Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-03

AUTHORS

B. Böttcher, S. A. Wynne, R. A. Crowther

ABSTRACT

Hepatitis B virus, a major human pathogen with an estimated 300 million carriers worldwide, can lead to cirrhosis and liver cancer in cases of chronic infection. The virus consists of an inner nucleocapsid or core, surrounded by a lipid envelope containing virally encoded surface proteins. The core protein, when expressed in bacteria, assembles into core shell particles, closely resembling the native core of the virus. Here we use electron cryomicroscopy to solve the structure of the core protein to 7.4 Å resolution. Images of about 6,400 individual particles from 34 micrographs at different levels of defocus were combined, imposing icosahedral symmetry. The three-dimensional map reveals the complete fold of the polypeptide chain, which is quite unlike previously solved viral capsid proteins and is largely α-helical. The dimer clustering of subunits produces spikes on the surface of the shell, which consist of radial bundles of four long α-helices. Our model implies that the sequence corresponding to the immunodominant region of the core protein lies at the tip of the spike and also explains other properties of the core protein. More... »

PAGES

88-91

Journal

TITLE

Nature

ISSUE

6620

VOLUME

386

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/386088a0

DOI

http://dx.doi.org/10.1038/386088a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1050523440

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9052786


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