Abstract
Recent sequence analysis revealed that the human pathogen echovirus 22 (EV22) is genetically distant from all the other picornaviruses studied to date (T. Hyypiä, C. Horsnell, M. Maaronen, M. Khan, N. Kalkkinen, P. Auvinen, L. Kinnunen, and G. Stanway, Proc. Natl. Acad. Sci. USA 89:8847-8851, 1992). We have further characterized the biological properties of the virus and show here that the virion has properties similar to those of other picornaviruses. However, the protein composition is unique, in that most copies of one of the three major capsid proteins, VP0, do not undergo the further processing to VP2 and VP4 observed during the maturation of the virus in previously studied picornaviruses. Alignment of the capsid protein sequences with those of other picornaviruses revealed, furthermore, that the VP3 polypeptide contains an apparent insertion of approximately 25 amino acids at its amino terminus. An arginine-glycine-aspartic acid (RGD) motif is found in VP1, and by using synthetic peptides, it was shown that this sequence plays a role in cell surface receptor recognition. Finally, EV23 was shown to share remarkable identity with EV22 in certain parts of the genome and also belongs to this previously unrecognized picornavirus group.
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- Abraham G., Colonno R. J. Many rhinovirus serotypes share the same cellular receptor. J Virol. 1984 Aug;51(2):340–345. doi: 10.1128/jvi.51.2.340-345.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Acharya R., Fry E., Stuart D., Fox G., Rowlands D., Brown F. The three-dimensional structure of foot-and-mouth disease virus at 2.9 A resolution. Nature. 1989 Feb 23;337(6209):709–716. doi: 10.1038/337709a0. [DOI] [PubMed] [Google Scholar]
- Baumann M., Lauraeus M. Purification of membrane proteins using a micropreparative gel electrophoresis apparatus: purification of subunits of the integral membrane protein Bacillus subtilis aa3-type quinol oxidase for low level amino acid sequence analysis. Anal Biochem. 1993 Oct;214(1):142–148. doi: 10.1006/abio.1993.1469. [DOI] [PubMed] [Google Scholar]
- Chang K. H., Auvinen P., Hyypiä T., Stanway G. The nucleotide sequence of coxsackievirus A9; implications for receptor binding and enterovirus classification. J Gen Virol. 1989 Dec;70(Pt 12):3269–3280. doi: 10.1099/0022-1317-70-12-3269. [DOI] [PubMed] [Google Scholar]
- Chang K. H., Day C., Walker J., Hyypiä T., Stanway G. The nucleotide sequences of wild-type coxsackievirus A9 strains imply that an RGD motif in VP1 is functionally significant. J Gen Virol. 1992 Mar;73(Pt 3):621–626. doi: 10.1099/0022-1317-73-3-621. [DOI] [PubMed] [Google Scholar]
- Chow M., Newman J. F., Filman D., Hogle J. M., Rowlands D. J., Brown F. Myristylation of picornavirus capsid protein VP4 and its structural significance. Nature. 1987 Jun 11;327(6122):482–486. doi: 10.1038/327482a0. [DOI] [PubMed] [Google Scholar]
- Coller B. A., Chapman N. M., Beck M. A., Pallansch M. A., Gauntt C. J., Tracy S. M. Echovirus 22 is an atypical enterovirus. J Virol. 1990 Jun;64(6):2692–2701. doi: 10.1128/jvi.64.6.2692-2701.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Coller B. G., Tracy S. M., Etchison D. Cap-binding complex protein p220 is not cleaved during echovirus 22 replication in HeLa cells. J Virol. 1991 Jul;65(7):3903–3905. doi: 10.1128/jvi.65.7.3903-3905.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Devereux J., Haeberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 1984 Jan 11;12(1 Pt 1):387–395. doi: 10.1093/nar/12.1part1.387. [DOI] [PMC free article] [PubMed] [Google Scholar]
- EGGERS H. J., TAMM I. Spectrum and characteristics of the virus inhibitory action of 2-(alpha-hydroxybenzyl)-benzimidazole. J Exp Med. 1961 Apr 1;113:657–682. doi: 10.1084/jem.113.4.657. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fox G., Parry N. R., Barnett P. V., McGinn B., Rowlands D. J., Brown F. The cell attachment site on foot-and-mouth disease virus includes the amino acid sequence RGD (arginine-glycine-aspartic acid). J Gen Virol. 1989 Mar;70(Pt 3):625–637. doi: 10.1099/0022-1317-70-3-625. [DOI] [PubMed] [Google Scholar]
- Hogle J. M., Chow M., Filman D. J. Three-dimensional structure of poliovirus at 2.9 A resolution. Science. 1985 Sep 27;229(4720):1358–1365. doi: 10.1126/science.2994218. [DOI] [PubMed] [Google Scholar]
- Hyypiä T., Horsnell C., Maaronen M., Khan M., Kalkkinen N., Auvinen P., Kinnunen L., Stanway G. A distinct picornavirus group identified by sequence analysis. Proc Natl Acad Sci U S A. 1992 Sep 15;89(18):8847–8851. doi: 10.1073/pnas.89.18.8847. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jamison R. M. An electron microscopic study of the intracellular development of echovirus 22. Arch Gesamte Virusforsch. 1974;44(3):184–194. doi: 10.1007/BF01240606. [DOI] [PubMed] [Google Scholar]
- Kawasaki H., Suzuki K. Separation of peptides dissolved in a sodium dodecyl sulfate solution by reversed-phase liquid chromatography: removal of sodium dodecyl sulfate from peptides using an ion-exchange precolumn. Anal Biochem. 1990 May 1;186(2):264–268. doi: 10.1016/0003-2697(90)90077-m. [DOI] [PubMed] [Google Scholar]
- Luo M., Vriend G., Kamer G., Minor I., Arnold E., Rossmann M. G., Boege U., Scraba D. G., Duke G. M., Palmenberg A. C. The atomic structure of Mengo virus at 3.0 A resolution. Science. 1987 Jan 9;235(4785):182–191. doi: 10.1126/science.3026048. [DOI] [PubMed] [Google Scholar]
- Roivainen M., Hyypiä T., Piirainen L., Kalkkinen N., Stanway G., Hovi T. RGD-dependent entry of coxsackievirus A9 into host cells and its bypass after cleavage of VP1 protein by intestinal proteases. J Virol. 1991 Sep;65(9):4735–4740. doi: 10.1128/jvi.65.9.4735-4740.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Roivainen M., Piirainen L., Hovi T., Virtanen I., Riikonen T., Heino J., Hyypiä T. Entry of coxsackievirus A9 into host cells: specific interactions with alpha v beta 3 integrin, the vitronectin receptor. Virology. 1994 Sep;203(2):357–365. doi: 10.1006/viro.1994.1494. [DOI] [PubMed] [Google Scholar]
- Rossmann M. G., Arnold E., Erickson J. W., Frankenberger E. A., Griffith J. P., Hecht H. J., Johnson J. E., Kamer G., Luo M., Mosser A. G. Structure of a human common cold virus and functional relationship to other picornaviruses. Nature. 1985 Sep 12;317(6033):145–153. doi: 10.1038/317145a0. [DOI] [PubMed] [Google Scholar]
- Ruoslahti E., Pierschbacher M. D. New perspectives in cell adhesion: RGD and integrins. Science. 1987 Oct 23;238(4826):491–497. doi: 10.1126/science.2821619. [DOI] [PubMed] [Google Scholar]
- Stanway G., Hughes P. J., Mountford R. C., Minor P. D., Almond J. W. The complete nucleotide sequence of a common cold virus: human rhinovirus 14. Nucleic Acids Res. 1984 Oct 25;12(20):7859–7875. doi: 10.1093/nar/12.20.7859. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Stanway G. Structure, function and evolution of picornaviruses. J Gen Virol. 1990 Nov;71(Pt 11):2483–2501. doi: 10.1099/0022-1317-71-11-2483. [DOI] [PubMed] [Google Scholar]
- Tesar M., Jia X. Y., Summers D. F., Ehrenfeld E. Analysis of a potential myristoylation site in hepatitis A virus capsid protein VP4. Virology. 1993 Jun;194(2):616–626. doi: 10.1006/viro.1993.1301. [DOI] [PubMed] [Google Scholar]
- WIGAND R., SABIN A. B. Properties of ECHO types 22, 23 and 24 viruses. Arch Gesamte Virusforsch. 1961;11:224–247. doi: 10.1007/BF01241688. [DOI] [PubMed] [Google Scholar]

