Visualization of individual reovirus particles by low-temperature, high-resolution scanning electron microscopy

被引:21
作者
Centonze, VE
Chen, Y
Severson, TF
Borisy, GG
Nibert, ML
机构
[1] UNIV WISCONSIN, INST MOLEC VIROL, MADISON, WI 53706 USA
[2] UNIV WISCONSIN, DEPT BIOCHEM, MADISON, WI 53706 USA
关键词
D O I
10.1006/jsbi.1995.1046
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
We used low-temperature, high-resolution scanning electron microscopy (cryo-HRSEM) to visualize surface structures on individual reovirus particles. Both intact virions and two forms of subvirion particles-infectious subvirion particles and cores-were examined, and despite some distortion of particles during specimen preparation and viewing in the microscope, the images obtained by cryo-HRSEM exhibited a level of interpretable detail not routinely achieved by other methods without image averaging. Cryo-HRSEM images of discrete reovirus particles were used to characterize and confirm features of the outer protein capsid of this virus by comparison with image reconstructions previously derived from cryotransmission electron microscopy. Distinct surface features attributable to each of the four outer-capsid proteins were identified. In addition, cryo-HRSEM images confirmed that significant changes occur on the surfaces of individual reovirus particles during disassembly and entry of cells and that the reovirus outer capsid is organized as a left-handed T=13 icosahedron. Several unique capabilities and potential uses suggest that cryo-HRSEM has a place alongside other, more established methods for molecular characterizations of virus particles. (C) 1995 Academic Press, Inc.
引用
收藏
页码:215 / 225
页数:11
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