NationMaster - Encyclopedia: Neuraminidase

Sialidase 1 (lysosomal sialidase), also known as NEU1, is a human gene.^[1] The Entrez logo The Entrez Global Query Cross-Database Search System allows access to databases at the National Center for Biotechnology Information (NCBI) website. ... Ensembl is a bioinformatics research project aiming to develop a software system which produces and maintains automatic annotation on selected eukaryotic genomes. It is run in a collaboration between the Wellcome Trust Sanger Institute and the European Bioinformatics Institute, an outstation of the European Molecular Biology Laboratory. ... UniProt is the universal protein database, a central repository of protein data created by combining Swiss-Prot, TrEMBL and PIR. This makes it the worlds most comprehensive resource on protein information. ... Medline is a comprehensive literature database of life sciences and biomedical information. ... For other uses, see Gene (disambiguation). ...

The protein encoded by this gene encodes the lysosomal enzyme, which cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. In the lysosome, this enzyme is part of a heterotrimeric complex together with beta-galactosidase and cathepsin A (the latter also referred to as 'protective protein'). Mutations in this gene can lead to sialidosis.^[1]

Neuraminidase is a glycoside hydrolase enzyme (EC 3.2.1.18). It is frequently found as an antigenic glycoprotein and is best known as one of the enzymes found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. At least four neuraminidases in the human genome have been described. Deficiencies in the human enzyme NEU1 leads to sialidosis, a rare lysosomal storage disease. Glycoside hydrolases (also called glycosidases) catalyze the hydrolysis of the glycosidic linkage to generate two smaller sugars. ... Ribbon diagram of the enzyme TIM, surrounded by the space-filling model of the protein. ... The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. ... An antigen or immunogen is a molecule that stimulates an immune response. ... N-linked protein glycosylation (N-glycosylation of N-glycans) at Asn residues (Asn-x-Ser/Thr motifs) in glycoproteins[1]. Glycoproteins are proteins that contain oligosaccharide chains (glycans) covalently attached to their polypeptide backbones. ... Flu redirects here. ... A graphical representation of the normal human karyotype. ... Categories: Possible copyright violations ... The lysosomal storage diseases are a group of which over forty disorders are currently known that result from defects in lysosomal function. ...

Subtypes

Swiss-Prot lists 137 types of neuraminidase from various species as of October 18, 2006.^[2] Nine subtypes of influenza neuraminidase are known; many occur only in various species of duck and chicken. Subtypes N1 and N2 have been positively linked to epidemics in man, and strains with N3 or N7 subtypes have been identified in a number of isolated deaths^{[citation needed]}. Swiss-Prot is a curated biological database of protein sequences created in 1986 by Amos Bairoch during his PhD and developed by the Swiss Institute of Bioinformatics and the European Bioinformatics Institute. ...

Structure

Influenza neuraminidase exists as a mushroom-shape projection on the surface of the influenza virus. It has a head consisting of four co-planar and roughly spherical subunits, and a hydrophobic region that is embedded within the interior of the virus' membrane. It comprises a single polypeptide chain that is oriented in the opposite direction to the hemagglutinin antigen. The composition of the polypeptide is a single chain of six conserved polar amino acids, followed by hydrophilic, variable amino acids. Flu redirects here. ...

Function

Neuraminidase has functions that aid in the efficiency of virus release from cells. Neuraminidase cleaves terminal sialic acid residues from carbohydrate moieties on the surfaces of infected cells. This promotes the release of progeny viruses from infected cells. Neuraminidase also cleaves sialic acid residues from viral proteins, preventing aggregation of viruses. Administration of chemical inhibitors of neuraminidase is a treatment that limits the severity and spread of viral infections. Sialic acid is a generic term for the N- or O-substituted derivatives of neuraminic acid, a nine-carbon monosaccharide. ... Lactose is a disaccharide found in milk. ...

Neuraminidase is also a virulence factor for many bacteria including Bacteroides fragilis and Pseudomonas aeruginosa, where it is produced to cleave a sialic acid residue off ganglioside-GM1 (a modulator of cell surface and receptor activity) turning it into asialo-GM1 to which its type 4 pilli (attachment factors) bind preferentially. Species etc. ... Binomial name Pseudomonas aeruginosa (Schroeter 1872) Migula 1900 Synonyms Bacterium aeruginosum Schroeter 1872 Bacterium aeruginosum Cohn 1872 Micrococcus pyocyaneus Zopf 1884 Bacillus aeruginosus (Schroeter 1872) Trevisan 1885 Bacillus pyocyaneus (Zopf 1884) FlÃ¼gge 1886 Pseudomonas pyocyanea (Zopf 1884) Migula 1895 Bacterium pyocyaneum (Zopf 1884) Lehmann and Neumann 1896 Pseudomonas polycolor...

Ideally influenza virus neuraminidase (NA) should act on the same type of virus receptor the virus Hemagglutinin (HA) binds to. This is not always so. It is not quite clear how the virus manages to function when there is no close match between the specificities of NA and HA. Hemagglutinin, as depicted in a simplified molecular model. ...

Neuraminidase also plays a role in the beginning of influenza pathogenesis by cleaving sialic acid from the host glycoprotein and allowing the virus to enter the host (T-phages, macrophages, etc.).

Neuraminidase inhibitors

Neuraminidase inhibitors are useful for combating influenza infection: zanamivir, administered by inhalation; oseltamivir, administered orally; and under research is peramivir administered parenterally, that is through intravenous or intramuscular injection. Neuraminidase inhibitors are a class of antiviral drugs, whose mode of action relies on blocking the function of viral neuraminidase protein, thus preventing the virus from budding from the host cell. ... Flu redirects here. ... Zanamivir is a neuraminidase inhibitor used in the treatment of and prophylaxis of both influenza A and influenza B. Zanamivir was the first neuraminidase inhibitor commercially developed. ... Oseltamivir (INN) (IPA: ) is an antiviral drug that is used in the treatment and prophylaxis of both Influenzavirus A and Influenzavirus B. Like zanamivir, oseltamivir is a neuraminidase inhibitor. ... Peramivir is a pharmaceutical drug used to viral infections. ...

Further reading

Okamura-Oho Y, Zhang S, Callahan JW (1994). "The biochemistry and clinical features of galactosialidosis.". Biochim. Biophys. Acta 1225 (3): 244-54. PMID 8312369.
Seyrantepe V, Poupetova H, Froissart R, et al. (2004). "Molecular pathology of NEU1 gene in sialidosis.". Hum. Mutat. 22 (5): 343-52. doi:10.1002/humu.10268. PMID 14517945.
Verheijen FW, Palmeri S, Galjaard H (1987). "Purification and partial characterization of lysosomal neuraminidase from human placenta.". Eur. J. Biochem. 162 (1): 63-7. PMID 3102233.
Verheijen FW, Palmeri S, Hoogeveen AT, Galjaard H (1985). "Human placental neuraminidase. Activation, stabilization and association with beta-galactosidase and its protective protein.". Eur. J. Biochem. 149 (2): 315-21. PMID 3922758.
Hu H, Shioda T, Moriya C, et al. (1996). "Infectivities of human and other primate lentiviruses are activated by desialylation of the virion surface.". J. Virol. 70 (11): 7462-70. PMID 8892864.
Pshezhetsky AV, Potier M (1996). "Association of N-acetylgalactosamine-6-sulfate sulfatase with the multienzyme lysosomal complex of beta-galactosidase, cathepsin A, and neuraminidase. Possible implication for intralysosomal catabolism of keratan sulfate.". J. Biol. Chem. 271 (45): 28359-65. PMID 8910459.
Bonten E, van der Spoel A, Fornerod M, et al. (1997). "Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis.". Genes Dev. 10 (24): 3156-69. PMID 8985184.
Milner CM, Smith SV, Carrillo MB, et al. (1997). "Identification of a sialidase encoded in the human major histocompatibility complex.". J. Biol. Chem. 272 (7): 4549-58. PMID 9020182.
Pshezhetsky AV, Richard C, Michaud L, et al. (1997). "Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis.". Nat. Genet. 15 (3): 316-20. doi:10.1038/ng0397-316. PMID 9054950.
Vinogradova MV, Michaud L, Mezentsev AV, et al. (1998). "Molecular mechanism of lysosomal sialidase deficiency in galactosialidosis involves its rapid degradation.". Biochem. J. 330 ( Pt 2): 641-50. PMID 9480870.
van der Spoel A, Bonten E, d'Azzo A (1998). "Transport of human lysosomal neuraminidase to mature lysosomes requires protective protein/cathepsin A.". EMBO J. 17 (6): 1588-97. doi:10.1093/emboj/17.6.1588. PMID 9501080.
Lukong KE, Elsliger MA, Chang Y, et al. (2000). "Characterization of the sialidase molecular defects in sialidosis patients suggests the structural organization of the lysosomal multienzyme complex.". Hum. Mol. Genet. 9 (7): 1075-85. PMID 10767332.
Naganawa Y, Itoh K, Shimmoto M, et al. (2000). "Molecular and structural studies of Japanese patients with sialidosis type 1.". J. Hum. Genet. 45 (4): 241-9. PMID 10944856.
Bonten EJ, Arts WF, Beck M, et al. (2000). "Novel mutations in lysosomal neuraminidase identify functional domains and determine clinical severity in sialidosis.". Hum. Mol. Genet. 9 (18): 2715-25. PMID 11063730.
Lukong KE, Landry K, Elsliger MA, et al. (2001). "Mutations in sialidosis impair sialidase binding to the lysosomal multienzyme complex.". J. Biol. Chem. 276 (20): 17286-90. doi:10.1074/jbc.M100460200. PMID 11279074.
Penzel R, Uhl J, Kopitz J, et al. (2001). "Splice donor site mutation in the lysosomal neuraminidase gene causing exon skipping and complete loss of enzyme activity in a sialidosis patient.". FEBS Lett. 501 (2-3): 135-8. PMID 11470272.
Lukong KE, Seyrantepe V, Landry K, et al. (2002). "Intracellular distribution of lysosomal sialidase is controlled by the internalization signal in its cytoplasmic tail.". J. Biol. Chem. 276 (49): 46172-81. doi:10.1074/jbc.M104547200. PMID 11571282.
Sergi C, Penzel R, Uhl J, et al. (2001). "Prenatal diagnosis and fetal pathology in a Turkish family harboring a novel nonsense mutation in the lysosomal alpha-N-acetyl-neuraminidase (sialidase) gene.". Hum. Genet. 109 (4): 421-8. doi:10.1007/s004390100592. PMID 11702224.
Itoh K, Naganawa Y, Matsuzawa F, et al. (2002). "Novel missense mutations in the human lysosomal sialidase gene in sialidosis patients and prediction of structural alterations of mutant enzymes.". J. Hum. Genet. 47 (1): 29-37. PMID 11829139.

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External links

Medical Subject Headings (MeSH) is a huge controlled vocabulary (or metadata system) for the purpose of indexing journal articles and books in the life sciences. ... In biochemistry, a hydrolase is an enzyme that can break a chemical bond by hydrolysis. ... The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. ... Glycoside hydrolases (also called glycosidases) catalyze the hydrolysis of the glycosidic linkage to generate two smaller sugars. ... Amylase is the name given to glycoside hydrolase enzymes that break down starch into glucose molecules. ... Human salivary amylase. ... Chitinase (barley seed chitinase: PDB 1CNS, EC 3. ... Lysozyme single crystal. ... Galactosidases are enzymes (glycoside hydrolases) which catalyzes the hydrolysis of galactosides into monosaccharides If the galactoside is an alpha-galactoside, the enzyme is called alpha-galactosidase, and if it is a beta-galactoside, it is called beta-galactosidase. ... A Î²-galactosidase is a type of hydrolase enzyme (EC 3. ... Lactase (or β-galactosidase) is the enzyme involved in the hydrolysis of lactose to galactose and glucose. ... alpha-Mannosidase is an enzyme involved in the cleavage of the alpha form of mannose. ... Glucuronidase is a lysosomal glycosidase, a type of enzyme that removes carbohydrate groups from proteins. ... Hyaluronidase The hyaluronidases (EC 3. ... Pullulanase is a specific kind of glucanase, an amylolytic exoenzyme, that degrades pullulan. ... Acid Î²-glucosidase, drawn from PDB 1OGS. Glucocerebrosidase (also called glucosylceramidase or D-glucosyl-N-acylsphingosine glucohydrolase) is an enzyme (EC 3. ... Galactosylceramidase is an enzyme which removes galactose from ceramide derivatives. ... Alpha-N-acetylglucosaminidase is a protein associated with Sanfilippo syndrome. ... Alpha-Fucosidase is an enzyme that breaks down fucose. ... Hexosaminidase is an enzyme involved in the hydrolysis of several molecules containing hexose. ... Iduronidase is an enzyme involved in the degeneration of dermatan sulfate. ... Disaccharidase is a type of enzyme that breaks down disaccharides into monosaccharides. ... Headline text Sucrase (EC 3. ... Sucrase-isomaltase is an glucosidase enzyme. ... Invertase (EC 3. ... Maltase, drawn from PDB 1OBB. Maltase (EC 3. ... Wikipedia does not have an article with this exact name. ... Lactase is a member of the Î²-galactosidase family of enzyme: enzymes that hydrolysis Î² 1,4 bonded attachments off of galactose. ... Glucosidases are glycoside hydrolase enzymes categorized under the EC number 3. ... Cellulase is an enzyme complex which breaks down cellulose to beta-glucose. ... Alpha-glucosidase (EC 3. ... Beta-glucosidase is a glucosidase enzyme which acts upon Î² bonds. ... A debranching enzyme is a molecule that helps facilitate the breakdown of glycogen. ... DNA glycosylases are a family of enzymes involved in base excision repair. ... Oxoguanine glycosylase is a DNA glycosylase enzyme. ...

Contents

Subtypes

Structure

Function

Neuraminidase inhibitors

See also

References

Further reading

External links

Contents

Subtypes GA_googleFillSlot("encyclopedia_square");

Structure

Function

Neuraminidase inhibitors

See also

References

Further reading

External links

Subtypes