Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (17)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Monti, E.
Right arrow Articles by Borsani, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Monti, E.
Right arrow Articles by Borsani, G.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Glycobiology, 1999, Vol. 9, No. 12 1313-1321
© 1999 Oxford University Press

Expression of a novel human sialidaseencoded by the NEU2 gene

Eugenio Montia,2, Augusto Preti2, Carlo Nesti, Andrea Ballabio and Giuseppe Borsani

Telethon Institute of Genetics and Medicine (TIGEM), SanRaffaele Biomedical Science Park, via Olgettina 58, 20132 Milan,Italy and 2Department of BiomedicalScience and Biotechnology, University of Brescia, via Valsabbina19, 25123 Brescia, Italy

Sialidases (E.C.3.2.1.18) belong to a group of glycohydrolyticenzymes, widely distributed in nature, which remove sialic acidresidues from glycoproteins and glycolipids. All of the sialidaseso far characterized at the molecular level share an Asp block,repeated three to five times in the primary structure, and an F/YRIPsequence motif which is part of the active site. Using a sequencehomology-based approach, we previously identified a human gene,named NEU2, mapping to chromosome 2q37. NEU2 encoded protein isa polypeptide of 380 amino acids with two Asp block consensusesand the YRIP sequence in the amino terminal part of the primarystructure. Here we demonstrate that NEU2 encodes a functional sialidase.NEU2 was expressed in COS7 cells, giving rise to a dramatic increasein the sialidase activity measured in cell extracts with the artificial substrate4-MU-NANA. Using a rabbit polyclonal antiserum, on Western blotsa protein band with a molecular weight of about 42 kDa was detectable,and its cytosolic localization was demonstrated with cell fractionation experiments.These results were confirmed using immunohistochemical techniques.NEU2 expression in E.coli cells allowed purificationof the recombinant protein. As already observed in the enzyme expressedin COS7 cells, NEU2 pH optimum corresponds to 5.6 and the polypeptideshowed a Km for 4-MU-NANA of 0.07 mM. In addition, basedon the detectable similarities between the NEU2 amino acid sequenceand bacterial sialidases, a prediction of the three-dimensionalstructure of the enzyme was carried out using a protein homologymodeling approach.

a To whom correspondence should be addressed.E-mail: monti{at}tigem.it


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
C. Tringali, B. Lupo, L. Anastasia, N. Papini, E. Monti, R. Bresciani, G. Tettamanti, and B. Venerando
Expression of Sialidase Neu2 in Leukemic K562 Cells Induces Apoptosis by Impairing Bcr-Abl/Src Kinases Signaling
J. Biol. Chem., May 11, 2007; 282(19): 14364 - 14372.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
F. Liang, V. Seyrantepe, K. Landry, R. Ahmad, A. Ahmad, N. M. Stamatos, and A. V. Pshezhetsky
Monocyte Differentiation Up-regulates the Expression of the Lysosomal Sialidase, Neu1, and Triggers Its Targeting to the Plasma Membrane via Major Histocompatibility Complex Class II-positive Compartments
J. Biol. Chem., September 15, 2006; 281(37): 27526 - 27538.
[Abstract] [Full Text] [PDF]

Home page
 Antimicrob. Agents Chemother.Home page
M. P. Malakhov, L. M. Aschenbrenner, D. F. Smee, M. K. Wandersee, R. W. Sidwell, L. V. Gubareva, V. P. Mishin, F. G. Hayden, D. H. Kim, A. Ing, et al.
Sialidase fusion protein as a novel broad-spectrum inhibitor of influenza virus infection.
Antimicrob. Agents Chemother., April 1, 2006; 50(4): 1470 - 1479.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Hinek, A. V. Pshezhetsky, M. von Itzstein, and B. Starcher
Lysosomal Sialidase (Neuraminidase-1) Is Targeted to the Cell Surface in a Multiprotein Complex That Facilitates Elastic Fiber Assembly
J. Biol. Chem., February 10, 2006; 281(6): 3698 - 3710.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. M. G. Chavas, C. Tringali, P. Fusi, B. Venerando, G. Tettamanti, R. Kato, E. Monti, and S. Wakatsuki
Crystal Structure of the Human Cytosolic Sialidase Neu2: EVIDENCE FOR THE DYNAMIC NATURE OF SUBSTRATE RECOGNITION
J. Biol. Chem., January 7, 2005; 280(1): 469 - 475.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
V. Seyrantepe, K. Landry, S. Trudel, J. A. Hassan, C. R. Morales, and A. V. Pshezhetsky
Neu4, a Novel Human Lysosomal Lumen Sialidase, Confers Normal Phenotype to Sialidosis and Galactosialidosis Cells
J. Biol. Chem., August 27, 2004; 279(35): 37021 - 37029.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Tringali, N. Papini, P. Fusi, G. Croci, G. Borsani, A. Preti, P. Tortora, G. Tettamanti, B. Venerando, and E. Monti
Properties of Recombinant Human Cytosolic Sialidase HsNEU2: THE ENZYME HYDROLYZES MONOMERICALLY DISPERSED GM1 GANGLIOSIDE MOLECULES
J. Biol. Chem., January 30, 2004; 279(5): 3169 - 3179.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.