Abstract
Coronaviruses have a simple protein composition. While there is some variation among different members, a basic set of four protein species universally occurs: the nucleocapsid protein (N), the spike protein (S), a small membrane protein (SM), and the membrane glycoprotein (M). Some coronaviruses have an additional membrane glycoprotein (HE). The M protein, previously also called El, is the subject of this chapter. As will become clear, M is a peculiar glycoprotein, different from all other viral glycoproteins in its structural and biochemical features. These unique features may be responsible for important biological properties of coronaviruses, in particular for their intracellular budding.
Chapter PDF
Similar content being viewed by others
Keywords
- Golgi Complex
- Infectious Bronchitis Virus
- Mouse Hepatitis Virus
- Infectious Bronchitis Virus Strain
- Transmissible Gastroenteritis Virus
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
References
Armstrong, J., and Patel, S., 1991, The Golgi sorting domain of Coronavirus El protein, J. Cell Sci. 98:567.
Armstrong, J., Niemann, H., Smeekens, S., Rottier, P., and Warren, G., 1984, Sequence and topology of a model intracellular membrane protein, El glycoprotein, from a Coronavirus, Nature 308:751.
Armstrong, J., McCrae, M., and Colman, A., 1987, Expression of Coronavirus El and rotavirus VP10 membrane proteins from synthetic RNA, J. Cell. Biochem. 35:129.
Armstrong, J., Patel, S., and Riddle, P., 1990, Lysosomal sorting mutants of Coronavirus El protein, a Golgi membrane protein, J. Cell Sci. 95:191.
Becker, W. B., McIntosh, K., Dees, J. H., and Chanock, R. M., 1967, Morphogenesis of avian infectious bronchitis virus and a related human virus (strain 229E), J. Virol. 1:1019.
Binns, M. M., Boursnell, M. E. G., Tomley, F. M., and Brown, T. D. K., 1986, Nucleotide sequence encoding the membrane protein of the IBV strain 6/82, Nucleic Acids Res. 14:5558.
Boursnell, M. E. G., Brown, T. D. K., and Binns, M. M., 1984, Sequence of the membrane protein gene from avian Coronavirus IBV, Virus Res. 1:303.
Bradburne, A. F., 1970, Antigenic relationships amongst coronaviruses, Arch. Gesamte Virusforsch. 31:352.
Buchmeier, M. J., Lewicki, H. A., Talbot, P. J., and Knobler, R. L., 1984, Murine hepatitis virus-4 (strain JHM)-induced neurologic disease is modulated in vivo by monoclonal antibody, Virology 132:261.
Callebaut, P. E., and Pensaert, M. B., 1980, Characterization and isolation of structural polypeptides in haemagglutinating encephalomyelitis virus, J. Gen. Virol. 48:193.
Cavanagh, D., 1981, Structural polypeptides of Coronavirus IBV, J. Gen. Virol. 53:93.
Cavanagh, D., 1983, Coronavirus IBV glycopolypeptides: Size of their polypeptide moieties and nature of their oligosaccharides, J. Gen. Virol. 64:1187.
Cavanagh, D., and Davis, P. J., 1988. Evolution of avian Coronavirus IBV: Sequence of the matrix glycoprotein gene and intergenic region of several serotypes, J. Gen. Virol. 69:621.
Cavanagh, D., Davis, P. J., and Pappin, D. J. C., 1986a, Coronavirus IBV glycopolypeptides: Ideational studies using proteases and saponin, a membrane permeabilizer, Virus Res. 4:145.
Cavanagh, D., Davis, P. J., Pappin, D. J. C., Binns, M. M., Boursnell, M. E. G., and Brown, T. D. K., 1986b, Coronavirus IBV: Partial amino terminal sequencing of spike polypeptide S2 identifies the sequence Arg-Arg-Phe-Arg-Arg at the cleavage site of the spike precursor propolypeptide of IBV strains Beaudette and M41, Virus Res. 4:133.
Charley, B., and Laude, H., 1988, Induction of alpha interferon by transmissible gastroenteritis Coronavirus: Role of transmembrane glycoprotein El, J. Virol. 62:8.
Chasey, D., and Alexander, D. J., 1976. Morphogenesis of avian infectious bronchitis virus in primary chick kidney cells, Arch. Virol. 52:101.
Collins, A. R., Knobler, R. L., Powell, H., and Buchmeier, M. J., 1982, Monoclonal antibodies to murine hepatitis virus 4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion, Virology 119:358.
David-Ferreira, J. F., and Manaker, R. A., 1965, An electron microscope study of the development of a mouse hepatitis virus in tissue culture cells, J. Cell Biol. 24:57.
Deregt, D., and Babiuk, L. A., 1987, Monoclonal antibodies to bovine Coronavirus: Characteristics and topographical mapping of neutralizing epitopes on the E2 and E3 glycoproteins, Virology 161:410.
Deregt, D., Sahara, M., and Babiuk, L. A., 1987, Structural proteins of bovine Coronavirus and their intracellular processing, J. Gen. Virol. 68:2863.
Doyle, C., Sambrook, J., and Gething, M.-J., 1986, Analysis of progressive deletions of the transmembrane and cytoplasmic domains of influenza hemagglutinin, J. Cell Biol. 103:1193.
Dubois-Dalcq, M. E., Doller, E. W., Haspel, M. V., and Holmes, K. V., 1982, Cell tropism and expression of mouse hepatitis viruses (MHV) in mouse spinal cord cultures, Virology 119:317.
Dubois-Dalcq, M. E., Holmes, K. V., and Rentier, B., 1984, Assembly of RNA Viruses, Springer Verlag, New York.
Earl, P. L., Moss, B., and Doms, R. W., 1991, Folding, interaction with GRP78-BiP, assembly, and transport of the human immunodeficiency virus type 1 envelope protein, J. Virol. 65:2047.
Fiscus, S. A., and Teramoto, Y. A., 1987, Antigenic comparison of feline Coronavirus isolates: Evidence for markedly different peplomer glycoproteins, J. Virol. 61:2607.
Fleming, J. O., Shubin, R. A., Sussman, M. A., Casteel, N., and Stohlman, S. A., 1989, Monoclonal antibodies to the matrix (El) glycoprotein of mouse hepatitis virus protect mice from encephalitis, Virology 168:162.
Gallagher, T. M., Parker, S. E., and Buchmeier, M. J., 1990, Neutralization-resistant variants of the neurotropic Coronavirus are generated by deletions within the amino-terminal half of the spike glycoprotein, J. Virol. 64:731.
Garwes, D. J., Pocock, D. H., and Pike, B. V., 1976, Isolation of subviral components from transmissible gastroenteritis virus, J. Gen. Virol. 32:283.
Geyer, H., Holschbach, C., Hunsmann, G., and Schneider, J., 1988, Carbohydrates of human immunodeficiency virus. Structures of olisosaccharides linked to the envelope glycoprotein 120, J. Biol. Chem. 263:1 1760.
Hasony, H. J., and Macnaughton, M. R., 1981, Antigenicity of mouse hepatitis virus strain 3 subcomponents in C57 strain mice, Arch. Virol. 69:33.
Hauri, H.-P., and Schweizer, A., 1992, The endoplasmic reticulum-Golgi intermediate compartment, Curr. Opin. Cell Biol. 4:600.
Hogue, B. G., and Brian, D. A., 1986, Structural proteins of human respiratory Coronavirus OC43, Virus Res. 5:131.
Holmes, K. V., and Behnke, J. N., 1981, Evolution of a Coronavirus during persistent infection in vitro, Adv. Exp. Med. Biol. 142:287.
Holmes, K. V., Doller, E. W., and Behnke, J. N., 1981a, Analysis of the functions of Coronavirus glycoproteins by differential inhibition of synthesis with tunicamycin, Adv. Exp. Med. Biol. 142:133.
Holmes, K. V., Doller, E. W., and Sturman, L. S., 1981b, Tunicamycin resistant glycosylation of a Coronavirus glycoprotein: Demonstration of a novel type of viral glycoprotein, Virology 115:334.
Horsburgh, B. C., Brierley, I., and Brown, T. D. K., 1992, Analysis of a 9.6 kb sequence from the 3′ end of canine Coronavirus genomic RNA, J. Gen. Virol. 73:2849.
Horzinek, M. C., Lutz, H., and Pedersen, N. C., 1982, Antigenic relationships among homologous structural polypeptides of porcine, feline, and canine coronaviruses. Infect, Immunology 37:1148.
Jacobs, L., Van der Zeijst, B. A. M., and Horzinek, M. C., 1986, Characterization and translation of transmissible gastroenteritis virus mRNAs, J. Virol. 57:1010.
Kapke, P. A., Tung, F. Y. T., Hogue, B. G., Brian, D. A., Woods, R. D., and Wesley, R., 1988, The amino-terminal signal peptide on the porcine transmissible gastroenteritis Coronavirus matrix protein is not an absolute requirement for membrane translocation and glycosylation, Virology 165:367.
King, B., and Brian, D. A., 1982, Bovine Coronavirus structural proteins, J. Virol. 42:700.
Klumperman, J., Krijnse Locker, J., Meijer, A., Horzinek, M. C., Geuze, H. J., and Rottier, P. J. M., 1994, Coronavirus M proteins accumulate in the Golgi complex beyond the site of virion budding, J. Virol. 68:6523.
Krijnse Locker, J., Griffiths, G., Horzinek, M. C., and Rottier, P. J. M., 1992a, O-glycosylation of the Coronavirus M protein, J. Biol. Chem. 267:14094.
Krijnse Locker, J., Rose, J. K., Horzinek, M. C., and Rottier, P. J. M., 1992b, Membrane assembly of the triple-spanning Coronavirus M protein, J. Biol. Chem. 267:2 1911.
Krijnse Locker, J., Ericsson, M., Rottier, P. J. M., and Griffiths, G., 1994, Characterization of the budding compartment of mouse hepatitis virus, J. Cell Biol. 124:55.
Krijnse Locker, J., Klumperman, J., Oorschot, V., Geuze, H. J., Horzinek, M. C., and Rottier, P. J. M., 1995, The cytoplasmic tail of mouse hepatitis virus M protein is essential but not sufficient for its retention in the Golgi complex, J. Biol. Chem. 269:28263.
Kyte, J., and Doolittle, R. F., 1982, A simple method for displaying the hydropathic character of a protein, J. Mol. Biol. 157:105.
Lanser, J. A., and Howard, C. R., 1980, The polypeptides of infectious bronchitis virus (IBV-41 strain). J. Gen. Virol. 46:349.
Lapps, W., Hogue, B. G., and Brian, D. A., 1987, Sequence analysis of the bovine Coronavirus nucleocapsid and matrix protein genes, Virology 157:47.
Laude, H., Chapsal, J.-M., Gelfi, J., Labiau, S., and Grosclaude, J., 1986, Antigenic structure of transmissible gastroenteritis virus. I. Properties of monoclonal antibodies directed against virion proteins, J. Gen. Virol. 67:119.
Laude, H., Rasschaert, D., and Huet, J.-C., 1987, Sequence and N-terminal processing of the transmissible protein El of the Coronavirus transmissible gastroenteritis virus, J. Gen. Virol. 68:1687.
Laude, H., Gelfi, J., Lavenant, L., and Charley, B., 1992, Single amino acid changes in the viral glycoprotein M affect induction of alpha interferon by the Coronavirus transmissible gastroenteritis virus, J. Virol. 66:743.
Laviada, M. D., Videgain, S. P., Moreno, L., Alonso, F., Enjuanes, L., and Escribano, J. M., 1990, Expression of swine transmissible gastroenteritis virus envelope antigens on the surface of infected cells: Epitopes externally exposed, Virus Res. 16:247.
Luytjes, W., Sturman, L. S., Bredenbeek, P. J., Charité, J., Van der Zeijst, B. A. M., Horzinek, M. C., and Spaan, W. J. M., 1987, Primary structure of the glycoprotein E2 of Coronavirus MHV-A59 and identification of the trypsin cleavage site, Virology 161:479.
Machamer, C. E., and Rose, J. K., 1987, A specific transmembrane domain of a Coronavirus El glycoprotein is required for its retention in the Golgi region, J. Cell Biol. 105:1205.
Machamer, C. E., Mentone, S. A., Rose, J. K., and Farquhar, M. G., 1990, The El glycoprotein of an avian Coronavirus is targeted to the cis Golgi complex, Proc. Natl. Acad. Sci. USA 87:6944.
Machamer, C. E., Grim, M. G., Esquela, A., Chung, S. W., Rolls, M., Ryan, K., and Swift, A. M., 1993, Retention of a cis Golgi protein requires polar residues on one face of a predicted a-helix in the transmembrane domain, Mol. Biol. Cell 4:695.
Macnaughton, M. R., 1981, Structural and antigenic relationships between human, murine and avian coronaviruses, Adv. Exp. Med. Biol. 142:19.
Mayer, T., Tamura, T., Falk, M., and Niemann, H., 1988, Membrane integration and intracellular transport of the Coronavirus glycoprotein El, a class III membrane glycoprotein, J. Biol. Chem. 263:14956.
Mcintosh, K., Kapikian, A. Z., Hardison, K. A., Hartley, J. W., and Chanock, R. M., 1969, Antigenic relationships among the coronaviruses of man and between human and animal coronaviruses, J. Immunol. 102:1109.
Mobley, J., Evans, G., Dailey, M. O., and Perlman, S., 1992, Immune response to a murine coronavirus: Identification of a homing receptor-negative CD4+ T cell subset that responds to viral glycoproteins, Virology 187:443.
Mounir, S., and Talbot, P. J., 1992, Sequence analysis of the membrane protein gene of human Coronavirus OC43 and evidence for O-glycosylation, J. Gen. Virol. 73:2731.
Niemann, H., and Klenk, H.-D., 1981, Coronavirus glycoprotein El, a new type of viral glycoprotein, J. Mol. Biol. 153:993.
Niemann, H., Boschek, B., Evans, D., Rosing, M., Tamura, T., and Klenk, H.-D., 1982, Post-translational glycosylation of Coronavirus glycoprotein El: Inhibition by monensin, EMBO J. 1:1499.
Niemann, H., Geyer, R., Klenk, H.-D., Linder, D., Stirm, S., and Wirth, M., 1984, The carbohydrates of mouse hepatitis virus (MHV) A59: Structures of the O-glycosidically linked oligosaccharides of glycoprotein El, EMBO J. 3:665.
Opstelten, D.-J. E., Horzinek, M. C., and Rottier, P. J. M., 1993a, Complex formation between the spike protein and the membrane protein during mouse hepatitis virus assembly, Adv. Exp. Med. Biol. 342:189.
Opstelten, D.-J. E., De Groote, P., Horzinek, M. C., Vennema, H., and Rottier, P. J. M., 1993b, Disulfide bonds in folding and transport of mouse hepatitis Coronavirus glycoproteins, J. Virol. 67:7394.
Opstelten, D.-J. E., De Groote, P., Horzinek, M. C., and Rottier, P. J. M., 1994, Folding of the mouse hepatitis virus spike protein and its association with the membrane protein, Arch. Virol. (Suppl) 9:319.
Parker, S. E., Gallagher, T. M., and Buchmeier, M. J., 1989, Sequence analysis reveals extensive polymorphism and evidence of deletions within the E2 glycoprotein gene of several strains of murine hepatitis virus, Virology 173:664.
Pedersen, N. C., Ward, I., and Mengeling, W. L., 1978, Antigenic relationships of the feline infectious peritonitis virus to coronaviruses of other species, Arch. Virol. 58:45.
Pfleiderer, M., Skinner, M. A., and Siddell, S. G., 1986, Coronavirus MHV-JHM: Nucleotide sequence of the mRNA that encodes the membrane protein, Nucleic Acids Res. 14:6338.
Pulford, D. J., and Britton, P., 1990, Expression and cellular localisation of porcine transmissible gastroenteritis virus N and M proteins by recombinant vaccinia viruses, Virus Res. 18:203.
Raabe, T., and Siddell, S. G., 1989, Nucleotide sequence of the gene encoding the membrane protein of human Coronavirus 229 E, Arch. Virol. 107:323.
Rasschaert, D., Duarte, M., and Laude, H., 1990, Porcine respiratory Coronavirus differs from transmissible gastroenteritis virus by a few genomic deletions, J. Gen. Virol. 71:2599.
Rottier, P. J. M., and Rose, J. K., 1987, Coronavirus El glycoprotein expressed from cloned cDNA localizes in the Golgi region, J. Virol. 61:2042.
Rottier, P. J. M., Spaan, W. J. M., Horzinek, M. C., and Van der Zeijst, B. A. M., 1981a, Translation of three mouse hepatitis virus strain A59 subgenomic RNAs in Xenopus laevis oocytes, J. Virol. 38:20.
Rottier, P. J. M., Horzinek, M. C., and Van der Zeijst, B. A. M., 1981b, Viral protein synthesis in mouse hepatitis virus strain A59-infected cells: Effect of tunicamycin, J. Virol. 40:350.
Rottier, P., Brandenburg, D., Armstrong, J., Van der Zeijst, B., and Warren, G., 1984, Assembly in vitro of a spanning membrane protein of the endoplasmic reticulum: The El glycoprotein of Coronavirus mouse hepatitis virus A59, Proc. Natl. Acad. Sci. USA 81:1421.
Rottier, P., Armstrong, J., and Meyer, D. I., 1985, Signal recognition particle-dependent insertion of Coronavirus El, an intracellular membrane glycoprotein, J. Biol. Chem. 260:4648.
Rottier, P. J. M., Welling, G. W., Welling-Wester, S., Niesters, H. G. M., Lenstra, J. A., and Van der Zeijst, B. A. M., 1986, Predicted membrane topology of the Coronavirus protein El, Biochemistry 25:1335.
Rottier, P. J. M., Krijnse Locker, J., Horzinek, M. C., and Spaan, W. J. M., 1990, Expression of MHV-A59 M glycoprotein: Effects of deletions on membrane integration and intracellular transport, Adv. Exp. Med. Biol. 276:127.
Sanchez, C. M., Jimenez, G., Laviada, M. D., Correa, I., Sune, C., Bullido, M. J., Gebauer, F., Smerdou, C., Callebaut, P., Escribano, J. M., and Enjuanes, L., 1990, Antigenic homology among coronaviruses related to transmissible gastroenteritis virus, Virology 174:410.
Schmidt, I., Skinner, M., and Siddell, S., 1987, Nucleotide sequence of the gene encoding the surface projection glycoprotein of Coronavirus MHV-JHM, J. Gen. Virol. 68:47.
Schmidt, M. F. G., 1982, Acylation of viral spike glycoproteins, a feature of enveloped RNA viruses, Virology 116:327.
Schmidt, O. W., and Kenny, G. E., 1982, Polypeptides and functions of antigens from human coronaviruses 229E and OC43, Infect. Immun. 35:515.
Siddell, S. G., Wege, H., Barthel, A., and Ter Meulen, V., 1981, Coronavirus JHM. Intracellular protein synthesis, J. Gen. Virol. 53:145.
Stern, D. F., and Sefton, B. M., 1982a, Coronavirus proteins: Biogenesis of avian infectious bronchitis virus virion proteins, J. Virol. 44:794.
Stern, D. F., and Sefton, B. M., 1982b, Coronavirus proteins: Structure and function of the oligosaccharides of the avian infectious bronchitis virus glycoproteins, J. Virol. 44:804.
Stern, D. F., Burgess, L., and Sefton, B. M., 1982, Structural analysis of virion proteins of the avian Coronavirus infectious bronchitis virus, J. Virol. 42:208.
Stohlman, S. A., and Lai, M. M. C., 1979, Phosphoproteins of murine hepatitis viruses, J. Virol. 32:672.
Sturman, L. S., 1977, Characterization of a Coronavirus. I. Structural proteins: Effects of preparative conditions on the migration of protein in Polyacrylamide gels, Virology 77:637.
Sturman, L. S., 1981, The structure and behaviour of Coronavirus A59 glycoproteins, Adv. Exp. Med. Biol. 142:1.
Sturman, L. S., and Holmes, K. V., 1977, Characterization of a Coronavirus. II. Glycoproteins of the viral envelope: Tryptic peptide analysis, Virology 77:650.
Sturman, L. S., Holmes, K. V., and Behnke, J., 1980, Isolation of Coronavirus envelope glycoproteins and interaction with the viral nucleocapsid, J. Virol. 33:449.
Sugiyama, K., and Amano, Y., 1981, Morphological and biological properties of a new Coronavirus associated with diarrhea in infant mice, Arch. Virol. 67:241.
Swift, A. M., and Machamer, C. E., 1991, A Golgi retention signal in a membrane-spanning domain of Coronavirus El protein, J. Cell Biol. 115:19.
Tooze, J., Tooze, S., and Warren, G., 1984, Replication of Coronavirus MHV-A59 in sac” cells: Determination of the first site of budding of progeny virions, Eur. J. Cell Biol. 33:281.
Tooze, J., Tooze, S. A., and Warren, G., 1985, Laminated cisternae of the rough endoplasmic reticulum induced by Coronavirus MHV-A59 infection, Eur. J. Cell Biol. 36:108.
Tooze, J., Tooze, S. A., and Fuller, S. D., 1987, Sorting of progeny Coronavirus from condensed secretory proteins at the exit from the trans-Golgi network of AtT20 cells, J. Cell Biol. 105:1215.
Tooze, S. A., and Stanley, K. K., 1986, Identification of two epitopes in the carboxyterminal 15 amino acids of the El glycoprotein of mouse hepatitis virus A59 by using hybrid proteins, J. Virol. 60:928.
Tooze, S. A., Tooze, J., and Warren, G., 1988, Site of addition of N-acetyl-galactosamine to the El glycoprotein of mouse hepatitis virus-A59, J. Cell. Biol. 106:1475.
Vennema, H., De Groot, R. J., Harbour, D. A., Dalderup, M., Gruffydd-Jones, T., Horzinek, M. C., and Spaan, W. J. M., 1990a, Early death after feline infectious peritonitis virus challenge due to recombinant vaccinia virus immunization, J. Virol. 64:1407.
Vennema, H., Heijnen, L., Zijderveld, A., Horzinek, M. C., and Spaan, W. J. M., 1990b, Intracellular transport of recombinant Coronavirus spike proteins: Implications for virus assembly, J. Virol. 64:339.
Vennema, H., De Groot, R. J., Harbour, D. A., Horzinek, M. C., and Spaan, W. J. M., 1991a, Primary structure of the membrane and nucleocapsid protein genes of feline infectious peritonitis virus and immunogenicity of recombinant vaccinia viruses in kittens, Virology 181:327.
Vennema, H., Rijnbrand, R., Heijnen, L., Horzinek, M. C., and Spaan, W. J. M., 1991b, Enhancement of the vaccinia virus/phage T7 RNA polymerase expression system using encephalomyocarditis virus 5′-untranslated region sequences, Gene 108:201.
Verbeek, A., and Tijssen, P., 1991, Sequence analysis of the turkey enteric Coronavirus nucleocapsid and membrane protein genes: A close genomic relationship with bovine Coronavirus, J. Gen. Virol. 72:1659.
Wang, F.-I., Fleming, J. O., and Lai, M. M. C., 1992, Sequence analysis of the spike protein gene of murine Coronavirus variants: Study of genetic sites affecting neuropathogenicity, Virology 186:742.
Wege, H., Wege, H., Nagashima, K., and Ter Meulen, V., 1979, Structural polypeptides of the murine Coronavirus JHM, J. Gen. Virol. 42:37.
Weisz, O. A., Swift, A. M., and Machamer, C. E., 1993, Oligomerization of a membrane protein correlates with its retention in the Golgi complex, J. Cell Biol. 122:1185.
Wesseling, J. G., Godeke, G.-J., Schijns, V. E. C. J., Prevec, L., Graham, F. L., Horzinek, M. C., and Rottier, P. J. M., 1993, Mouse hepatitis virus spike and nucleocapsid proteins expressed by adenovirus vectors protect mice against a lethal infection, J. Gen. Virol. 74:2061.
Wesseling, J. G., Vennema, H., Godeke, G.-J., Horzinek, M. C., and Rottier, P. J. M., 1994, Nucleotide sequence and expression of the spike (S) gene of canine Coronavirus and comparison with the S proteins of feline and porcine coronaviruses, J. Gen. Virol. 75:1789.
Woods, R. D., Wesley, R. D., and Kapke, P. A., 1988, Neutralization of porcine transmissible gastroenteritis virus by complement-dependent monoclonal antibodies, Am. f. Vet. Res. 49:300.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1995 Springer Science+Business Media New York
About this chapter
Cite this chapter
Rottier, P.J.M. (1995). The Coronavirus Membrane Glycoprotein. In: Siddell, S.G. (eds) The Coronaviridae. The Viruses. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1531-3_6
Download citation
DOI: https://doi.org/10.1007/978-1-4899-1531-3_6
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-1533-7
Online ISBN: 978-1-4899-1531-3
eBook Packages: Springer Book Archive