Skip to main content
NCBI home page
Springer Nature - PMC COVID-19 Collection logoLink to Springer Nature - PMC COVID-19 Collection
. 1987;93(1):31–49. doi: 10.1007/BF01313892

Biological properties of mengovirus: Characterization of avirulent, hemagglutination-defective mutants

Kevin Anderson 1, Clifford W Bond 1
PMCID: PMC7087273  PMID: 3028343

Summary

Biological properties of two mengovirus mutants, 205 and 280, were compared to those of wild-type virus. The mutants exhibited alterations in plaque morphology, hemagglutination, and virulence in mice, but were not temperature-sensitive. Agglutination of human erythrocytes by mengovirus was dependent on the presence of sialic acid on the erythrocyte surface; however, free sialic acid failed to inhibit hemagglutination. Glycophorin, the major sialoglycoprotein of human erythrocyte membranes, exhibited receptor specificity for wild-type virus, but not for mutants 205 or 280. Cross-linking studies indicated that glycophorin exhibited binding specificity for the alpha (1 D) structural protein. The LD50 titers for wild-type mengovirus were 7 and 1500 plaque forming units (PFU) in mice infected intracranially (IC) and intraperitoneally (IP), respectively. However, mice infected IC or IP with 106 or 107 PFU of mutant 205 or 280 did not exhibit symptoms indicative of virus infection. Revertants were isolated from the brains of mice infected with mutant 205, but not from the brains of mice infected with mutant 280. The biological characterization of the revertants indicated that hemagglutination and virulence may be phenotypically-linked traits.

Keywords: Infectious Disease, Virus Infection, Sialic Acid, Biological Property, Binding Specificity

Footnotes

With 2 Figures

References

  • 1.Agol VI, Grachev VP, Drozdov SG, Kolesnikova MS, Kozlov VG, Ralph NM, Romanova LI, Tolskaya EA, Tyufanov AV, Victorova EG. Construction and properties of intertypic poliovirus recombinants: First approximation mapping of the major determinants of neurovirulence. Virology. 1984;136:41–55. doi: 10.1016/0042-6822(84)90246-0. [DOI] [PubMed] [Google Scholar]
  • 2.Amako K, Dales S. Cytopathology of mengovirus infection. I. Relationship between cellular disintegration and virulence. Virology. 1967;32:184–200. doi: 10.1016/0042-6822(67)90269-3. [DOI] [PubMed] [Google Scholar]
  • 3.Anderson K, Bond CW. Structural and physiological properties of mengovirus: avirulent, hemagglutination-defective mutants express altered alpha (1 D) proteins and are adsorption-defective. Arch Virol. 1987;93:13–29. doi: 10.1007/BF01313891. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 4.Bond CW, Swim HE. Physiological characterization of temperature-sensitive mutants of mengovirus. J Virol. 1975;15:288–296. doi: 10.1128/jvi.15.2.288-296.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 5.Bond CW, Swim HE. Factors affecting composition and thermostability of mengovirus virions. J Virol. 1977;21:1256–1261. doi: 10.1128/jvi.21.3.1256-1261.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 6.Bond CW, Anderson K, Goss S, Sardinia L. Relatedness of virion and intracellular proteins of the murine coronaviruses JHM and A 59. In: ter Meulen V, Siddell S, Wege H, editors. Biochemistry and biology of coronaviruses. New York: Plenum; 1981. pp. 103–110. [DOI] [PubMed] [Google Scholar]
  • 7.Bonner WM, Laskey RA. A film detection method for tritium labelled proteins and nucleic acids in polyacrylamide gels. Eur J Biochem. 1974;46:83–88. doi: 10.1111/j.1432-1033.1974.tb03599.x. [DOI] [PubMed] [Google Scholar]
  • 8.Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
  • 9.Burness ATH, Pardoe IU. Effect of enzymes on the attachment of influenza and encephalomyocarditis viruses to erythrocytes. J Gen Virol. 1981;55:275–288. doi: 10.1099/0022-1317-55-2-275. [DOI] [PubMed] [Google Scholar]
  • 10.Burness ATH, Pardoe IU. A sialoglycopeptide from human erythrocytes with receptor-like properties for encephalomyocarditis and influenza viruses. J Gen Virol. 1983;64:1137–1148. doi: 10.1099/0022-1317-64-5-1137. [DOI] [PubMed] [Google Scholar]
  • 11.Campbell JB, Colter JS. Studies of three variants of mengo encephalomyelitis virus. IV. Affinities for mouse tissuesin vitro andin vivo. Virology. 1967;32:69–73. doi: 10.1016/0042-6822(67)90253-x. [DOI] [PubMed] [Google Scholar]
  • 12.Carroll SM, Higa HH, Paulson JC. Different cell-surface receptor determinants of antigenically similar influenza viruses. J Biol Chem. 1981;256:8357–8363. [PubMed] [Google Scholar]
  • 13.Colter JS, Campbell JB, Hatch LR. The pathogenicity to mice of three variants of mengo encephalomyelitis virus. J Cell Comp Physiol. 1965;65:229–236. doi: 10.1002/jcp.1030650209. [DOI] [PubMed] [Google Scholar]
  • 14.Ellem KAO, Colter JS. The isolation of three variants of mengo virus differing in plaque morphology and hemagglutinating characteristics. Virology. 1961;15:340–347. doi: 10.1016/0042-6822(61)90365-8. [DOI] [PubMed] [Google Scholar]
  • 15.Emini EA, Jameson BA, Lewis AJ, Larsen GR, Wimmer E. Poliovirus neutralization epitopes: analysis and localization with neutralizing monoclonal antibodies. J Virol. 1982;43:997–1005. doi: 10.1128/jvi.43.3.997-1005.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 16.Enegren BJ, Burness ATH. Chemical structure of attachment sites for viruses on human erythrocytes. Nature. 1977;268:536–537. doi: 10.1038/268536a0. [DOI] [PubMed] [Google Scholar]
  • 17.Fairbanks G, Steck TL, Wallach DFH. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971;10:2606–2617. doi: 10.1021/bi00789a030. [DOI] [PubMed] [Google Scholar]
  • 18.Herrmann EC, Jr, Engle C. Tumor-cell induced mouse ascites fluid as a source of viral antibodies. Proc Soc Exp Biol Med. 1958;98:257–259. doi: 10.3181/00379727-98-24009. [DOI] [PubMed] [Google Scholar]
  • 19.Hordern JS, Leonard JD, Scraba DG. Structure of the mengovirion. VI. Spatial relationships of the capsid polypeptides as determined by chemical cross-linking analysis. Virology. 1979;97:131–140. doi: 10.1016/0042-6822(79)90379-9. [DOI] [PubMed] [Google Scholar]
  • 20.Kohara M, Omata T, Kameda A, Semler BL, Itoh H, Wimmer E, Nomoto A. In vitro phenotypic markers of a poliovirus recombinant constructed from infectious cDNA clones of the neurovirulent Mahoney strain and the attenuated Sabin 1 strain. J Virol. 1985;53:786–792. doi: 10.1128/jvi.53.3.786-792.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 21.Laemmli UK, Favre MJ. Maturation of the head of bacteriophage T4. I. DNA packaging events. J Mol Biol. 1973;80:575–599. doi: 10.1016/0022-2836(73)90198-8. [DOI] [PubMed] [Google Scholar]
  • 22.Marchesi VT, Andrews EP. Glycoproteins: isolation from cell membranes with lithium diiodosalicylate. Science. 1971;174:1247–1248. doi: 10.1126/science.174.4015.1247. [DOI] [PubMed] [Google Scholar]
  • 23.Marchesi VT, Tillack TW, Jackson RL, Segrest JP, Scott RE. Chemical characterization and surface orientation of the major glycoprotein of the human erythrocyte membrane. Proc Natl Acad Sci USA. 1972;69:1445–1449. doi: 10.1073/pnas.69.6.1445. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 24.Martin EM, Malec J, Sved S, Work TS. Studies on protein and nucleic acid metabolism in virus-infected mammalian cells. Biochem J. 1961;80:585–596. doi: 10.1042/bj0800585. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 25.Morishima T, McClintock PR, Aulakh GS, Billups LC, Notkins AL. Genomic and receptor attachment differences between mengovirus and encephalomyocarditis virus. Virology. 1982;122:461–465. doi: 10.1016/0042-6822(82)90245-8. [DOI] [PubMed] [Google Scholar]
  • 26.Putnak JR, Phillips BA. Picornaviral structure and assembly. Micro Rev. 1981;45:287–315. doi: 10.1128/mr.45.2.287-315.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 27.Robb JA, Bond CW. Pathogenic murine coronaviruses: I. Characterization of biological behaviorin vitro and virus-specific intracellular RNA of strongly neurotropic JHMV and weakly neurotropic A 59 V viruses. Virology. 1979;94:352–370. doi: 10.1016/0042-6822(79)90467-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 28.Rueckert RR. On the structure and morphogenesis of picornaviruses. In: Fraenkel-Conrat H, Wagner RR, editors. Comprehensive virology, vol. 6. New York: Plenum; 1976. pp. 131–212. [Google Scholar]
  • 29.Rueckert RR, Wimmer E. Systematic nomenclature for picornavirus proteins. J Virol. 1984;50:957–959. doi: 10.1128/jvi.50.3.957-959.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 30.Scraba DG. The picornavirion: structure and assembly. In: Perez-Bercoff R, editor. The molecular biology of picornaviruses. New York: Plenum; 1979. pp. 1–23. [Google Scholar]
  • 31.Yoon JW, Morishima T, McClintock PR, Austin M, Notkins AL. Virus-induced diabetes mellitis: mengovirus infects pancreatic beta cell sin strains of mice resistant to the effects of encephalomyocarditis virus. J Virol. 1984;50:684–690. doi: 10.1128/jvi.50.3.684-690.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 32.Ziola BR, Scraba DG. Structure of the mengovirion. I. Polypeptide and ribonucleate components of the virus particle. Virology. 1974;57:531–542. doi: 10.1016/0042-6822(74)90192-5. [DOI] [PubMed] [Google Scholar]

Articles from Archives of Virology are provided here courtesy of Nature Publishing Group

RESOURCES