Ve. Centonze et al., VISUALIZATION OF INDIVIDUAL REOVIRUS PARTICLES BY LOW-TEMPERATURE, HIGH-RESOLUTION SCANNING ELECTRON-MICROSCOPY, Journal of structural biology, 115(3), 1995, pp. 215-225
We used low-temperature, high-resolution scanning electron microscopy
(cryo-HRSEM) to visualize surface structures on individual reovirus pa
rticles. Both intact virions and two forms of subvirion particles-infe
ctious subvirion particles and cores-were examined, and despite some d
istortion of particles during specimen preparation and viewing in the
microscope, the images obtained by cryo-HRSEM exhibited a level of int
erpretable detail not routinely achieved by other methods without imag
e averaging. Cryo-HRSEM images of discrete reovirus particles were use
d 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 oc
cur on the surfaces of individual reovirus particles during disassembl
y and entry of cells and that the reovirus outer capsid is organized a
s a left-handed T=13 icosahedron. Several unique capabilities and pote
ntial uses suggest that cryo-HRSEM has a place alongside other, more e
stablished methods for molecular characterizations of virus particles.
(C) 1995 Academic Press, Inc.