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Updated: Jun 19, 2026
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A Miniaturized Glycan Microarray Assay for Assessing Avidity and Specificity of Influenza A Virus Hemagglutinins
Published on: May 29, 2016
THE SIZE OF INFLUENZA VIRUS.
1Department of Animal and Plant Pathology of The Rockefeller Institute for Medical Research, Princeton, New Jersey.
The Journal of Experimental Medicine
|October 30, 2009
Summary
Influenza virus activity is primarily associated with larger particles (approx. 70 nm diameter, 600 S sedimentation) rather than smaller ones (approx. 10 nm diameter, 30 S sedimentation). Variable sedimentation in electrolyte solutions was attributed to experimental disturbances, not inherent virus properties.
Area of Science:
- Virology
- Biochemistry
- Ultracentrifugation
Background:
- Influenza virus sedimentation behavior in electrolyte solutions is variable.
- High molecular weight proteins in infected allantoic fluid exist as distinct components.
Purpose of the Study:
- To elucidate the true sedimentation behavior of influenza virus.
- To identify which protein component possesses virus activity.
Main Methods:
- Ultracentrifugation in dilute electrolyte solutions and sucrose density gradients.
- Differential centrifugation for purification of protein components.
- Assay of specific virus activity in purified fractions.
Main Results:
- Variable sedimentation in electrolyte solutions was due to disturbances; sucrose gradients showed consistent sedimentation (approx. 80-120 nm).
- Allantoic fluid contains 600 S (approx. 70 nm) and 30 S (approx. 10 nm) protein components.
- The 600 S component exhibited significantly higher specific virus activity than the 30 S component.
Conclusions:
- Influenza virus activity is solely associated with the 600 S component (approx. 70 nm diameter).
- The 30 S component does not represent infectious influenza virus particles.
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