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Review
. 2002 Feb;76(4):1537-47.
doi: 10.1128/jvi.76.4.1537-1547.2002.

Herpesvirus assembly and egress

Thomas C Mettenleiter  1
Affiliations
Review

Herpesvirus assembly and egress

Thomas C Mettenleiter. J Virol. 2002 Feb.
No abstract available

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Figures

FIG. 1.
FIG. 1.
Assembly and egress of HSV-1. Electron microscopic illustration of intranuclear capsid assembly (A), budding of capsid at the inner nuclear membrane (B), perinuclear primary enveloped virion in the perinuclear space (C), and fusion of primary envelope with the outer nuclear membrane (D). In a rare picture, budding at the inner nuclear membrane and fusion at the outer nuclear membrane of HSV-1 capsids has been observed in the same section (E; taken, with permission, from reference 34). (F) Overview of HSV-1 morphogenesis events in the cytoplasm. Secondary envelopment of intracytoplasmic capsids by budding into vesicles (F inset, G) results in complete enveloped virions inside exocytic vesicles (H). Fusion of the vesicle membrane with the plasma membrane then leads to release of mature virions (I and J). Bars, 150 nm in panels A to E, panel F inset, and panels G and H and 750 nm in panel F.
FIG. 2.
FIG. 2.
Assembly and egress of ILTV and mutant PrV. Intranuclear assembly (A), formation of perinuclear virions (B and C), and fusion with the outer nuclear membrane (D) do not differ morphologically from those of the other alphaherpesviruses examined (34). However, large amounts of tegument material may be incorporated into virions (G and H), which is clearly observed to occur in the cytoplasm only (E to F; see also reference 34). (G) An enveloped ILTV virion inside a vesicle. (H) An extracellular released virion. In panel E on the right, a capsidless L particle is demonstrated. (I) Intracytoplasmic PrV capsid accumulations without apparent tegument in the absence of the UL37 protein (45). (J) Accumulations of tegumented PrV capsids in the absence of gE/gI and gM (6). Bars, 150 nm in panels A to H and 250 nm in panels I and J.
FIG. 3.
FIG. 3.
Diagram of the interactions of gene products of HSV-1 and PrV involved in virion formation. Solid lines or direct contacts between the rectangles representing the designated gene products indicate physical interaction, whereas arrows indicate functional effects. Dotted lines and question marks denote suggested, but not firmly established, interactions or involvement of proteins. Between glycoproteins, only direct contacts resulting in complex formation are depicted. Steps: 1, primary envelopment; 2, de-envelopment; 3, secondary (final) envelopment. NUC, nucleus; CYT, cytoplasm.
FIG. 4.
FIG. 4.
Summary diagram of the proposed pathway of herpesvirus egress.
See this image and copyright information in PMC

References

    1. Avitabile, E., P. Ward, C. Di Lazzaro, M. Torrisi, B. Roizman, and G. Campadelli-Fiume. 1994. The herpes simplex virus UL20 protein compensates for the differential disruption of exocytosis of virions and viral membrane glycoproteins associated with fragmentation of the Golgi apparatus. J. Virol. 68:7397-7405. - PMC - PubMed
    1. Baines, J. D., P. L. Ward, G. Campadelli-Fiume, and B. Roizman. 1991. The UL20 gene of herpes simplex virus 1 encodes a function necessary for viral egress. J. Virol. 65:6414-6424. - PMC - PubMed
    1. Baines, J. D., and B. Roizman. 1992. The UL11 gene of herpes simplex virus 1 encodes a function that facilitates nucleocapsid envelopment and egress from cells. J. Virol. 66:5168-5174. - PMC - PubMed
    1. Batterson, W., and B. Roizman. 1983. Characterization of the herpes simplex virion-associated factor responsible for the induction of α genes. J. Virol. 46:371-377. - PMC - PubMed
    1. Baxter, M. K., and W. Gibson. 2001. Cytomegalovirus basic phosphoprotein (pUL32) binds to capsids in vitro through its amino one-third. J. Virol. 75:6865-6873. - PMC - PubMed

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