Stanway G, Kalkkinen N, Roivainen M, Ghazi F, Khan M, Smyth M, Meurman O, Hyypiä T
Department of Virology, University of Turku, Finland.
J Virol. 1994 Dec;68(12):8232-8. doi: 10.1128/JVI.68.12.8232-8238.1994.
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.
最近的序列分析显示，人类病原体埃可病毒22（EV22）在基因上与迄今研究的所有其他小RNA病毒距离较远（T. 许皮埃、C. 霍斯内尔、M. 马罗宁、M. 汗、N. 卡尔基宁、P. 奥维宁、L. 金努宁和G. 斯坦韦，《美国国家科学院院刊》89:8847 - 8851，1992年）。我们进一步对该病毒的生物学特性进行了表征，在此表明该病毒粒子具有与其他小RNA病毒相似的特性。然而，其蛋白质组成是独特的，因为三种主要衣壳蛋白之一的VP0的大多数拷贝在成熟过程中不像之前研究的小RNA病毒那样进一步加工成VP2和VP4。此外，将衣壳蛋白序列与其他小RNA病毒的序列比对发现，VP3多肽在其氨基末端含有一个约25个氨基酸的明显插入序列。在VP1中发现了一个精氨酸 - 甘氨酸 - 天冬氨酸（RGD）基序，并且通过使用合成肽表明该序列在细胞表面受体识别中起作用。最后，EV23在基因组的某些部分与EV22具有显著的同源性，并且也属于这个先前未被识别的小RNA病毒组。
