Morphology and stability changes of recombinant TMV particles caused by a cysteine residue in the foreign peptide fused to the coat protein

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• 作者：Qiaoli Li ; Lubin Jiang ; Mangmang Li ; Ping Li ; Qingqi Zhang ; Rentao Song ; Zhengkai Xu
• 关键词：TMV recombinant ; Morphology ; Infectivity ; Foreign peptide ; Cysteine residue
• 刊名：Journal of Virological Methods
• 出版年：2007
• 出版时间：March 2007
• 年：2007
• 卷：140
• 期：1-2
• 页码：212-217
• 全文大小：638 K

文摘

In the studies of expressing various foreign peptides using a TMV-based vector, a portion of morphologically altered progeny viral particles from some recombinant TMV constructs were detected by transmission electron microscopy in the first systematically infected upper leaves, but not in the fully expanded inoculated leaves, from infected tobacco plants. Furthermore, in vitro stability of such recombinant TMV constructs were lower than those of the wild type and other recombinant TMV constructs able to form regular rod-shape virions, hence causing the lower yields of recombinant viral particles purified from the infected tobacco plants. Our studies revealed that the presence of a cysteine residue in the foreign peptides, regardless of its position and the peptide sequence, was directly related to changes in the morphology and stability of these TMV recombinants.