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MOLECULAR AND BIOLOGICAL CHARACTERISTICS OF ECHOVIRUS-22, - A REPRESENTATIVE OF A NEW PICORNAVIRUS GROUP
被引:167
作者:
STANWAY, G
KALKKINEN, N
ROIVAINEN, M
GHAZI, F
KHAN, M
SMYTH, M
MEURMAN, O
HYYPIA, T
机构:
[1] UNIV HELSINKI,INST BIOTECHNOL,SF-00380 HELSINKI,FINLAND
[2] UNIV TURKU,DEPT VIROL,SF-20520 TURKU,FINLAND
[3] NATL PUBL HLTH INST,ENTEROVIRUS LAB,SF-00300 HELSINKI,FINLAND
[4] UNIV ESSEX,DEPT BIOL,COLCHESTER CO4 3SQ,ESSEX,ENGLAND
[5] UNIV OXFORD,MOLEC BIOPHYS LAB,OXFORD OX1 3QU,ENGLAND
关键词:
D O I:
10.1128/JVI.68.12.8232-8238.1994
中图分类号:
Q93 [微生物学];
学科分类号:
071005 ;
100705 ;
摘要:
Recent sequence analysis revealed that the human pathogen echovirus 22 (EV22) is genetically distant from all the other picornaviruses studied to date (T. Hyypia, 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, VPO, 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 VPI, 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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页码:8232 / 8238
页数:7
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