Three-Dimensional Localization of the Smallest Capsid Protein in the Human Cytomegalovirus Capsid

AUTOR(ES)

Yu, Xuekui

FONTE

American Society for Microbiology

RESUMO

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.

Documentos Relacionados

• Three-Dimensional Structure of the Human Herpesvirus 8 Capsid
• Three-Dimensional Localization of pORF65 in Kaposi's Sarcoma-Associated Herpesvirus Capsid
• The three-dimensional structure of retinol-binding protein.
• Three-dimensional model of the potyviral genome-linked protein.
• The three-dimensional structure of P2 myelin protein.