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The Structure of Ppv0l, A Marine Algal Virus with a T=219 Capsid

Published online by Cambridge University Press:  02 July 2020

X. Yan
Affiliation:
Department of Biological Sciences, Purdue University, West Lafayette, IN, 47907
P. Chipman
Affiliation:
Department of Biological Sciences, Purdue University, West Lafayette, IN, 47907
T. Castberg
Affiliation:
Department of Microbiology, University of Bergen, N-5020, Bergen, Norway
G. Bratbak
Affiliation:
Department of Microbiology, University of Bergen, N-5020, Bergen, Norway
T. S. Baker
Affiliation:
Department of Biological Sciences, Purdue University, West Lafayette, IN, 47907
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Abstract

Phaeocystispouchetii virus (PpV0l), first isolated from Norwegian coastal water in 1995, infects and lyses the haptophyte Phaeocystis pouchetii Lagerheim. PpV0l has not yet been assigned to a family. Phaeocystis may play an important role in ocean climate control and PpV0l infection could alter the amount of this haptophyte. The virion contains a dsDNA genome (∼450 kbps) encapsulated within a large icosahedral shell. The most abundant protein has a mass of 59 kDa. More than five minor polypeptides with masses ranging from 30 to 50 kDa have also been identified. We have used cryo-electron microscopy (cryo-EM) and three-dimensional (3D) image reconstruction methods to examine the native morphology of PpV0l.

Purified PpV0l samples were prepared for Cryo-EM as described. Images were recorded on film at 33,000x nominal magnification in a Philips CM300 FEG microscope at 300kV, at 1.0μm to 2.0μm under focus, and with an electron dose of 2200e-/nm2 (Fig. 1A).

Type
Microbiology
Copyright
Copyright © Microscopy Society of America 2001

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References

1.Jacobsen, A., J. Phycol. 32(1996)923.CrossRefGoogle Scholar
2.Adrian, M. et al, Nature 308(1984)32CrossRefGoogle Scholar
3.Baker, T. S. and Cheng, R. H., J. Struct. Biology 116(1996)120.CrossRefGoogle Scholar
4.Fuller, S. D. et al, J. Struct. Biology 116(1996)48.CrossRefGoogle Scholar
5.Toyoshima, C. et al., Ultramicrosc. 48(1993)165.CrossRefGoogle Scholar
6.Caspar, D. L. D., and Klug, A., Cold Spring Harb. Symp. Quant. Biol. 27(1962)1.CrossRefGoogle Scholar
7.Yan, X. et al., Nature Structural Biology 7(2000)101.Google Scholar
8.We thank R. Ashmore for assistance with programming. Work supported in part by grants from the NIH (GM-33050) and AI-45976 and NSF (MCB-9527131) to T.S.B. and by a grant from The Research Council of Norway (project no.121425/420) and an award to Purdue Structural Biology Group from the Keck Foundation.Google Scholar