Open AccessThree-Dimensional Localization of the Smallest Capsid Protein in the Human Cytomegalovirus Capsid
Author(s) -
Xuekui Yu,
Sanket Shah,
Ivo Atanasov,
Pierrette Lo,
Fenyong Liu,
William J. Britt,
Zhen Zhou
Publication year - 2005
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.79.2.1327-1332.2005
Subject(s) - capsid , biology , human cytomegalovirus , cytomegalovirus , virology , cryo electron microscopy , sequence (biology) , function (biology) , virus , microbiology and biotechnology , computational biology , herpesviridae , biophysics , genetics , viral disease
The smallest capsid proteins (SCPs) of the human herpesviruses differ substantially in size and sequence and are thought to impart some unique aspects of infection to their respective viruses. We used electron cryomicroscopy and antibody labeling to show that the 8-kDa SCP of human cytomegalovirus is attached only to major capsid protein subunits of the hexons, not the pentons. Thus, the SCPs of different herpesviruses illustrate that a protein can evolve significantly in sequence, structure, and function, while preserving its role in the architecture of the virus by binding to a specific partner in a specific oligomeric state.