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Virus-Cell Interactions

Pseudorabies Virus UL37 Gene Product Is Involved in Secondary Envelopment

Barbara G. Klupp, Harald Granzow, Egbert Mundt, Thomas C. Mettenleiter
Barbara G. Klupp
Institutes of Molecular Biology and
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Harald Granzow
Infectology,Friedrich-Loeffler-Institutes, Federal Research Centre for Virus Diseases of Animals, D-17498 Insel Riems, Germany
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Egbert Mundt
Institutes of Molecular Biology and
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Thomas C. Mettenleiter
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DOI: 10.1128/JVI.75.19.8927-8936.2001
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ABSTRACT

Herpesvirus envelopment is a two-step process which includes acquisition of a primary envelope resulting from budding of intranuclear capsids through the inner nuclear membrane. Fusion with the outer leaflet of the nuclear membrane releases nucleocapsids into the cytoplasm, which then gain their final envelope by budding intotrans-Golgi vesicles. It has been shown that the UL34 gene product is required for primary envelopment of the alphaherpesvirus pseudorabies virus (PrV) (B. G. Klupp, H. Granzow, and T. C. Mettenleiter, J. Virol. 74:10063–10073, 2000). For secondary envelopment, several virus-encoded PrV proteins are necessary, including glycoproteins E, I, and M (A. R. Brack, J. M. Dijkstra, H. Granzow, B. G. Klupp, and T. C. Mettenleiter, J. Virol. 73:5364–5372, 1999). We show here that the product of the UL37 gene of PrV, which is a constituent of mature virions, is involved in secondary envelopment. Replication of a UL37 deletion mutant, PrV-ΔUL37, was impaired in normal cells; this defect could be complemented on cells stably expressing UL37. Ultrastructural analysis demonstrated that intranuclear capsid maturation and budding of capsids into and release from the perinuclear space were unimpaired. However, secondary envelopment was drastically reduced. Instead, apparently DNA-filled capsids accumulated in the cytoplasm in large aggregates similar to those observed in the absence of glycoproteins E/I and M but lacking the surrounding electron-dense tegument material. Although displaying an ordered structure, capsids did not contact each other directly. We postulate that the UL37 protein is necessary for correct addition of other tegument proteins, which are required for secondary envelopment. In the absence of the UL37 protein, capsids interact with each other through unknown components but do not acquire the electron-dense tegument which is normally found around wild-type capsids during and after secondary envelopment. Thus, apposition of the UL37 protein to cytoplasmic capsids may be crucial for the addition of other tegument proteins, which in turn are able to interact with viral glycoproteins to mediate secondary envelopment.

  • Copyright © 2001 American Society for Microbiology
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Pseudorabies Virus UL37 Gene Product Is Involved in Secondary Envelopment
Barbara G. Klupp, Harald Granzow, Egbert Mundt, Thomas C. Mettenleiter
Journal of Virology Oct 2001, 75 (19) 8927-8936; DOI: 10.1128/JVI.75.19.8927-8936.2001

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Pseudorabies Virus UL37 Gene Product Is Involved in Secondary Envelopment
Barbara G. Klupp, Harald Granzow, Egbert Mundt, Thomas C. Mettenleiter
Journal of Virology Oct 2001, 75 (19) 8927-8936; DOI: 10.1128/JVI.75.19.8927-8936.2001
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KEYWORDS

Herpesvirus 1, Suid
viral structural proteins
virus assembly

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