Neuraminidase

Details

Name
Neuraminidase
Synonyms
  • 3.2.1.18
Gene Name
NA
Organism
Influenza A virus (strain A/Tokyo/3/1967 H2N2)
Amino acid sequence
>lcl|BSEQ0011033|Neuraminidase
MNPNQKIITIGSVSLTIATVCFLMQIAILVTTVTLHFKQHECDSPASNQVMPCEPIIIER
NITEIVYLNNTTIEKEICPKVVEYRNWSKPQCQITGFAPFSKDNSIRLSAGGDIWVTREP
YVSCDPVKCYQFALGQGTTLDNKHSNDTVHDRIPHRTLLMNELGVPFHLGTRQVCIAWSS
SSCHDGKAWLHVCITGDDKNATASFIYDGRLVDSIGSWSQNILRTQESECVCINGTCTVV
MTDGSASGRADTRILFIEEGKIVHISPLAGSAQHVEECSCYPRYPGVRCICRDNWKGSNR
PVVDINMEDYSIDSSYVCSGLVGDTPRNDDRSSNSNCRNPNNERGTQGVKGWAFDNGNDL
WMGRTISKDLRSGYETFKVIGGWSTPNSKSQINRQVIVDSDNRSGYSGIFSVEGKSCINR
CFYVELIRGRKQETRVWWTSNSIVVFCGTSGTYGTGSWPDGANINFMPI
Number of residues
469
Molecular Weight
52130.36
Theoretical pI
6.79
GO Classification
Functions
exo-alpha-(2->3)-sialidase activity / exo-alpha-(2->6)-sialidase activity / exo-alpha-(2->8)-sialidase activity / metal ion binding
Processes
carbohydrate metabolic process
Components
host cell plasma membrane / integral component of membrane / virion membrane
General Function
Metal ion binding
Specific Function
Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moities on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.
Pfam Domain Function
Transmembrane Regions
7-35
Cellular Location
Virion membrane
Gene sequence
>lcl|BSEQ0002913|1410 bp
ATGAATCCAAATCAAAAGATAATAACAATTGGCTCTGTCTCTCTCACCATTGCAACAGTA
TGCTTTCTCATGCAGATTGCCATCTTGGTAACTACTGTAACATTGCACTTTAAGCAACAT
GAGTGCGACTCCCCCGCGAGCAACCAAGTAATGCCGTGTGAACCAATAATAATAGAAAGG
AACATAACAGAGATAGTGTATTTGAATAACACCACCATAGAGAAAGAGATATGCCCCAAA
GTAGTGGAATACAGAAATTGGTCAAAGCCGCAATGTCAAATTACAGGATTTGCACCTTTT
TCTAAGGACAATTCAATCCGGCTTTCTGCTGGTGGGGACATTTGGGTGACGAGAGAACCT
TATGTGTCATGCGATCCTGTCAAGTGTTATCAATTTGCACTCGGGCAGGGGACCACACTA
GACAACAAACATTCAAATGACACAGTACATGATAGAATCCCTCATCGAACCCTATTAATG
AATGAGTTGGGTGTTCCATTTCACTTAGGAACCAGGCAAGTGTGTATAGCATGGTCCAGC
TCAAGTTGTCACGATGGAAAAGCATGGCTGCATGTTTGTATCACTGGGGATGATAAAAAT
GCAACTGCTAGCTTCATTTATGACGGGAGGCTTGTGGACAGTATTGGTTCATGGTCTCAA
AATATCCTCAGAACCCAGGAGTCGGAATGCGTTTGTATCAATGGGACTTGCACAGTAGTA
ATGACTGATGGAAGTGCTTCAGGAAGAGCCGATACTAGAATACTATTCATTGAAGAGGGG
AAAATTGTCCATATTAGCCCATTGGCAGGAAGTGCTCAGCATGTAGAGGAGTGTTCCTGT
TATCCTCGATATCCTGGCGTCAGATGTATCTGCAGAGACAACTGGAAAGGCTCTAATAGG
CCCGTCGTAGACATAAATATGGAAGATTATAGCATTGATTCCAGTTATGTGTGCTCAGGG
CTTGTTGGCGACACACCTAGAAACGATGACAGATCTAGCAATAGCAATTGCAGGAATCCT
AACAATGAGAGAGGGACTCAAGGAGTGAAAGGCTGGGCCTTTGACAATGGAAATGACTTG
TGGATGGGAAGAACAATCAGCAAGGATTTACGCTCAGGTTATGAAACTTTCAAAGTCATT
GGTGGTTGGTCCACACCTAATTCCAAATCGCAGATCAATAGACAAGTCATAGTTGACAGT
GATAATCGGTCAGGTTACTCTGGTATTTTCTCTGTTGAGGGCAAAAGCTGCATCAATAGG
TGCTTTTATGTGGAGTTGATAAGGGGAAGGAAACAGGAGACTAGAGTATGGTGGACCTCA
AACAGTATTGTTGTGTTTTGTGGCACTTCAGGTACCTATGGAACAGGCTCATGGCCTGAT
GGGGCGAACATCAATTTCATGCCTATATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP06820
UniProtKB Entry NameNRAM_I67A0
GenBank Protein ID1480200
GenBank Gene IDK01393
General References
  1. Lentz MR, Air GM, Laver WG, Webster RG: Sequence of the neuraminidase gene of influenza virus A/Tokyo/3/67 and previously uncharacterized monoclonal variants. Virology. 1984 May;135(1):257-65. [Article]
  2. Lindstrom SE, Cox NJ, Klimov A: Genetic analysis of human H2N2 and early H3N2 influenza viruses, 1957-1972: evidence for genetic divergence and multiple reassortment events. Virology. 2004 Oct 10;328(1):101-19. [Article]
  3. Nayak DP, Hui EK, Barman S: Assembly and budding of influenza virus. Virus Res. 2004 Dec;106(2):147-65. [Article]
  4. Moscona A: Neuraminidase inhibitors for influenza. N Engl J Med. 2005 Sep 29;353(13):1363-73. [Article]
  5. Suzuki Y: Sialobiology of influenza: molecular mechanism of host range variation of influenza viruses. Biol Pharm Bull. 2005 Mar;28(3):399-408. [Article]
  6. Varghese JN, Colman PM: Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 A resolution. J Mol Biol. 1991 Sep 20;221(2):473-86. [Article]
  7. White CL, Janakiraman MN, Laver WG, Philippon C, Vasella A, Air GM, Luo M: A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies. J Mol Biol. 1995 Feb 3;245(5):623-34. [Article]
  8. Jedrzejas MJ, Singh S, Brouillette WJ, Laver WG, Air GM, Luo M: Structures of aromatic inhibitors of influenza virus neuraminidase. Biochemistry. 1995 Mar 14;34(10):3144-51. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB022684-(Acetylamino)-3-Amino Benzoic AcidexperimentalunknownDetails
DB028294-(Acetylamino)-3-[(Aminoacetyl)Amino]Benzoic AcidexperimentalunknownDetails
DB045654-(Acetylamino)-3-[(Hydroxyacetyl)Amino]Benzoic AcidexperimentalunknownDetails
DB085704-(ACETYLAMINO)-3-HYDROXY-5-NITROBENZOIC ACIDexperimentalunknownDetails
DB085714-(ACETYLAMINO)-5-AMINO-3-HYDROXYBENZOIC ACIDexperimentalunknownDetails