Abstract
Herpes viruses are prevalent and well characterized human pathogens. Despite extensive study, much remains to be learned about the structure of the genome packaging and release machinery in the capsids of these large and complex double-stranded DNA viruses. However, such machinery is well characterized in tailed bacteriophage, which share a common evolutionary origin with herpesvirus. In tailed bacteriophage, the genome exits from the virus particle through a portal and is transferred into the host cell by a complex apparatus (i.e. the tail) located at the portal vertex. Here we use electron cryo-tomography of human herpes simplex type-1 (HSV-1) virions to reveal a previously unsuspected feature at the portal vertex, which extends across the HSV-1 tegument layer to form a connection between the capsid and the viral membrane. The location of this assembly suggests that it plays a role in genome release into the nucleus and is also important for virion architecture.
Highlights
Human herpesviruses cause a range of diseases from cold sores and chicken pox to congenital defects, blindness, and cancer [1]
This paper describes a previously unrecognized feature within the tegument of Herpes simplex virus type-1 (HSV-1) virions, which, by analogy with tailed bacteriophages, may mediate interactions between the portal vertex and cellular components at key points in the viral life cycle
Herpes Simplex Virus (HSV)-1 virions were collected while the sample was rotated through 120u (Video S1)
Summary
Human herpesviruses cause a range of diseases from cold sores and chicken pox to congenital defects, blindness, and cancer [1]. Electron cryo-microscopic (cryo-EM) and electron cryo-tomographic (cryo-ET) methods have been developed to allow visualization of nonicosahedral features in such particles This has allowed the DNA packaging and release machinery (e.g. portal and tail components) of tailed bacteriophages to be studied in detail [7,8,9,10,11,12]. Evolutionary and structural links between tailed bacteriophages and herpesviruses suggest that equivalent machinery might be present in herpesvirus particles. This assumption is reinforced by the structural description of the HSV-1 portal as occupying a similar position and with a similar subunit organization as that of the tailed bacteriophages [3,6,13]. This paper describes a previously unrecognized feature within the tegument of HSV-1 virions, which, by analogy with tailed bacteriophages, may mediate interactions between the portal vertex and cellular components at key points in the viral life cycle
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