The capsid and tegument of the alphaherpesviruses are linked by an interaction between the UL25 and VP1/2 proteins.
How alphaherpesvirus capsids acquire tegument proteins remains a key question in viral assembly. Using pseudorabies virus (PRV), we have previously shown that the 62 carboxy-terminal amino acids of the VP1/2 large tegument protein are essential for viral propagation and when transiently expressed as a fusion to green fluorescent protein relocalize to nuclear capsid assemblons following viral infection. Here, we show that localization of the VP1/2 capsid-binding domain (VP1/2cbd) into assemblons is conserved in herpes simplex virus type 1 (HSV-1) and that this recruitment is specifically on capsids. Using a mutant virus screen, we find that the protein product of the UL25 gene is essential for VP1/2cbd association with capsids. An interaction between UL25 and VP1/2 was corroborated by coimmunoprecipitation from cells transiently expressing either HSV-1 or PRV proteins. Taken together, these findings suggest that the essential function of the VP1/2 carboxy terminus is to anchor the VP1/2 tegument protein to capsids. Furthermore, UL25 encodes a multifunctional capsid protein involved in not only encapsidation, as previously described, but also tegumentation.
Coller
Kelly Elizabeth
KE
Department of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Lee
Joy I-Hsuan
JI
Ueda
Aki
A
Smith
Gregory Allan
GA
D018138:Alphaherpesvirinae / Q000737:chemistry / Q000502:physiology*; D000818:Animals; D002213:Capsid; D002460:Cell Line; D002522:Chlorocebus aethiops; D015967:Gene Expression Regulation, Viral; D047468:Immunoprecipitation; D009154:Mutation; D016366:Open Reading Frames; D011485:Protein Binding; D013552:Swine; D014709:Vero Cells; D014758:Viral Core Proteins / Q000737:chemistry*; D014764:Viral Proteins / Q000737:chemistry*
D014758:Viral Core Proteins; D014764:Viral Proteins; C069185:DNA cleavage and packaging proteins, Herpesvirus
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