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Capsid assembly and DNA packaging in herpes simplex virus
Reviews in Medical Virology
|July 1, 1997
Summary
This review details the structure and assembly of the Herpes Simplex Virus type 1 (HSV-1) capsid. It summarizes knowledge on HSV-1 capsid proteins, assembly intermediates, and DNA packaging mechanisms.
Area of Science:
- Virology
- Structural Biology
- Molecular Biology
Background:
- The Herpes Simplex Virus type 1 (HSV-1) virion comprises a lipid envelope, tegument, icosahedral capsid, and DNA core.
- The HSV-1 capsid, composed of 162 capsomers, includes major protein VP5 and minor proteins VP19C, VP23, and VP26.
Purpose of the Study:
- To review current knowledge on the structure and assembly of the HSV-1 capsid.
- To summarize the roles of viral proteins and genetic factors in capsid formation and DNA packaging.
Main Methods:
- Cryoelectron microscopy has elucidated capsid shell structure.
- Recombinant baculoviruses facilitated analysis of capsid assembly proteins.
- An in vitro system identified assembly intermediates and maturation pathways.
Main Results:
- The HSV-1 capsid is an icosahedral structure with 162 capsomers.
- Assembly involves structural proteins, protease, scaffolding protein preVP22a, and seven DNA packaging proteins.
- An in vitro system revealed a procapsid intermediate that matures into the final capsid.
Conclusions:
- Significant progress has been made in understanding HSV-1 capsid structure and assembly.
- The identified assembly pathway and intermediates provide insights into viral morphogenesis.
- Further research on DNA packaging genes is ongoing.