Summary
Murine monoclonal antibodies against the fusion (F) and hemagglutininneuraminidase (HN) proteins of Sendai virus (SV) were prepared and studied on their antiviral activities, particularly on the neutralization of infectivity. On the analysis with solid phase competitive ELISA, 26 anti-HN antibodies were divided into at least four groups (HN-I, -II, -III and -IV). Antigenic sites recognized by the HN-I, -II, and -III group antibodies topographically separate from each other. Sites recognized by the HN-IV group antibodies overlaps partially with ones recognized by the HN-I, HN-II and -III group antibodies. The antibodies belonging to the HN-III group highly neutralize the infectivity of SV and weakly or not at all inhibit the hemagglutination (HA). In contrast, the HN-IV group antibodies strongly inhibit HA, but weakly neutralize the infectivity. Adsorption of SV to chicken red blood cells or L cells is inhibited by the HN-IV antibodies, but scarcely by the HN-III antibodies. On the other hand, incubation with HN-III antibodies of HeLa cells that have been preadsorbed with SV at 4° C, followed by culture at 37° C, causes inhibition of infection, but the HN-IV antibodies do not effectively interfere with such infection.
The competitive ELISA showed that 17 anti-F antibodies were divided into two groups (F-I and -II). Two antigenic sites recognized by the antibodies, however, seem to be near to each other because a certain competition is observed between the antibodies of both groups. Two of the seven antibodies belonging to the F-II group inhibit the hemolysis activity and also neutralize the infectivity of SV, but the other five F-II antibodies do not. One of the anti-F antibodies has a low HI activity, and, in competition tests, competes with one of the anti-HN antibodies (HN-IV).
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Aminoff D (1961) Methods for the quantitative estimation of N-acetylneuraminic acid and their application to hydrolysates of sialomucoids. Biochem J 81: 384–392
Galfre G, Howe SC, Milstein C, Butcher GW, Howard JC (1977) Antibodies to major histocompatibility antigens produced by hybrid cell lines. Nature 266: 550–552
Homma M, Ohuchi M (1973) Trypsin action on the growth of Sendai virus in tissue culture cells. III. Structural difference of Sendai viruses grown in eggs and tissue culture cells. J Virol 12: 1457–1465
Homma M, Tozawa H, Shimizu K, Ishida N (1975) A proposal for designation of Sendai virus proteins. Jpn J Microbiol 19: 467–470
Hsu M-C, Scheid A, Choppin PW (1979) Reconstitution of membranes with individual paramyxovirus glycoproteins and phospholipid in cholate solution. Virology 95: 476–491
Iorio RM, Bratt MA (1984) Monoclonal antibodies as functional probes of the HN glycoprotein of Newcastle disease virus: Antigenic separation of the hemagglutinating and neuraminidase sites. J Immunol 133: 2215–2219
Kashiwazaki H, Homma M, Ishida N (1965) Assay of Sendai virus by immuno-fluorescence and hemadsorbed cell-counting procedures. Proc Soc Exp Biol Med 120: 134–138
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with Folin phenol reagent. J Biol Chem 193: 265–275
Markwell MAK, Fox CF (1978) Surface-specific iodination of membrane proteins of viruses and eucaryotic cells using 1, 3, 4, 6, -tetrachloro-3α, 6α-diphenylglycoluril. Biochemistry 17: 4807–4817
Markwell MAK, Portner A, Schwartz AL (1985) An Alternative route of infection for viruses: Entry by means of the asialoglycoprotein receptor of a Sendai virus mutant lacking its attachment protein. Proc Natl Acad Sci USA 82: 978–982
Merz DC, Scheid A, Choppin PW (1981) Immunological studies of the functions of paramyxovirus glycoproteins. Virology 109: 94–105
Miura N, Uchida T, Okada Y (1982) HVJ (Sendai virus)-induced envelope fusion and cell fusion are blocked by monoclonal anti-HN protein antibody that does not inhibit hemagglutination activity of HVJ. Exp Cell Res 141: 409–420
Nishikawa K, Isomura S, Suzuki S, Watanabe E, Hamaguchi M, Yoshida T, Nagai Y (1983) Monoclonal antibodies to the YN glycoprotein of Newcastle disease virus. Biological characterization and use for strain comparisons. Virology 130: 318–330
Örvell C, Grandien M (1982) The effects of monoclonal antibodies on biologic activities of structural proteins of Sendai virus. J Immunol 129: 2779–2787
Örvell C (1984) The reactions of monoclonal antibodies with structural proteins of mumps virus. J Immunol 132: 2622–2629
Portner A (1981) The HN glycoprotein of Sendai virus: Analysis of site(s) involved in hemagglutinating and neuraminidase activities. Virology 115: 375–384
Russell PH, Griffiths PC, Goswami KKA, Alexander DJ, Cannon MJ, Russell WC (1983) The characterization of monoclonal antibodies to Newcastle disease virus. J gen Virol 64: 2069–2072
Sato H, Ogura H, Tanaka J, Hatano M (1984) Antigenic variation of HVJ (Sendai virus) HN glycoprotein detectable by monoclonal antibodies during persistent infection. J gen Virol 65: 185–189
Scheid A, Caliguiri LA, Compans RW, Choppin PW (1972) Isolation of paramyxovirus glycoproteins. Association of both hemagglutinating and neuraminidase activities with the larger SV 5 glycoprotein. Virology 50: 640–652
Scheid A, Choppin PW (1974) Identification of biological activities of paramyxovirus glycoproteins. Activation of cell fusion, hemolysis, and infectivity by proteolytic cleavage of an inactive precursor protein of Sendai virus. Virology 57: 475–490
Server AC, Merz DC, Waxham MN, Wolinsky JS (1982) Differentiation of mumps virus strains with monoclonal antibody to the HN glycoprotein. Infect Immun 35: 178–186
Shimizu K, Shimizu YK, Kohama T, Ishida N (1974) Isolation and characterization of two distinct types of HVJ (Sendai virus) spikes. Virology 62: 90–101
Togashi H, Tozawa H (1982) Neutralization of Sendai virus by the IgG subclass antibodies of the guinea pig. Microbiol Immunol 26: 821–829
Tozawa H, Watanabe M, Ishida N (1973) Structural components of Sendai virus. Serological and physiochemical characterization of hemagglutinin subunit associated with neuraminidase activity. Virology 55: 242–253
Van Wyke Coelingh KL, Winter C, Murphy BR (1985) Antigenic variation in the hemagglutinin-neuraminidase protein of human parainfluenza type 3 virus. Virology 143: 569–582
Watanabe M, Tozawa H, Kumagai K, Ishida N (1975) Specific macrophage immunity to Sendai virus: Macrophage aggregationin vitro with Sendai virus by cytophilic antibodies. Infect Immun 12: 324–332
Wilson BM, Nakane PK (1978) Recent developments in the periodate method of conjugating horseradish peroxidase (HRPO) to antibodies. In:Knapp W, Holubar K, Wick G (eds) Immunofluorescence and related staining techniques. Elsevier, Amsterdam, p 215–224
Yamamoto N, Hinuma Y (1982) Antigens in an adult T-cell leukemia virus-producer cell line: Reactivity with human serum antibodies. Int J Cancer 30: 289–293
Yedwell J, Gerhard W (1982) Delineation of four antigenic sites on a paramyxovirus glycoprotein via which monoclonal antibodies mediate distinct antiviral activities. J Immunol 128: 2670–2675
Author information
Authors and Affiliations
Additional information
With 2 Figures
Rights and permissions
About this article
Cite this article
Tozawa, H., Komatsu, H., Ohkata, K. et al. Neutralizing activity of the antibodies against two kinds of envelope glycoproteins of Sendai virus. Archives of Virology 91, 145–161 (1986). https://doi.org/10.1007/BF01316735
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF01316735