Surface processes in the crystallization of turnip yellow mosaic virus visualized by atomic force microscopy.
In situ atomic force microscopy (AFM) was used to investigate surface evolution during the growth of single crystals of turnip yellow mosaic virus (TYMV). Growth of the (101) face of TYMV crystals proceeded by two-dimensional nucleation. The molecular structure of the step edges and adsorption of individual virus particles and their aggregates on the crystalline surface were recorded. The surfaces of individual virions within crystals were visualized and seen to be quite distinctive with the hexameric and pentameric capsomers of the T = 3 capsids being clearly resolved. This, so far as we are aware, is the first direct visualization of the capsomere structure of a virus by AFM. In the course of recording the in situ development of the crystals, a profound restructuring of the surface arrangement was observed. This transformation was highly cooperative in nature, but the transitions were unambiguous and readily explicable in terms of an organized loss of classes of virus particles from specific lattice positions. In some cases areas of a single crystal surface were recorded in which were captured successive phases of the transition. We believe this provides the first visual record of a cooperative restructuring of the surface of a supramolecular crystal.
Malkin
A J
AJ
Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, California, 92697-3900, USA. amalkin@uci.edu
Kuznetsov
Y G
YG
Lucas
R W
RW
McPherson
A
A
D002213:Capsid / Q000378:metabolism / Q000648:ultrastructure; D003460:Crystallization; D018625:Microscopy, Atomic Force; D013499:Surface Properties; D017806:Tymovirus / Q000737:chemistry* / Q000648:ultrastructure*; D014771:Virion / Q000378:metabolism / Q000648:ultrastructure