β-structure of the coat protein subunits in spherical particles generated by tobacco mosaic virus thermal denaturation

被引：26

作者：

Dobrov, Evgeny N. ^{[1
]}

Nikitin, Nikolai A. ^{[2
]}

Trifonova, Ekaterina A. ^{[2
]}

Parshina, Evgenia Yu. ^{[3
]}

Makarov, Valentin V. ^{[1
]}

Maksimov, George V. ^{[3
]}

Karpova, Olga V. ^{[2
]}

Atabekov, Joseph G. ^{[1
,2
]}

机构：

[1] Moscow MV Lomonosov State Univ, AN Belozersky Inst Physicochem Biol, Moscow 119991, Russia

[2] Moscow MV Lomonosov State Univ, Dept Virol, Moscow 119991, Russia

[3] Moscow MV Lomonosov State Univ, Dept Biophys, Moscow 119991, Russia

来源：

JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS | 2014年 / 32卷 / 05期

基金：

俄罗斯基础研究基金会;

关键词：

tobacco mosaic virus; spherical particles; amyloid structures; alpha-and beta-structures; thermal remodeling; CIRCULAR-DICHROISM; TRANSITION; AGGREGATE; FLUORESCENCE; SPECTRA; RANGE; PH;

D O I：

10.1080/07391102.2013.788983

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Conversion of the rod-like tobacco mosaic virus (TMV) virions into "ball-like particles" by thermal denaturation at 90-98 degrees C had been described by R.G. Hart in 1956. We have reported recently that spherical particles (SPs) generated by thermal denaturation of TMV at 94-98 degrees C were highly stable, RNA-free, and water-insoluble. The SPs were uniform in shape but varied widely in size (53-800 nm), which depended on the virus concentration. Here, we describe some structural characteristics of SPs using circular dichroism, fluorescence spectroscopy, and Raman spectroscopy. It was found that the structure of SPs protein differs strongly from that of the native TMV and is characterized by coat protein subunits transition from mainly (about 50%) alpha-helical structure to a structure with low content of alpha-helices and a significant fraction of beta-sheets. The SPs demonstrate strong reaction with thioflavin T suggesting the formation of amyloid-like structures.

引用

页码：701 / 708

页数：8

共 25 条

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