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Gene Review

NA  -  neuraminidase

Influenza B virus

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Disease relevance of NA


High impact information on NA


Chemical compound and disease context of NA


Biological context of NA

  • The reading frame for this polypeptide begins with the first AUG codon on the mRNA and overlaps the reading frame for the viral neuraminidase by 292 nucleotides [9].
  • The deduced amino acid sequences for neuraminidase showed only a 7% difference, whereas those for the NB proteins differed by 20% [12].
  • A guanidino group incorporated into two unrelated NA inhibitors was previously reported to occupy different negatively charged sites in the NA active site, A new inhibitor containing two guanidino groups was synthesized in order to utilize both sites in an attempt to acquire a combined increase in affinity [13].
  • The virulence of the transfectant viruses in mice was directly proportional to the amount of NA incorporated [14].
  • Analysis of the genomes of non-ts recombinants obtained by crossing ts7 and UV-inactivated B/Lee showed that ts7 had the ts mutation only in RNA segment 6 coding for NA and the glycoprotein NB [2].

Anatomical context of NA

  • However, only one of these peptides, corresponding to residues 79 to 93 of NA (NA 79-93), was able to restimulate T cells of mice immunized with infectious virus [15].
  • These data suggest that the NA 79-93 T-cell determinant which is commonly presented during an encounter with influenza virus in vivo is processed preferentially from NA synthesized within antigen-presenting cells [15].
  • A comparison of the desialidation of the HA protein was made on MDCK and COS cells in the presence of bacterial NA and both cells were found to have similar sensitivity [16].
  • On the accumulation of the HA and NA proteins in the trans-Golgi network of MDCK cells by means of low-temperature treatment, desialidation of the HA protein in the presence of Zanamivir was detected by two-dimensional gel electrophoresis [16].
  • The advantage of this assay is that since different natural substrates for neuraminidase (erythrocytes, fetuin or gangliosides) can be used to coat the microplates, the capacity of anti-neuraminidase antibody to inhibit the neuraminidase activity towards different types of sialoglycoconjugates can be evaluated [17].

Associations of NA with chemical compounds

  • Sucrose gradient sedimentation and analysis of the structure of the mRNA by nuclease S1 mapping and sequence analysis by the primer extension method indicated that polypeptide NB and the neuraminidase are translated from a single bicistronic mRNA [9].
  • Inhibition of type A (N2) and type B NA activity by ePANA was approximately a 100-fold better than by sialic acid, but inhibition of type A (N9) NA was only ten-fold better than by sialic acid [18].
  • We also suggest that the removal of neuraminic acid from HA by NA is essential for the subsequent cleavage of HA by cellular protease [19].
  • A phosphonate analog of N-acetyl neuraminic acid (PANA) has been designed as a potential neuraminidase (NA) inhibitor and synthesized as both the alpha (ePANA) and beta (aPANA) anomers [18].
  • A zanamivir-resistant variant bearing a Glu119-to-Gly (Glu119-->Gly) or Glu119-->Ala substitution in an NA (N2) remained susceptible to RWJ-270201 and oseltamivir carboxylate [10].

Other interactions of NA

  • To improve the utility of the eight-plasmid system for generating 6 + 2 reassortants from recently circulating influenza B strains, we optimized the reverse transcriptase-PCR for cloning of the hemagglutinin (HA) and neuraminidase (NA) segments [20].
  • HA and NA DNAs conferred complete protection against the lethal viral challenge, whereas NB and NP DNAs failed to provide protection against infection [21].
  • Taken together, these results strongly suggest that BM2 is integrated into the plasma membrane at the N-terminal hydrophobic domain as fourth membrane protein, in addition to hemagglutinin, neuraminidase, and NB, of the influenza B virus [22].

Analytical, diagnostic and therapeutic context of NA


  1. Complete nucleotide sequence of the neuraminidase gene of influenza B virus. Shaw, M.W., Lamb, R.A., Erickson, B.W., Briedis, D.J., Choppin, P.W. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  2. Role of neuraminidase in the morphogenesis of influenza B virus. Yamamoto-Goshima, F., Maeno, K., Morishita, T., Ueda, M., Fujita, Y., Nakajima, K., Yoshii, S. J. Virol. (1994) [Pubmed]
  3. Selection of influenza A and B viruses for resistance to 4-guanidino-Neu5Ac2en in cell culture. Colacino, J.M., Laver, W.G., Air, G.M. J. Infect. Dis. (1997) [Pubmed]
  4. Influenza type B neuraminidase can replace the function of type A neuraminidase. Ghate, A.A., Air, G.M. Virology (1999) [Pubmed]
  5. Inhaled zanamivir for the prevention of influenza in families. Zanamivir Family Study Group. Hayden, F.G., Gubareva, L.V., Monto, A.S., Klein, T.C., Elliot, M.J., Hammond, J.M., Sharp, S.J., Ossi, M.J. N. Engl. J. Med. (2000) [Pubmed]
  6. Use of the selective oral neuraminidase inhibitor oseltamivir to prevent influenza. Hayden, F.G., Atmar, R.L., Schilling, M., Johnson, C., Poretz, D., Paar, D., Huson, L., Ward, P., Mills, R.G. N. Engl. J. Med. (1999) [Pubmed]
  7. Efficacy and safety of the neuraminidase inhibitor zanamivir in the treatment of influenzavirus infections. GG167 Influenza Study Group. Hayden, F.G., Osterhaus, A.D., Treanor, J.J., Fleming, D.M., Aoki, F.Y., Nicholson, K.G., Bohnen, A.M., Hirst, H.M., Keene, O., Wightman, K. N. Engl. J. Med. (1997) [Pubmed]
  8. The 2.2 A resolution crystal structure of influenza B neuraminidase and its complex with sialic acid. Burmeister, W.P., Ruigrok, R.W., Cusack, S. EMBO J. (1992) [Pubmed]
  9. A previously unrecognized influenza B virus glycoprotein from a bicistronic mRNA that also encodes the viral neuraminidase. Shaw, M.W., Choppin, P.W., Lamb, R.A. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  10. Comparison of the activities of zanamivir, oseltamivir, and RWJ-270201 against clinical isolates of influenza virus and neuraminidase inhibitor-resistant variants. Gubareva, L.V., Webster, R.G., Hayden, F.G. Antimicrob. Agents Chemother. (2001) [Pubmed]
  11. Recovery of drug-resistant influenza virus from immunocompromised patients: a case series. Ison, M.G., Gubareva, L.V., Atmar, R.L., Treanor, J., Hayden, F.G. J. Infect. Dis. (2006) [Pubmed]
  12. Sequence and crystallization of influenza virus B/Beijing/1/87 neuraminidase. Burmeister, W.P., Daniels, R.S., Dayan, S., Gagnon, J., Cusack, S., Ruigrok, R.W. Virology (1991) [Pubmed]
  13. Guanidinobenzoic acid inhibitors of influenza virus neuraminidase. Sudbeck, E.A., Jedrzejas, M.J., Singh, S., Brouillette, W.J., Air, G.M., Laver, W.G., Babu, Y.S., Bantia, S., Chand, P., Chu, N., Montgomery, J.A., Walsh, D.A., Luo, M. J. Mol. Biol. (1997) [Pubmed]
  14. Mutations in the cytoplasmic tail of influenza A virus neuraminidase affect incorporation into virions. Bilsel, P., Castrucci, M.R., Kawaoka, Y. J. Virol. (1993) [Pubmed]
  15. Immunogenic peptides of influenza virus subtype N1 neuraminidase identify a T-cell determinant used in class II major histocompatibility complex-restricted responses to infectious virus. Hackett, C.J., Horowitz, D., Wysocka, M., Eisenlohr, L.C. J. Virol. (1991) [Pubmed]
  16. Analysis of the desialidation process of the haemagglutinin protein of influenza B virus: the host-dependent desialidation step. Luo, C., Nobusawa, E., Nakajima, K. J. Gen. Virol. (2002) [Pubmed]
  17. Measurement of anti-influenza neuraminidase antibody using a peroxidase-linked lectin and microtitre plates coated with natural substrates. Lambré, C.R., Terzidis, H., Greffard, A., Webster, R.G. J. Immunol. Methods (1990) [Pubmed]
  18. A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies. White, C.L., Janakiraman, M.N., Laver, W.G., Philippon, C., Vasella, A., Air, G.M., Luo, M. J. Mol. Biol. (1995) [Pubmed]
  19. Characterization of a temperature-sensitive influenza B virus mutant defective in neuraminidase. Shibata, S., Yamamoto-Goshima, F., Maeno, K., Hanaichi, T., Fujita, Y., Nakajima, K., Imai, M., Komatsu, T., Sugiura, S. J. Virol. (1993) [Pubmed]
  20. Rescue of influenza B virus from eight plasmids. Hoffmann, E., Mahmood, K., Yang, C.F., Webster, R.G., Greenberg, H.B., Kemble, G. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  21. Protection against influenza B virus infection by immunization with DNA vaccines. Chen, Z., Kadowaki, S., Hagiwara, Y., Yoshikawa, T., Sata, T., Kurata, T., Tamura, S. Vaccine (2001) [Pubmed]
  22. Influenza B virus BM2 protein is transported through the trans-Golgi network as an integral membrane protein. Watanabe, S., Imai, M., Ohara, Y., Odagiri, T. J. Virol. (2003) [Pubmed]
  23. Comparison of structure and sequence of influenza B/Yamagata and B/Beijing neuraminidases shows a conserved "head" but much greater variability in the "stalk" and NB protein. Burmeister, W.P., Baudin, F., Cusack, S., Ruigrok, R.W. Virology (1993) [Pubmed]
  24. Molecular mechanisms of influenza virus resistance to neuraminidase inhibitors. Gubareva, L.V. Virus Res. (2004) [Pubmed]
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