外壳蛋白与辅助成分之间的特定相互作用与马铃薯Y病毒属病毒的蚜虫传播相关。

A specific interaction between coat protein and helper component correlates with aphid transmission of a potyvirus.

作者信息

Blanc S, López-Moya J J, Wang R, García-Lampasona S, Thornbury D W, Pirone T P

机构信息

Department of Plant Pathology, University of Kentucky, Lexington 40546, USA.

出版信息

Virology. 1997 Apr 28;231(1):141-7. doi: 10.1006/viro.1997.8521.

DOI:10.1006/viro.1997.8521

PMID:9143313

Abstract

Specific binding between the coat protein (CP) and the helper component (HC) of the tobacco vein mottling potyvirus (TVMV) was characterized using a protein blotting-overlay protocol. In this in vitro assay, HC interacted with either virions or CP monomers originating from the aphid-transmissible TVMV-AT but not from the non-aphid-transmissible TVMV-NAT. There was a strong correlation between the aphid transmissibility of a series of TVMV variants having mutations in the DAG motif of the CP and their ability to bind HC. Expression of TVMV CP derivatives in bacteria allowed a precise determination of the minimum domain mediating HC binding. This domain is composed of seven amino acids, including the DAG motif (DTVDAGK), located in the N-terminus of the TVMV CP at amino acid positions 2 to 8.

摘要

利用蛋白质印迹覆盖法对烟草脉斑驳马铃薯Y病毒（TVMV）的外壳蛋白（CP）与辅助成分（HC）之间的特异性结合进行了表征。在这个体外试验中，HC与源自蚜虫传播的TVMV-AT的病毒粒子或CP单体相互作用，但不与非蚜虫传播的TVMV-NAT的病毒粒子或CP单体相互作用。在CP的DAG基序中具有突变的一系列TVMV变体的蚜虫传播能力与其结合HC的能力之间存在很强的相关性。TVMV CP衍生物在细菌中的表达使得能够精确确定介导HC结合的最小结构域。该结构域由七个氨基酸组成，包括位于TVMV CP N端第2至8位氨基酸处的DAG基序（DTVDAGK）。