文献类型： 外文期刊

作者： Niu, Shengniao ¹ ; Gil-Salas, Francisco M. ¹ ; Tewary, Sunil Kumar ¹ ; Samales, Ashwin Kuppusamy ¹ ; Johnson, Jo ¹ ;

作者机构： 1.Natl Univ Singapore, Dept Biol Sci, Singapore 117548, Singapore

2.Chinese Acad Trop Agr Sci, Inst Trop Biosci & Biotechnol, Minist Agr, Key Lab Trop Crop Biotechnol, Hainan, Peoples R China

3.Inst Andaluz Invest & Formac Agr Pesquera Aliment, Almeria, Spain

4.Scripps Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA

5.Temasek Life Sci Lab, Singapore, Singapore

6.Natl Univ Singapore, Suzhou Res Inst, Suzhou, Jiangsu, Peoples R China

期刊名称：PLOS ONE （ 影响因子：3.24； 五年影响因子：3.788 ）

ISSN： 1932-6203

年卷期： 2014 年 9 卷 11 期

页码：

收录情况： SCI

摘要： Hibiscus chlorotic ringspot virus (HCRSV) is a member of the genus Carmovirus in the family Tombusviridae. In order to study its coat protein (CP) functions on virus replication and movement in kenaf (Hibiscus cannabinus L.), two HCRSV mutants, designated as p2590 (A to G) in which the first start codon ATG was replaced with GTG and p2776 (C to G) in which proline 63 was replaced with alanine, were constructed. In vitro transcripts of p2590 (A to G) were able to replicate to a similar level as wild type without CP expression in kenaf protoplasts. However, its cell-to-cell movement was not detected in the inoculated kenaf cotyledons. Structurally the proline 63 in subunit C acts as a kink for beta-annulus formation during virion assembly. Progeny of transcripts derived from p2776 (C to G) was able to move from cell-to-cell in inoculated cotyledons but its long-distance movement was not detected. Virions were not observed in partially purified mutant virus samples isolated from 2776 (C to G) inoculated cotyledons. Removal of the N-terminal 77 amino acids of HCRSV CP by trypsin digestion of purified wild type HCRSV virions resulted in only T = 1 empty virus-like particles. Taken together, HCRSV CP is dispensable for viral RNA replication but essential for cell-to-cell movement, and virion is required for the virus systemic movement. The proline 63 is crucial for HCRSV virion assembly in kenaf plants and the N-terminal 77 amino acids including the b-annulus domain is required in T = 3 assembly in vitro.