Consideration of the three dimensional structure of the adenovirus hexon from electron microscopy and computer modelling |
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| Affiliation: | 1. Loyola University Chicago, 2016 S. First Avenue, Maywood, IL 60153, USA;2. The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA;1. Departamento de Física de la Materia Condensada, Universidad Autónoma de Madrid and IFIMAC, 28049 Madrid, Spain;2. Departamento de Estructura de Macromoléculas, Centro Nacional de Biotecnología (CNB-CSIC), Darwin 3, 28049 Madrid, Spain;3. Biomolecular Mass Spectrometry and Proteomics, Bijvoet Centre for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Padualaan 8, 3584 CH Utrecht, The Netherlands,;4. Netherlands Proteomics Center, Padualaan 8, 3584 CH, Utrecht, The Netherlands,;5. Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, California 92037, and;6. Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California 92037 |
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| Abstract: | A three-dimensional model of the adenovirus hexon has been built up from electron microscopic observations and information obtained by computer modelling. It has been shown that the hexons (in upright position) are negatively stained from below and that stain layer after drying is only 1–2nm high. Thus the top, i.e. the external part, of the hexon is triangular, the waist is hexagonal and the bottom is ‘round’ with a large axial hole. The top is twisted through 30° with respect to the waist. This morphological polarity is accompanied by differences in physico-chemical properties: the top appears to be negatively charged at neutral pH, whereas the bottom is rather hydrophobic. Because of the hexagonal region at the waist of the hexon the virus capsid becomes sealed allowing passage of small molecules only, presumably via a narrow central channel. |
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