메뉴 건너뛰기




Volumn 175, Issue 2, 2011, Pages 175-181

Novel post-translational modifications of the hemagglutinin and neuraminidase proteins of avian influenza virus expressed by Kluyveromyces lactis

Author keywords

Avian influenza virus; HA and NA proteins; Kluyveromyces lactis

Indexed keywords

INFLUENZA VIRUS HEMAGGLUTININ; VIRUS SIALIDASE;

EID: 79959358915     PISSN: 01660934     EISSN: 18790984     Source Type: Journal    
DOI: 10.1016/j.jviromet.2011.05.006     Document Type: Article
Times cited : (4)

References (23)
  • 1
    • 0025313449 scopus 로고
    • Isolation, characterization and properties of Saccharomyces cerevisae mnn mutants with nonconditional protein glycosylation defects
    • Ballou C.E. Isolation, characterization and properties of Saccharomyces cerevisae mnn mutants with nonconditional protein glycosylation defects. Methods Enzymol. 1990, 185:440-476.
    • (1990) Methods Enzymol. , vol.185 , pp. 440-476
    • Ballou, C.E.1
  • 2
    • 33748950305 scopus 로고    scopus 로고
    • Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium
    • Bottcher E., Matrosovich T., Beyerle M., Klenk H., Garten W., Matrosovich M. Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium. J. Virol. 2006, 80:9896-9898.
    • (2006) J. Virol. , vol.80 , pp. 9896-9898
    • Bottcher, E.1    Matrosovich, T.2    Beyerle, M.3    Klenk, H.4    Garten, W.5    Matrosovich, M.6
  • 8
    • 0024396988 scopus 로고
    • Interplay between carbohydrate in the stalk and the length of the connecting peptide determines the cleavability of influenza virus hemagglutinin
    • Kawaoka Y., Webster R.G. Interplay between carbohydrate in the stalk and the length of the connecting peptide determines the cleavability of influenza virus hemagglutinin. J. Virol. 1989, 63:3296-3300.
    • (1989) J. Virol. , vol.63 , pp. 3296-3300
    • Kawaoka, Y.1    Webster, R.G.2
  • 9
    • 7644241814 scopus 로고    scopus 로고
    • Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium
    • Matrosovich M.N., Matrosovichi T.Y., Gray T., Roberts N.A., Klenk H.D. Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium. J. Virol. 2004, 78:12665-12667.
    • (2004) J. Virol. , vol.78 , pp. 12665-12667
    • Matrosovich, M.N.1    Matrosovichi, T.Y.2    Gray, T.3    Roberts, N.A.4    Klenk, H.D.5
  • 10
    • 25144469371 scopus 로고    scopus 로고
    • Effect of hemagglutinin glycosylation on influenza virus susceptibility to neuraminidase inhibitors
    • Mishin V.P., Novikov D., Hayden F.G., Gubareva L.V. Effect of hemagglutinin glycosylation on influenza virus susceptibility to neuraminidase inhibitors. J. Virol. 2005, 79:12416-12424.
    • (2005) J. Virol. , vol.79 , pp. 12416-12424
    • Mishin, V.P.1    Novikov, D.2    Hayden, F.G.3    Gubareva, L.V.4
  • 11
    • 34548254386 scopus 로고    scopus 로고
    • Acetamide selection of Kluyveromyces lactis cells transformed with an integrative vector leads to high-frequency formation of multicopy strains
    • Read J.D., Colussi P.A., Ganatra M.B., Taron C.H. Acetamide selection of Kluyveromyces lactis cells transformed with an integrative vector leads to high-frequency formation of multicopy strains. Appl. Environ. Microbiol. 2007, 73:5088-5096.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 5088-5096
    • Read, J.D.1    Colussi, P.A.2    Ganatra, M.B.3    Taron, C.H.4
  • 13
    • 77954056442 scopus 로고    scopus 로고
    • Enhancement of the influenza A hemagglutinin HA-mediated cell-cell fusion and virus entry by the viral neuraminidase (NA)
    • Su B., Wurtzer S., Rameix-Welti M., Dwyer D., van der Werf S., Naffakh N., Clavel F., Labrosse B. Enhancement of the influenza A hemagglutinin HA-mediated cell-cell fusion and virus entry by the viral neuraminidase (NA). PLoS One 2009, 4:e8495.
    • (2009) PLoS One , vol.4
    • Su, B.1    Wurtzer, S.2    Rameix-Welti, M.3    Dwyer, D.4    van der Werf, S.5    Naffakh, N.6    Clavel, F.7    Labrosse, B.8
  • 15
    • 1542285487 scopus 로고    scopus 로고
    • Characterization of N- and O-linked glycosylation of recombinant human bile salt-stimulated lipase secreted by Pichia pastoris
    • Trimble R.B., Lubowski C., Hauer C.R., Stack R., McNaughton L., Gemmill T.R., Kumar S.A. Characterization of N- and O-linked glycosylation of recombinant human bile salt-stimulated lipase secreted by Pichia pastoris. Glycobiology 2004, 14:265-274.
    • (2004) Glycobiology , vol.14 , pp. 265-274
    • Trimble, R.B.1    Lubowski, C.2    Hauer, C.R.3    Stack, R.4    McNaughton, L.5    Gemmill, T.R.6    Kumar, S.A.7
  • 16
    • 33645981934 scopus 로고    scopus 로고
    • The kluyveromyces lactis α1,6-mannosyltransferase KlOch1p is required for cell-wall organization and proper functioning of the secretary pathway
    • Ucelletti D., Farina F., Rufini S., Magnelli P., Abeijon C., Palleschi C. The kluyveromyces lactis α1,6-mannosyltransferase KlOch1p is required for cell-wall organization and proper functioning of the secretary pathway. FEMS Yeast Res. 2006, 6:449-457.
    • (2006) FEMS Yeast Res. , vol.6 , pp. 449-457
    • Ucelletti, D.1    Farina, F.2    Rufini, S.3    Magnelli, P.4    Abeijon, C.5    Palleschi, C.6
  • 17
    • 70350335336 scopus 로고    scopus 로고
    • Detection of NP, N3 and N7 antibodies to avain influenza virus by indirect ELISA using yeast-expressed antigens
    • Upadhyay C., Ammayappan A., Vakharia V.N. Detection of NP, N3 and N7 antibodies to avain influenza virus by indirect ELISA using yeast-expressed antigens. Virol. J. 2009, 6:158.
    • (2009) Virol. J. , vol.6 , pp. 158
    • Upadhyay, C.1    Ammayappan, A.2    Vakharia, V.N.3
  • 19
    • 0027355666 scopus 로고
    • Deduced amino acid sequences at the hemagglutinin cleavage site of avian influenza A viruses of H5 and H7 subtypes
    • Wood G.W., McCauley J.W., Bashiruddin J.B., Alexander D.J. Deduced amino acid sequences at the hemagglutinin cleavage site of avian influenza A viruses of H5 and H7 subtypes. Arch. Virol. 1993, 130:209-217.
    • (1993) Arch. Virol. , vol.130 , pp. 209-217
    • Wood, G.W.1    McCauley, J.W.2    Bashiruddin, J.B.3    Alexander, D.J.4
  • 21
    • 0031550787 scopus 로고    scopus 로고
    • Hemagglutinin specificity and neuraminidase coding capacity of neuraminidase-deficient influenza viruses
    • Yang P., Bansal A., Liu C., Air G.M. Hemagglutinin specificity and neuraminidase coding capacity of neuraminidase-deficient influenza viruses. Virology 1997, 229:155-165.
    • (1997) Virology , vol.229 , pp. 155-165
    • Yang, P.1    Bansal, A.2    Liu, C.3    Air, G.M.4
  • 22
    • 34247235806 scopus 로고    scopus 로고
    • Display of avian influenza virus hemagglutinin on baculovirus envelope: effect of cytoplasmic domain on virus properties and potentials as vaccine
    • Yang D.G., Chung Y.C., Lai Y.K., Lai C.W., Liu H.J., Hu Y.C. Display of avian influenza virus hemagglutinin on baculovirus envelope: effect of cytoplasmic domain on virus properties and potentials as vaccine. Mol. Ther. 2007, 15(5):989-996.
    • (2007) Mol. Ther. , vol.15 , Issue.5 , pp. 989-996
    • Yang, D.G.1    Chung, Y.C.2    Lai, Y.K.3    Lai, C.W.4    Liu, H.J.5    Hu, Y.C.6
  • 23
    • 37449008244 scopus 로고    scopus 로고
    • Development and application of monoclonal antibodies against avian influenza virus nucleoprotein
    • Yang M., Berhane Y., Salo T., Li M., Hole K., Clavijo A. Development and application of monoclonal antibodies against avian influenza virus nucleoprotein. J. Virol. Methods 2008, 147:265-274.
    • (2008) J. Virol. Methods , vol.147 , pp. 265-274
    • Yang, M.1    Berhane, Y.2    Salo, T.3    Li, M.4    Hole, K.5    Clavijo, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.