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TMV recombinants encoding fused foreign transmembrane domains to the CP subunit caused local necrotic response on susceptible tobacco.

ABSTRACT: With regard to the effects of various foreign peptides fused to the coat protein subunits on the infectivity of corresponding TMV recombinants, some of TMV recombinants were found to induce necrotic local lesions on the inoculated leaves of susceptible tobacco. This paper reported that there existed a group of TMV recombinants in which the fused foreign peptides contained a transmembrane domain according to the predictions by three programs of SOSUI, TMpred and DAS. Further studies showed for the first time that a foreign transmembrane domain in a fused peptide of the corresponding TMV recombinant would result in the local lesions on the susceptible tobacco leaves. In addition, it was concluded that none of the TMV recombinants that systematically infected susceptible tobacco contained a transmembrane domain in the coat protein subunits.

SUBMITTER: Li Q

PROVIDER: S-EPMC7111735 | biostudies-literature | 2006 May

REPOSITORIES: biostudies-literature

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TMV recombinants encoding fused foreign transmembrane domains to the CP subunit caused local necrotic response on susceptible tobacco.

Li Qiaoli Q Li Mangmang M Jiang Lubin L Zhang Qingqi Q Song Rentao R Xu Zhengkai Z

Virology 20060320 2

With regard to the effects of various foreign peptides fused to the coat protein subunits on the infectivity of corresponding TMV recombinants, some of TMV recombinants were found to induce necrotic local lesions on the inoculated leaves of susceptible tobacco. This paper reported that there existed a group of TMV recombinants in which the fused foreign peptides contained a transmembrane domain according to the predictions by three programs of SOSUI, TMpred and DAS. Further studies showed for th ...[more]

PMID: 16542697

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Project description:BackgroundCrystal structures of the tobacco mosaic virus (TMV) coat protein (CP) in its helical and disk conformations have previously been determined at the atomic level. For the helical structure, interactions of proteins and nucleic acids in the main chains were clearly observed; however, the conformation of residues at the C-terminus was flexible and disordered. For the four-layer aggregate disk structure, interactions of the main chain residues could only be observed through water-mediated hydrogen bonding with protein residues. In this study, the effects of the C-terminal peptides on the interactions of TMV CP were investigated by crystal structure determination.Methodology/principal findingsThe crystal structure of a genetically engineered TMV CP was resolved at 3.06 Å. For the genetically engineered TMV CP, a six-histidine (His) tag was introduced at the N-terminus, and the C-terminal residues 155 to 158 were truncated (N-His-TMV CP(19)). Overall, N-His-TMV CP(19) protein self-assembled into the four-layer aggregate form. The conformations of residues Gln36, Thr59, Asp115 and Arg134 were carefully analyzed in the high radius and low radius regions of N-His-TMV CP(19), which were found to be significantly different from those observed previously for the helical and four-layer aggregate forms. In addition, the aggregation of the N-His-TMV CP(19) layers was found to primarily be mediated through direct hydrogen-bonding. Notably, this engineered protein also can package RNA effectively and assemble into an infectious virus particle.ConclusionThe terminal sequence of amino acids influences the conformation and interactions of the four-layer aggregate. Direct protein-protein interactions are observed in the major overlap region when residues Gly155 to Thr158 at the C-terminus are truncated. This engineered TMV CP is reassembled by direct protein-protein interaction and maintains the normal function of the four-layer aggregate of TMV CP in the presence of RNA.

Dataset Information

TMV recombinants encoding fused foreign transmembrane domains to the CP subunit caused local necrotic response on susceptible tobacco.

Publications

TMV recombinants encoding fused foreign transmembrane domains to the CP subunit caused local necrotic response on susceptible tobacco.

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