Onimatsu Hideki, Sugimoto Ichiro, Fujie Makoto, Usami Shoji, Yamada Takashi
Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, Higashi-Hiroshima 739-8530, Japan.
Virology. 2004 Feb 5;319(1):71-80. doi: 10.1016/j.virol.2003.10.030.
A protein, Vp130, that interacts with the host cell wall was isolated from Chlorovirus CVK2. From its peptide sequence, the gene for Vp130 was identified on the PBCV-1 genomic sequence as an ORF combining A140R and A145R. In Vp130, the N-terminus was somehow modified and the C-terminus was occupied by 23-26 tandem repeats of a PAPK motif. In the internal region, Vp130 contained seven repeats of 70-73 amino acids, each copy of which was separated by PAPK sequences. This protein was well conserved among NC64A viruses. A recombinant rVp130N protein formed in Escherichia coli was shown not only to bind directly to the host cell wall in vitro but also to specifically bind to the host cells, as demonstrated by fluorescence microscopy. Because externally added rVp130N competed with CVK2 to bind to host cells, Vp130 is most likely to be a host-recognizing protein on the virion.
从绿藻病毒CVK2中分离出一种与宿主细胞壁相互作用的蛋白质Vp130。根据其肽序列，在PBCV-1基因组序列上确定Vp130基因是一个由A140R和A145R组合而成的开放阅读框。在Vp130中，N端以某种方式被修饰，C端被23 - 26个PAPK基序串联重复序列占据。在内部区域，Vp130包含7个70 - 73个氨基酸的重复序列，每个拷贝由PAPK序列隔开。这种蛋白质在NC64A病毒中高度保守。在大肠杆菌中形成的重组rVp130N蛋白不仅在体外能直接结合宿主细胞壁，而且通过荧光显微镜观察表明能特异性结合宿主细胞。由于外部添加的rVp130N与CVK2竞争结合宿主细胞，Vp130很可能是病毒体上一种识别宿主的蛋白质。
