,381 Da. The deduced amino acid sequence does not resemble any of the viral, bacterial, or parasitic sialidases, although it contains two Asp blocks, which are conserved in these enzymes (Roggentin et al., 1989). 

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