Three-dimensional localization of the smallest capsid protein in the human cytomegalovirus capsid.
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.
Yu
Xuekui
X
Department of Pathology and Laboratory Medicine, University of Texas Medical School at Houston, 6431 Fannin St., MSB 2.280, Houston, TX 77030, USA.
Shah
Sanket
S
Atanasov
Ivo
I
Lo
Pierrette
P
Liu
Fenyong
F
Britt
William J
WJ
Zhou
Z Hong
ZH
D000595:Amino Acid Sequence; D002213:Capsid / Q000737:chemistry*; D036022:Capsid Proteins / Q000032:analysis* / Q000737:chemistry; D003587:Cytomegalovirus / Q000737:chemistry*; D006801:Humans; D007091:Image Processing, Computer-Assisted; D008854:Microscopy, Electron; D008969:Molecular Sequence Data
D036022:Capsid Proteins