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PLoS One. 2014 Feb 6;9(2):e88288. doi: 10.1371/journal.pone.0088288. eCollection 2014.

Morphology of influenza B/Lee/40 determined by cryo-electron microscopy.

Author information

1
Department of Microbiology and Immunology, Sophie Davis School of Biomedical Education, The City College of New York, New York, New York, United States of America.
2
Department of Computer Science, The Graduate Center, City University of New York, New York, New York, United States of America.
3
The New York Structural Biology Center, New York, New York, United States of America.
4
Department of Microbiology and Immunology, New York Medical College, Valhalla, New York, United States of America.
5
Department of Physics, The City College of New York, New York, New York, United States of America.

Abstract

Cryo-electron microscopy projection image analysis and tomography is used to describe the overall architecture of influenza B/Lee/40. Algebraic reconstruction techniques with utilization of volume elements (blobs) are employed to reconstruct tomograms of this pleomorphic virus and distinguish viral surface spikes. The purpose of this research is to examine the architecture of influenza type B virions by cryo-electron tomography and projection image analysis. The aims are to explore the degree of ribonucleoprotein disorder in irregular shaped virions; and to quantify the number and distribution of glycoprotein surface spikes (hemagglutinin and neuraminidase) on influenza B. Projection image analysis of virion morphology shows that the majority (∼83%) of virions are spherical with an average diameter of 134±19 nm. The aspherical virions are larger (average diameter = 155±47 nm), exhibit disruption of the ribonucleoproteins, and show a partial loss of surface protein spikes. A count of glycoprotein spikes indicates that a typical 130 nm diameter type B virion contains ∼460 surface spikes. Configuration of the ribonucleoproteins and surface glycoprotein spikes are visualized in tomogram reconstructions and EM densities visualize extensions of the spikes into the matrix. The importance of the viral matrix in organization of virus structure through interaction with the ribonucleoproteins and the anchoring of the glycoprotein spikes to the matrix is demonstrated.

PMID:
24516628
PMCID:
PMC3916419
DOI:
10.1371/journal.pone.0088288
[Indexed for MEDLINE]
Free PMC Article

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