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Volumn 174, Issue 1-2, 2013, Pages 137-147

Role of N-linked glycosylation of the human parainfluenza virus type 3 hemagglutinin-neuraminidase protein

Author keywords

Hemagglutinin neuraminidase protein; Hemagglutinin neuraminidase fusion protein complexes; Human parainfluenza virus type 3; Membrane fusion; Mutations; N linked glycosylation sites

Indexed keywords

CARBOHYDRATE; GLYCAN; HN PROTEIN; MUTANT PROTEIN; PROTEIN ANTIBODY; VIRUS SIALIDASE;

EID: 84877595007     PISSN: 01681702     EISSN: 18727492     Source Type: Journal    
DOI: 10.1016/j.virusres.2013.03.012     Document Type: Article
Times cited : (24)

References (47)
  • 1
    • 4444376554 scopus 로고    scopus 로고
    • Effect of the addition of oligosaccharides on the biological activities and antigenicity of influenza A/H3N2 virus hemagglutinin
    • Abe Y., Takashita E., Sugawara K., Matsuzaki Y., Muraki Y., Hongo S. Effect of the addition of oligosaccharides on the biological activities and antigenicity of influenza A/H3N2 virus hemagglutinin. Journal of Virology 2004, 78(18):9605-9611.
    • (2004) Journal of Virology , vol.78 , Issue.18 , pp. 9605-9611
    • Abe, Y.1    Takashita, E.2    Sugawara, K.3    Matsuzaki, Y.4    Muraki, Y.5    Hongo, S.6
  • 3
    • 73049171244 scopus 로고
    • Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids
    • Aminoff D. Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids. Biochemical Journal 1961, 81:384-392.
    • (1961) Biochemical Journal , vol.81 , pp. 384-392
    • Aminoff, D.1
  • 4
    • 0028883780 scopus 로고
    • Quantitative measurement of paramyxovirus fusion: differences in requirements of glycoproteins between simian virus 5 and human parainfluenza virus 3 or Newcastle disease virus
    • Bagai S., Lamb R.A. Quantitative measurement of paramyxovirus fusion: differences in requirements of glycoproteins between simian virus 5 and human parainfluenza virus 3 or Newcastle disease virus. Journal of Virology 1995, 69(11):6712-6719.
    • (1995) Journal of Virology , vol.69 , Issue.11 , pp. 6712-6719
    • Bagai, S.1    Lamb, R.A.2
  • 5
    • 3242724918 scopus 로고    scopus 로고
    • Role of nucleolin in human parainfluenza virus type 3 infection of human lung epithelial cells
    • Bose S., Basu M., Banerjee A.K. Role of nucleolin in human parainfluenza virus type 3 infection of human lung epithelial cells. Journal of Virology 2004, 78(15):8146-8158.
    • (2004) Journal of Virology , vol.78 , Issue.15 , pp. 8146-8158
    • Bose, S.1    Basu, M.2    Banerjee, A.K.3
  • 6
    • 19944415289 scopus 로고    scopus 로고
    • Role of N-linked glycosylation of the Hendra virus fusion protein
    • Carter J.R., Pager C.T., Fowler S.D., Dutch R.E. Role of N-linked glycosylation of the Hendra virus fusion protein. Journal of Virology 2005, 79(12):7922-7925.
    • (2005) Journal of Virology , vol.79 , Issue.12 , pp. 7922-7925
    • Carter, J.R.1    Pager, C.T.2    Fowler, S.D.3    Dutch, R.E.4
  • 7
    • 84870350334 scopus 로고    scopus 로고
    • 'a'-position-mutated and G4-mutated hemagglutinin-neuraminidase proteins of Newcastle disease virus impair fusion and hemagglutinin-neuraminidase-fusion interaction by different mechanisms
    • Chu F.-L., Wen H.-L., Zhang W.-Q., Lin B., Zhang Y., Sun C.-X., Ren G.-J., Song Y.-Y., Wang Z. 'a'-position-mutated and G4-mutated hemagglutinin-neuraminidase proteins of Newcastle disease virus impair fusion and hemagglutinin-neuraminidase-fusion interaction by different mechanisms. Intervirology 2013, 56(1):27-36.
    • (2013) Intervirology , vol.56 , Issue.1 , pp. 27-36
    • Chu, F.-L.1    Wen, H.-L.2    Zhang, W.-Q.3    Lin, B.4    Zhang, Y.5    Sun, C.-X.6    Ren, G.-J.7    Song, Y.-Y.8    Wang, Z.9
  • 8
    • 35348888403 scopus 로고    scopus 로고
    • Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein
    • Corey E.A., Iorio R.M. Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein. Journal of Virology 2007, 81(18):9900-9910.
    • (2007) Journal of Virology , vol.81 , Issue.18 , pp. 9900-9910
    • Corey, E.A.1    Iorio, R.M.2
  • 9
    • 0344304689 scopus 로고    scopus 로고
    • Role of the cytoplasmic domain of the Newcastle disease virus fusion protein in association with lipid rafts
    • Dolganiuc V., McGinnes L., Luna E.J., Morrison T.G. Role of the cytoplasmic domain of the Newcastle disease virus fusion protein in association with lipid rafts. Journal of Virology 2003, 77(24):12968-12979.
    • (2003) Journal of Virology , vol.77 , Issue.24 , pp. 12968-12979
    • Dolganiuc, V.1    McGinnes, L.2    Luna, E.J.3    Morrison, T.G.4
  • 11
    • 0031664797 scopus 로고    scopus 로고
    • Membrane fusion promoted by increasing surface densities of the paramyxovirus F and HN proteins: comparison of fusion reactions mediated by simian virus 5 F, human parainfluenza virus type 3 F, and influenza virus HA
    • Dutch R.E., Joshi S.B., Lamb R.A. Membrane fusion promoted by increasing surface densities of the paramyxovirus F and HN proteins: comparison of fusion reactions mediated by simian virus 5 F, human parainfluenza virus type 3 F, and influenza virus HA. Journal of Virology 1998, 72(10):7745-7753.
    • (1998) Journal of Virology , vol.72 , Issue.10 , pp. 7745-7753
    • Dutch, R.E.1    Joshi, S.B.2    Lamb, R.A.3
  • 12
    • 0022638538 scopus 로고
    • Human parainfluenza type 3 virus hemagglutinin-neuraminidase glycoprotein: nucleotide sequence of mRNA and limited amino acid sequence of the purified protein
    • Elango N., Coligan J.E., Jambou R.C., Venkatesan S. Human parainfluenza type 3 virus hemagglutinin-neuraminidase glycoprotein: nucleotide sequence of mRNA and limited amino acid sequence of the purified protein. Journal of Virology 1986, 57(2):481-489.
    • (1986) Journal of Virology , vol.57 , Issue.2 , pp. 481-489
    • Elango, N.1    Coligan, J.E.2    Jambou, R.C.3    Venkatesan, S.4
  • 13
    • 34147180914 scopus 로고    scopus 로고
    • N-linked glycosylation of Gn (but not Gc) is important for Crimean Congo hemorrhagic fever virus glycoprotein localization and transport
    • Erickson B.R., Deyde V., Sanchez A.J., Vincent M.J., Nichol S.T. N-linked glycosylation of Gn (but not Gc) is important for Crimean Congo hemorrhagic fever virus glycoprotein localization and transport. Virology 2007, 361(2):348-355.
    • (2007) Virology , vol.361 , Issue.2 , pp. 348-355
    • Erickson, B.R.1    Deyde, V.2    Sanchez, A.J.3    Vincent, M.J.4    Nichol, S.T.5
  • 17
    • 0026525004 scopus 로고
    • Functional interactions between the fusion protein and hemagglutinin-neuraminidase of human parainfluenza viruses
    • Hu X.L., Ray R., Compans R.W. Functional interactions between the fusion protein and hemagglutinin-neuraminidase of human parainfluenza viruses. Journal of Virology 1992, 66(3):1529-1534.
    • (1992) Journal of Virology , vol.66 , Issue.3 , pp. 1529-1534
    • Hu, X.L.1    Ray, R.2    Compans, R.W.3
  • 18
    • 39549123459 scopus 로고    scopus 로고
    • Lentiviruses inefficiently incorporate human parainfluenza type 3 envelope proteins
    • Jung C., Le Doux J.M. Lentiviruses inefficiently incorporate human parainfluenza type 3 envelope proteins. Biotechnology and Bioengineering 2008, 99(4):1016-1027.
    • (2008) Biotechnology and Bioengineering , vol.99 , Issue.4 , pp. 1016-1027
    • Jung, C.1    Le Doux, J.M.2
  • 19
    • 49149112340 scopus 로고    scopus 로고
    • A single N-linked glycosylation site in the Japanese encephalitis virus prM protein is critical for cell type-specific prM protein biogenesis, virus particle release, and pathogenicity in mice
    • Kim J.M., Yun S.I., Song B.H., Hahn Y.S., Lee C.H., Oh H.W., Lee Y.M. A single N-linked glycosylation site in the Japanese encephalitis virus prM protein is critical for cell type-specific prM protein biogenesis, virus particle release, and pathogenicity in mice. Journal of Virology 2008, 82(16):7846-7862.
    • (2008) Journal of Virology , vol.82 , Issue.16 , pp. 7846-7862
    • Kim, J.M.1    Yun, S.I.2    Song, B.H.3    Hahn, Y.S.4    Lee, C.H.5    Oh, H.W.6    Lee, Y.M.7
  • 22
    • 21244502470 scopus 로고    scopus 로고
    • Novel innate immune functions for galectin-1: galectin-1 inhibits cell fusion by Nipah virus envelope glycoproteins and augments dendritic cell secretion of proinflammatory cytokines
    • Levroney E.L., Aguilar H.C., Fulcher J.A., Kohatsu L., Pace K.E., Pang M., Gurney K.B., Baum L.G., Lee B. Novel innate immune functions for galectin-1: galectin-1 inhibits cell fusion by Nipah virus envelope glycoproteins and augments dendritic cell secretion of proinflammatory cytokines. Journal of Immunology 2005, 175(1):413-420.
    • (2005) Journal of Immunology , vol.175 , Issue.1 , pp. 413-420
    • Levroney, E.L.1    Aguilar, H.C.2    Fulcher, J.A.3    Kohatsu, L.4    Pace, K.E.5    Pang, M.6    Gurney, K.B.7    Baum, L.G.8    Lee, B.9
  • 23
    • 2342512265 scopus 로고    scopus 로고
    • Mutated form of the Newcastle disease virus hemagglutinin-neuraminidase interacts with the homologous fusion protein despite deficiencies in both receptor recognition and fusion promotion
    • Li J., Quinlan E., Mirza A., Iorio R.M. Mutated form of the Newcastle disease virus hemagglutinin-neuraminidase interacts with the homologous fusion protein despite deficiencies in both receptor recognition and fusion promotion. Journal of Virology 2004, 78(10):5299-5310.
    • (2004) Journal of Virology , vol.78 , Issue.10 , pp. 5299-5310
    • Li, J.1    Quinlan, E.2    Mirza, A.3    Iorio, R.M.4
  • 24
    • 0028858321 scopus 로고
    • The role of individual oligosaccharide chains in the activities of the HN glycoprotein of Newcastle disease virus
    • McGinnes L.W., Morrison T.G. The role of individual oligosaccharide chains in the activities of the HN glycoprotein of Newcastle disease virus. Virology 1995, 212(2):398-410.
    • (1995) Virology , vol.212 , Issue.2 , pp. 398-410
    • McGinnes, L.W.1    Morrison, T.G.2
  • 25
    • 8644256749 scopus 로고    scopus 로고
    • Amino acid substitutions in the F-specific domain in the stalk of the Newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein
    • Melanson V.R., Iorio R.M. Amino acid substitutions in the F-specific domain in the stalk of the Newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein. Journal of Virology 2004, 78(23):13053-13061.
    • (2004) Journal of Virology , vol.78 , Issue.23 , pp. 13053-13061
    • Melanson, V.R.1    Iorio, R.M.2
  • 26
    • 30344467852 scopus 로고    scopus 로고
    • Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion
    • Melanson V.R., Iorio R.M. Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion. Journal of Virology 2006, 80(2):623-633.
    • (2006) Journal of Virology , vol.80 , Issue.2 , pp. 623-633
    • Melanson, V.R.1    Iorio, R.M.2
  • 27
    • 77649103933 scopus 로고    scopus 로고
    • N-Linked Glycan at residue 523 of human parainfluenza virus type 3 hemagglutinin-neuraminidase masks a second receptor-binding site
    • Mishin V.P., Watanabe M., Taylor G., DeVincenzo J., Bose M., Portner A., Alymova I.V. N-Linked Glycan at residue 523 of human parainfluenza virus type 3 hemagglutinin-neuraminidase masks a second receptor-binding site. Journal of Virology 2010, 84(6):3094-3100.
    • (2010) Journal of Virology , vol.84 , Issue.6 , pp. 3094-3100
    • Mishin, V.P.1    Watanabe, M.2    Taylor, G.3    DeVincenzo, J.4    Bose, M.5    Portner, A.6    Alymova, I.V.7
  • 28
    • 0024564649 scopus 로고
    • Kinetics of pH-dependent fusion between 3T3 fibroblasts expressing influenza hemagglutinin and red blood cells. measurement by dequenching of fluorescence
    • Morris S.J., Sarkar D.P., White J.M., Blumenthal R. Kinetics of pH-dependent fusion between 3T3 fibroblasts expressing influenza hemagglutinin and red blood cells. measurement by dequenching of fluorescence. Journal of Biological Chemistry 1989, 264(7):3972-3978.
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.7 , pp. 3972-3978
    • Morris, S.J.1    Sarkar, D.P.2    White, J.M.3    Blumenthal, R.4
  • 29
    • 22144445629 scopus 로고    scopus 로고
    • Entry of parainfluenza virus into cells as a target for interrupting childhood respiratory disease
    • Moscona A. Entry of parainfluenza virus into cells as a target for interrupting childhood respiratory disease. Journal of Clinical Investigation 2005, 115(7):1688-1698.
    • (2005) Journal of Clinical Investigation , vol.115 , Issue.7 , pp. 1688-1698
    • Moscona, A.1
  • 30
    • 0025941857 scopus 로고
    • Fusion properties of cells persistently infected with human parainfluenza virus type 3: participation of hemagglutinin-neuraminidase in membrane fusion
    • Moscona A., Peluso R.W. Fusion properties of cells persistently infected with human parainfluenza virus type 3: participation of hemagglutinin-neuraminidase in membrane fusion. Journal of Virology 1991, 65(6):2773-2777.
    • (1991) Journal of Virology , vol.65 , Issue.6 , pp. 2773-2777
    • Moscona, A.1    Peluso, R.W.2
  • 31
    • 0027381637 scopus 로고
    • Relative affinity of the human parainfluenza virus type 3 hemagglutinin-neuraminidase for sialic acid correlates with virus-induced fusion activity
    • Moscona A., Peluso R.W. Relative affinity of the human parainfluenza virus type 3 hemagglutinin-neuraminidase for sialic acid correlates with virus-induced fusion activity. Journal of Virology 1993, 67(11):6463-6468.
    • (1993) Journal of Virology , vol.67 , Issue.11 , pp. 6463-6468
    • Moscona, A.1    Peluso, R.W.2
  • 32
    • 0025342516 scopus 로고
    • Different roles of individual N-linked oligosaccharide chains in folding, assembly, and transport of the simian virus 5 hemagglutinin-neuraminidase
    • Ng D.T., Hiebert S.W., Lamb R.A. Different roles of individual N-linked oligosaccharide chains in folding, assembly, and transport of the simian virus 5 hemagglutinin-neuraminidase. Molecular and Cellular Biology 1990, 10(5):1989-2001.
    • (1990) Molecular and Cellular Biology , vol.10 , Issue.5 , pp. 1989-2001
    • Ng, D.T.1    Hiebert, S.W.2    Lamb, R.A.3
  • 33
    • 34548169552 scopus 로고    scopus 로고
    • Fusion promotion by a paramyxovirus hemagglutinin-neuraminidase protein: pH modulation of receptor avidity of binding sites I and II
    • Palermo L.M., Porotto M., Greengard O., Moscona A. Fusion promotion by a paramyxovirus hemagglutinin-neuraminidase protein: pH modulation of receptor avidity of binding sites I and II. Journal of Virology 2007, 81(17):9152-9161.
    • (2007) Journal of Virology , vol.81 , Issue.17 , pp. 9152-9161
    • Palermo, L.M.1    Porotto, M.2    Greengard, O.3    Moscona, A.4
  • 34
    • 2342544913 scopus 로고    scopus 로고
    • Loss of N-linked glycosylation from the hemagglutinin-neuraminidase protein alters virulence of Newcastle disease virus
    • Panda A., Elankumaran S., Krishnamurthy S., Huang Z., Samal S.K. Loss of N-linked glycosylation from the hemagglutinin-neuraminidase protein alters virulence of Newcastle disease virus. Journal of Virology 2004, 78(10):4965-4975.
    • (2004) Journal of Virology , vol.78 , Issue.10 , pp. 4965-4975
    • Panda, A.1    Elankumaran, S.2    Krishnamurthy, S.3    Huang, Z.4    Samal, S.K.5
  • 35
    • 10044296412 scopus 로고    scopus 로고
    • Inhibition of parainfluenza virus type 3 and Newcastle disease virus hemagglutinin-neuraminidase receptor binding: effect of receptor avidity and steric hindrance at the inhibitor binding sites
    • Porotto M., Murrell M., Greengard O., Lawrence M.C., McKimm-Breschkin J.L., Moscona A. Inhibition of parainfluenza virus type 3 and Newcastle disease virus hemagglutinin-neuraminidase receptor binding: effect of receptor avidity and steric hindrance at the inhibitor binding sites. Journal of Virology 2004, 78(24):13911-13919.
    • (2004) Journal of Virology , vol.78 , Issue.24 , pp. 13911-13919
    • Porotto, M.1    Murrell, M.2    Greengard, O.3    Lawrence, M.C.4    McKimm-Breschkin, J.L.5    Moscona, A.6
  • 36
    • 84855272388 scopus 로고    scopus 로고
    • Mechanism of fusion triggering by human parainfluenza virus type III: communication between viral glycoproteins during entry
    • Porotto M., Palmer S.G., Palermo L.M., Moscona A. Mechanism of fusion triggering by human parainfluenza virus type III: communication between viral glycoproteins during entry. Journal of Biological Chemistry 2011, 287(1):778-793.
    • (2011) Journal of Biological Chemistry , vol.287 , Issue.1 , pp. 778-793
    • Porotto, M.1    Palmer, S.G.2    Palermo, L.M.3    Moscona, A.4
  • 37
    • 0030893879 scopus 로고    scopus 로고
    • Epidemiology and clinical impact of parainfluenza virus infections in otherwise healthy infants and young children <5years old
    • Reed G., Jewett P.H., Thompson J., Tollefson S., Wright P.F. Epidemiology and clinical impact of parainfluenza virus infections in otherwise healthy infants and young children <5years old. Journal of Infectious Diseases 1997, 175(4):807-813.
    • (1997) Journal of Infectious Diseases , vol.175 , Issue.4 , pp. 807-813
    • Reed, G.1    Jewett, P.H.2    Thompson, J.3    Tollefson, S.4    Wright, P.F.5
  • 38
    • 33846110885 scopus 로고    scopus 로고
    • N-linked glycosylation status of classical swine fever virus strain Brescia E2 glycoprotein influences virulence in swine
    • Risatti G.R., Holinka L.G., Fernandez Sainz I., Carrillo C., Lu Z., Borca M.V. N-linked glycosylation status of classical swine fever virus strain Brescia E2 glycoprotein influences virulence in swine. Journal of Virology 2007, 81(2):924-933.
    • (2007) Journal of Virology , vol.81 , Issue.2 , pp. 924-933
    • Risatti, G.R.1    Holinka, L.G.2    Fernandez Sainz, I.3    Carrillo, C.4    Lu, Z.5    Borca, M.V.6
  • 39
    • 0026745063 scopus 로고
    • N-linked glycosylation of rabies virus glycoprotein. Individual sequons differ in their glycosylation efficiencies and influence on cell surface expression
    • Shakin-Eshleman S.H., Remaley A.T., Eshleman J.R., Wunner W.H., Spitalnik S.L. N-linked glycosylation of rabies virus glycoprotein. Individual sequons differ in their glycosylation efficiencies and influence on cell surface expression. Journal of Biological Chemistry 1992, 267(15):10690-10698.
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.15 , pp. 10690-10698
    • Shakin-Eshleman, S.H.1    Remaley, A.T.2    Eshleman, J.R.3    Wunner, W.H.4    Spitalnik, S.L.5
  • 40
    • 27144542635 scopus 로고    scopus 로고
    • Role of N-linked glycans on Bunyamwera virus glycoproteins in intracellular trafficking, protein folding, and virus infectivity
    • Shi X., Brauburger K., Elliott R.M. Role of N-linked glycans on Bunyamwera virus glycoproteins in intracellular trafficking, protein folding, and virus infectivity. Journal of Virology 2005, 79(21):13725-13734.
    • (2005) Journal of Virology , vol.79 , Issue.21 , pp. 13725-13734
    • Shi, X.1    Brauburger, K.2    Elliott, R.M.3
  • 41
    • 0036891868 scopus 로고    scopus 로고
    • Role of the hemagglutinin-neuraminidase protein in the mechanism of Paramyxovirus-cell membrane fusion
    • Takimoto T., Taylor G.L., Connaris H.C., Crennell S.J., Portner A. Role of the hemagglutinin-neuraminidase protein in the mechanism of Paramyxovirus-cell membrane fusion. Journal of Virology 2002, 76(24):13028-13033.
    • (2002) Journal of Virology , vol.76 , Issue.24 , pp. 13028-13033
    • Takimoto, T.1    Taylor, G.L.2    Connaris, H.C.3    Crennell, S.J.4    Portner, A.5
  • 42
    • 33747892601 scopus 로고    scopus 로고
    • Antiviral effects of glycosylation and glucose trimming inhibitors on human parainfluenza virus type 3
    • Tanaka Y., Kato J., Kohara M., Galinski M.S. Antiviral effects of glycosylation and glucose trimming inhibitors on human parainfluenza virus type 3. Antiviral Research 2006, 72(1):1-9.
    • (2006) Antiviral Research , vol.72 , Issue.1 , pp. 1-9
    • Tanaka, Y.1    Kato, J.2    Kohara, M.3    Galinski, M.S.4
  • 43
    • 79960405099 scopus 로고    scopus 로고
    • Longer V1V2 region with increased number of potential N-linked glycosylation sites in the HIV-1 envelope glycoprotein protects against HIV-specific neutralizing antibodies
    • van Gils M.J., Bunnik E.M., Boeser-Nunnink B.D., Burger J.A., Terlouw-Klein M., Verwer N., Schuitemaker H. Longer V1V2 region with increased number of potential N-linked glycosylation sites in the HIV-1 envelope glycoprotein protects against HIV-specific neutralizing antibodies. Journal of Virology 2011, 85(14):6986-6995.
    • (2011) Journal of Virology , vol.85 , Issue.14 , pp. 6986-6995
    • van Gils, M.J.1    Bunnik, E.M.2    Boeser-Nunnink, B.D.3    Burger, J.A.4    Terlouw-Klein, M.5    Verwer, N.6    Schuitemaker, H.7
  • 45
    • 1642430785 scopus 로고    scopus 로고
    • An oligosaccharide at the C-terminus of the F-specific domain in the stalk of the human parainfluenza virus 3 hemagglutinin-neuraminidase modulates fusion
    • Wang Z., Mirza A.M., Li J., Mahon P.J., Iorio R.M. An oligosaccharide at the C-terminus of the F-specific domain in the stalk of the human parainfluenza virus 3 hemagglutinin-neuraminidase modulates fusion. Virus Research 2004, 99(2):177-185.
    • (2004) Virus Research , vol.99 , Issue.2 , pp. 177-185
    • Wang, Z.1    Mirza, A.M.2    Li, J.3    Mahon, P.J.4    Iorio, R.M.5
  • 47
    • 44749089365 scopus 로고    scopus 로고
    • Sendai virus recombinant vaccine expressing hPIV-3 HN or F elicits protective immunity and combines with a second recombinant to prevent hPIV-1, hPIV-3 and RSV infections
    • Zhan X., Slobod K.S., Krishnamurthy S., Luque L.E., Takimoto T., Jones B., Surman S., Russell C.J., Portner A., Hurwitz J.L. Sendai virus recombinant vaccine expressing hPIV-3 HN or F elicits protective immunity and combines with a second recombinant to prevent hPIV-1, hPIV-3 and RSV infections. Vaccine 2008, 26(27-28):3480-3488.
    • (2008) Vaccine , vol.26 , Issue.27-28 , pp. 3480-3488
    • Zhan, X.1    Slobod, K.S.2    Krishnamurthy, S.3    Luque, L.E.4    Takimoto, T.5    Jones, B.6    Surman, S.7    Russell, C.J.8    Portner, A.9    Hurwitz, J.L.10


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