The herpes simplex virus type 1 particle: structure and molecular functions. Review article.
This review is a summary of our present knowledge with respect to the structure of the virion of herpes simplex virus type 1. The virion consists of a capsid into which the DNA is packaged, a tegument and an external envelope. The protein compositions of the structures outside the genome are described as well as the functions of individual proteins. Seven capsid proteins are identified, and two of them are mainly present in precursors of mature DNA-containing capsids. The protein components of the 150 hexamers and 12 pentamers in the icosahedral capsid are known. These capsomers all have a central channel and are connected by Y-shaped triplexes. In contrast to the capsid, the tegument has a less defined structure in which 11 proteins have been identified so far. Most of them are phosphorylated. Eleven virus-encoded glycoproteins are present in the envelope, and there may be a few more membrane proteins not yet identified. Functions of these glycoproteins include attachment to and penetration of the cellular membrane. The structural proteins, their functions, coding genes and localizations are listed in table form.
National Centre for Research in Virology, University of Bergen, Norway.
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Haarr
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Skulstad
D002213:Capsid / Q000737:chemistry; D018259:Herpesvirus 1, Human / Q000737:chemistry / Q000648:ultrastructure; D014764:Viral Proteins / Q000737:chemistry; D014771:Virion / Q000737:chemistry / Q000648:ultrastructure*
D014764:Viral Proteins