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Gene Review

WSN  -  Waisman syndrome

Homo sapiens

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Disease relevance of WSN

  • We then systematically introduced point mutations into evolutionarily conserved amino acids in the N-terminal region of influenza virus A/WSN/33 [1].
  • Antiserum to NS1 isolated from cells infected with A/WSN/33 virus specifically precipitated NS1 from extracts of cells infected with seven distinct isolates of influenza A virus representing five different antigenic subtypes [2].
  • We have replaced the late genes of simian virus 40 (SV40) with a cloned cDNA copy of the neuraminidase (NA; EC gene of the WSN (H1N1) strain of human influenza virus [3].
  • Superinfection with helper virus lacking the WSN NA gene resulted in the release of virus containing the WSN NA gene [4].
  • We also used this eight-plasmid system for the generation of single and quadruple reassortant viruses between A/Teal/HK/W312/97 (H6N1) and A/WSN/33 (H1N1) [5].

Psychiatry related information on WSN


High impact information on WSN

  • Using reverse genetics, we generated a mutant of strain A/WSN/33 with a modified cleavage site within its hemagglutinin, which depends on proteolytic activation by elastase [7].
  • To synchronize the migration, we used a temperature-sensitive mutant of influenza WSN, ts61, which, at the nonpermissive temperature, 39.5 degrees C, exhibits a defect in the HA that prevents its exit from the endoplasmic reticulum [8].
  • ISG15(-/-) mice are more susceptible to influenza A/WSN/33 and influenza B/Lee/40 virus infections [9].
  • RNA corresponding to the neuraminidase (NA) gene of influenza A/WSN/33 (WSN) virus was transcribed in vitro from plasmid DNA and, following the addition of purified influenza virus RNA polymerase complex, was transfected into MDBK cells [4].
  • We then introduced five point mutations into the WSN NA gene by cassette mutagenesis of the plasmid DNA [4].

Chemical compound and disease context of WSN

  • These antibodies were not elicited by other influenza A or B viruses, including closely related recombinant strains, but were elicited by the isolated hemagglutinin of A/Bellamy/42 strain and by formaldehyde-fixed WSN virus--demonstrating that infection was not essential for the induction of autoantibodies [10].
  • We have investigated the effect of amantadine on the growth of four influenza viruses: A/WSN/33; N31S-M2WSN, a mutant in which an asparagine residue at position 31 in the M2 TM domain was replaced with a serine residue; MUd/WSN, which possesses seven RNA segments from WSN plus the RNA segment 7 derived from A/Udorn/72; and A/Udorn/72 [11].
  • The internal ribonucleoproteins of influenza C virions were found to sediment heterogeneously in glycerol velocity gradients as demonstrated previously with influenza A/WSN virus [12].
  • Cloned DNA fragments coding for parts of strain WSN (H1N1) influenza virus hemagglutinin (HA) were fused to a bacterial leader DNA derived from the Escherichia coli trp operon [13].
  • The effect of the beta-lactone antibiotic diffusomycin (oxazolomycin) was investigated against vaccinia (Lister), herpes simplex type 1 (Kupka), influenza A (WSN; H1N1), and Coxsackie A9 viruses [14].

Biological context of WSN

  • We have cloned and expressed the hemagglutinin (HA) gene of a human influenza virus (A/WSN/33) in monkey kidney cells by linking it to deleted simian virus 40 (SV40) genomes that contain the entire early gene region, the origin of replication, and late leader sequences [15].
  • Nucleotide sequence of the PA gene of influenza A/WSN/33(H1N1) [16].
  • Comparison with the gene sequence for the N1 strains A/WSN/33 and A/PR/8/34, the N2 strain A/Udorn/72 and the protein sequence for the N2 strain A/Tokyo/3/67 shows the amino acid sequence changes that have occurred during antigenic shift (60%) and drift (7-9%) [17].
  • The possible significance of these sequence changes in the primary structure of WSN NA in the unique role of WSN NA as a virulence factor in mouse brain and MDBK cells is discussed [18].
  • Introduction of a temperature-sensitive phenotype into influenza A/WSN/33 virus by altering the basic amino acid domain of influenza virus matrix protein [19].

Anatomical context of WSN

  • WSN (H0N1) influenza virus upon undiluted passages in different species of cells, namely, bovine kidney (MDBK), chicken embryo (CEF), and HeLa cells, produced a varying amount of defective interfering (DI) virus which correlated well with the ability of the species of cell to produce infectious virus [20].
  • Enzymatic activities of WSN/Stable-NAs were detected in endosomes of MDCK cells after 90 min of virus internalization by in situ fluorescent detection with 5-bromo-4-chloro-indole-3-yl-alpha-N-acetylneuraminic acid and Fast Red Violet LB [21].
  • Proteolytic cleavage of the hemagglutinin (HA) of human influenza viruses A/Aichi/2/68 (H3N2) and A/WSN/34 (H1N1) from HA0 to HA1/HA2 was studied in primary human adenoid epithelial cells (HAEC) [22].
  • These results indicate that the abortive replication of influenza virus A/WSN/33 in HeLa229 cells appears to be due to multiple defects involving both the entry and release of viral particles and that host cell membrane and microfilaments may be important contributing factors in these processes [23].
  • WSN virus-infected KB cells synthesized normal amounts of mature virus particles and had all the characteristics of a permissive replication cycle [24].

Associations of WSN with chemical compounds

  • In contrast, the enzymatic activities of WSN/Unstable-NAs, the replication of which had no effect on pretreatment with zanamivir, were undetectable in cells under the same conditions [21].
  • N31S-M2WSN was amantadine sensitive, whereas A/WSN/33 was amantadine resistant, indicating that the M2 residue N31 is the sole determinant of resistance of A/WSN/33 to amantadine [11].
  • Furthermore, early in the infectious cycle in WSN-infected cells, M1 acquired TX-100 resistance very slowly after a long chase and did not acquire TX-100 resistance at all when chased in the presence of cycloheximide [25].
  • When compared with the PR8 NA sequence, WSN NA appeared to possess a similar structure, including the identical location of all cysteine and proline residues [18].
  • Glycosylation sites of influenza viral glycoproteins. Tryptic glycopeptides from the A/WSN (H0N1) hemagglutinin glycoprotein [26].

Regulatory relationships of WSN


Other interactions of WSN

  • Here we demonstrate, through the use of dominant-negative Rab5 and Rab7, that influenza virus (Influenza A/WSN/33 (H1N1) and A/X-31 (H3N2)) requires both early and late endosomes for entry and subsequent infection in HeLa cells [28].
  • Analysis of the signals for polarized transport of influenza virus (A/WSN/33) neuraminidase and human transferrin receptor, type II transmembrane proteins [29].
  • By complementation tests against a set of prototype WSN ts mutants with a defined genetic lesion, the ts lesion of two H3N2 viruses (HK/8/68 and Xia-ts) was located on the NP gene and that of two H1N1 viruses (Tianjin/78/77 and Beijing/1/79) was located on the M protein gene [30].
  • Here we show that amounts of radiolabeled M1 protein in lysates of MEB cultures infected with PR8, WS, or WSN differ in proportion to previously reported single-cycle yields of trypsin-activated infectious virions [31].
  • The kinetics of biosynthesis of NA, including modification of N-linked sugar chains, association with GRP78-BiP, oligomerization, and transport to the cell surface, were examined in A/WSN/33 influenza-infected BHK cells [32].

Analytical, diagnostic and therapeutic context of WSN


  1. Amino acid residues in the N-terminal region of the PA subunit of influenza A virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding. Hara, K., Schmidt, F.I., Crow, M., Brownlee, G.G. J. Virol. (2006) [Pubmed]
  2. Immunologic studies on the influenza A virus nonstructural protein NS1. Shaw, M.W., Lamon, E.W., Compans, R.W. J. Exp. Med. (1982) [Pubmed]
  3. Active influenza virus neuraminidase is expressed in monkey cells from cDNA cloned in simian virus 40 vectors. Davis, A.R., Bos, T.J., Nayak, D.P. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  4. Introduction of site-specific mutations into the genome of influenza virus. Enami, M., Luytjes, W., Krystal, M., Palese, P. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  5. A DNA transfection system for generation of influenza A virus from eight plasmids. Hoffmann, E., Neumann, G., Kawaoka, Y., Hobom, G., Webster, R.G. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  6. Waisman syndrome, a human X-linked recessive basal ganglia disorder with mental retardation: localization to Xq27.3-qter. Gregg, R.G., Metzenberg, A.B., Hogan, K., Sekhon, G., Laxova, R. Genomics (1991) [Pubmed]
  7. A new approach to an influenza live vaccine: modification of the cleavage site of hemagglutinin. Stech, J., Garn, H., Wegmann, M., Wagner, R., Klenk, H.D. Nat. Med. (2005) [Pubmed]
  8. Intracellular transport of influenza virus hemagglutinin to the apical surface of Madin-Darby canine kidney cells. Rodriguez-Boulan, E., Paskiet, K.T., Salas, P.J., Bard, E. J. Cell Biol. (1984) [Pubmed]
  9. From the cover: IFN-stimulated gene 15 functions as a critical antiviral molecule against influenza, herpes, and Sindbis viruses. Lenschow, D.J., Lai, C., Frias-Staheli, N., Giannakopoulos, N.V., Lutz, A., Wolff, T., Osiak, A., Levine, B., Schmidt, R.E., García-Sastre, A., Leib, D.A., Pekosz, A., Knobeloch, K.P., Horak, I., Virgin, H.W. Proc. Natl. Acad. Sci. U.S.A. (2007) [Pubmed]
  10. Influenza viruses induce autoantibodies to a brain-specific 37-kDa protein in rabbit. Laing, P., Knight, J.G., Hill, J.M., Harris, A.G., Oxford, J.S., Webster, R.G., Markwell, M.A., Paul, S.M., Pert, C.B. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  11. Influenza a virus M2 ion channel activity is essential for efficient replication in tissue culture. Takeda, M., Pekosz, A., Shuck, K., Pinto, L.H., Lamb, R.A. J. Virol. (2002) [Pubmed]
  12. Structural components of influenza C virions. Compans, R.W., Bishop, D.H., Meier-Ewert, H. J. Virol. (1977) [Pubmed]
  13. Immune response to human influenza virus hemagglutinin expressed in Escherichia coli. Davis, A.R., Bos, T., Ueda, M., Nayak, D.P., Dowbenko, D., Compans, R.W. Gene (1983) [Pubmed]
  14. On the antiviral activity of diffusomycin (oxazolomycin). Tonew, E., Tonew, M., Gräfe, U., Zöpel, P. Acta Virol. (1992) [Pubmed]
  15. Human influenza virus hemagglutinin is expressed in monkey cells using simian virus 40 vectors. Hartman, J.R., Nayak, D.P., Fareed, G.C. Proc. Natl. Acad. Sci. U.S.A. (1982) [Pubmed]
  16. Nucleotide sequence of the PA gene of influenza A/WSN/33(H1N1). Odagiri, T., Tobita, K. Nucleic Acids Res. (1990) [Pubmed]
  17. Neuraminidase gene from the early Asian strain of human influenza virus, A/RI/5-/57 (H2N2). Elleman, T.C., Azad, A.A., Ward, C.W. Nucleic Acids Res. (1982) [Pubmed]
  18. Complete nucleotide sequence of the neuraminidase gene of human influenza virus A/WSN/33. Hiti, A.L., Nayak, D.P. J. Virol. (1982) [Pubmed]
  19. Introduction of a temperature-sensitive phenotype into influenza A/WSN/33 virus by altering the basic amino acid domain of influenza virus matrix protein. Liu, T., Ye, Z. J. Virol. (2004) [Pubmed]
  20. Defective interfering influenza viruses and host cells: establishment and maintenance of persistent influenza virus infection in MDBK and HeLa cells. De, B.K., Nayak, D.P. J. Virol. (1980) [Pubmed]
  21. Sialidase activity of influenza A virus in an endocytic pathway enhances viral replication. Suzuki, T., Takahashi, T., Guo, C.T., Hidari, K.I., Miyamoto, D., Goto, H., Kawaoka, Y., Suzuki, Y. J. Virol. (2005) [Pubmed]
  22. Cleavage of influenza a virus hemagglutinin in human respiratory epithelium is cell associated and sensitive to exogenous antiproteases. Zhirnov, O.P., Ikizler, M.R., Wright, P.F. J. Virol. (2002) [Pubmed]
  23. Abortive replication of influenza virus A/WSN/33 in HeLa229 cells: defective viral entry and budding processes. Gujuluva, C.N., Kundu, A., Murti, K.G., Nayak, D.P. Virology (1994) [Pubmed]
  24. Different patterns of replication in influenza virus-infected KB cells. Conti, G., Valcavi, P., Natali, A., Schito, G.C. Arch. Virol. (1980) [Pubmed]
  25. Association of influenza virus NP and M1 proteins with cellular cytoskeletal elements in influenza virus-infected cells. Avalos, R.T., Yu, Z., Nayak, D.P. J. Virol. (1997) [Pubmed]
  26. Glycosylation sites of influenza viral glycoproteins. Tryptic glycopeptides from the A/WSN (H0N1) hemagglutinin glycoprotein. Nakamura, K., Bhown, A.S., Compans, R.W. Virology (1980) [Pubmed]
  27. Direct inactivation of viruses by human granulocyte defensins. Daher, K.A., Selsted, M.E., Lehrer, R.I. J. Virol. (1986) [Pubmed]
  28. Differential requirements of Rab5 and Rab7 for endocytosis of influenza and other enveloped viruses. Sieczkarski, S.B., Whittaker, G.R. Traffic (2003) [Pubmed]
  29. Analysis of the signals for polarized transport of influenza virus (A/WSN/33) neuraminidase and human transferrin receptor, type II transmembrane proteins. Kundu, A., Nayak, D.P. J. Virol. (1994) [Pubmed]
  30. Occurrence of temperature-sensitive influenza A viruses in nature. Chu, C.M., Tian, S.F., Ren, G.F., Zhang, Y.M., Zhang, L.X., Liu, G.Q. J. Virol. (1982) [Pubmed]
  31. Replication of H1N1 influenza viruses in cultured mouse embryo brain cells: virus strain and cell differentiation affect synthesis of proteins encoded in RNA segments 7 and 8 and efficiency of mRNA splicing. Bradshaw, G.L., Schwartz, C.D., Schlesinger, R.W. Virology (1990) [Pubmed]
  32. Synthesis and processing of the influenza virus neuraminidase, a type II transmembrane glycoprotein. Hogue, B.G., Nayak, D.P. Virology (1992) [Pubmed]
  33. Sequence analysis of the polymerase 1 gene and the secondary structure prediction of polymerase 1 protein of human influenza virus A/WSN/33. Sivasubramanian, N., Nayak, D.P. J. Virol. (1982) [Pubmed]
  34. Association of influenza virus matrix protein with ribonucleoproteins. Ye, Z., Liu, T., Offringa, D.P., McInnis, J., Levandowski, R.A. J. Virol. (1999) [Pubmed]
  35. Antigenic variation in the influenza A virus nonstructural protein, NS1. Brown, L.E., Hinshaw, V.S., Webster, R.G. Virology (1983) [Pubmed]
  36. The generation of recombinant influenza A viruses expressing a PB2 fusion protein requires the conservation of a packaging signal overlapping the coding and noncoding regions at the 5' end of the PB2 segment. Dos Santos Afonso, E., Escriou, N., Leclercq, I., van der Werf, S., Naffakh, N. Virology (2005) [Pubmed]
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