The egress of alphaherpesviruses from the cell
- PMID: 21348111
- Bookshelf ID: NBK47427
The egress of alphaherpesviruses from the cell
Excerpt
A commonly accepted concept in herpesvirology holds that herpesvirions are formed by budding of nucleocapsids at the inner nuclear membrane and the enveloped virions are released into the perinuclear space (see Chapter 13). This is a closed compartment that virions need to exit, in order to reach the extracellular space and start a new infection cycle. How alphaherpesviruses accomplish this goal is a controversial issue. Of the two pathways of virus exit proposed, the single envelopment and the double envelopment, also referred to as de-envelopment–re-envelopment, each has evidence and supporters in the literature (the topic has been covered in excellent reviews and papers (Enquist et al., ; Skepper et al., ; Johnson and Huber, ; Mettenleiter, 2002). Part of the uncertainties that still dominate this topic comes from the difficulties in interpreting static electron microscopy images. Thus cytoplasmic virions juxtaposed to curved vesicles were interpreted in some studies as budding virions, i.e., as evidence for secondary envelopment and for the deenvelopment-reenvelopment pathway. In other studies they were interpreted as virions undergoing fusion with encasing vesicles, i.e., as evidence of de-envelopment (Campadelli-Fiume et al, : Roizman and Knipe, 2001). To solve these ambiguities, several approaches have been undertaken in recent years, including the generation of genetically modified mutants and cytochemistry.
Copyright © Cambridge University Press 2007.
Sections
Similar articles
-
Endoplasmic reticulum-to-Golgi transitions upon herpes virus infection.F1000Res. 2017 Oct 5;6:1804. doi: 10.12688/f1000research.12252.2. eCollection 2017. F1000Res. 2017. PMID: 30135710 Free PMC article.
-
Herpes Simplex Virus 1 Recruits CD98 Heavy Chain and β1 Integrin to the Nuclear Membrane for Viral De-Envelopment.J Virol. 2015 Aug;89(15):7799-812. doi: 10.1128/JVI.00741-15. Epub 2015 May 20. J Virol. 2015. PMID: 25995262 Free PMC article.
-
Herpes simplex virus 1 envelopment follows two diverse pathways.J Virol. 2005 Oct;79(20):13047-59. doi: 10.1128/JVI.79.20.13047-13059.2005. J Virol. 2005. PMID: 16189007 Free PMC article.
-
Intriguing interplay between viral proteins during herpesvirus assembly or: the herpesvirus assembly puzzle.Vet Microbiol. 2006 Mar 31;113(3-4):163-9. doi: 10.1016/j.vetmic.2005.11.040. Epub 2005 Dec 5. Vet Microbiol. 2006. PMID: 16330166 Review.
-
Budding events in herpesvirus morphogenesis.Virus Res. 2004 Dec;106(2):167-80. doi: 10.1016/j.virusres.2004.08.013. Virus Res. 2004. PMID: 15567495 Review.
References
-
- Ace C. I., Dalrymple M. A., Ramsay F. H., Preston V. G., Preston C. M. Mutational analysis of the herpes simplex virus type 1 trans-inducing factor Vmw65. J. Gen. Virol. 1988;69(10):2595–2605. - PubMed
-
- Alconada A., Bauer U., Baudoux L., Piette J., Hoflack B. Intracellular transport of the glycoproteins gE and gI of the varicella-zoster virus. gE accelerates the maturation of gI and determines its accumulation in the trans-Golgi network. J. Biol. Chem. 1998;273:13430–13436. - PubMed
-
- Avitabile E., Ward P. L., Lazzaro, Torrisi M. R., Roizman B., Campadelli-Fiume G. The herpes simplex virus UL20 protein compensates for the differential disruption of exocytosis of virions and membrane glycoproteins associated with fragmentation of the Golgi apparatus. J. Virol. 1994a;68:7397–7405. - PMC - PubMed
Publication types
LinkOut - more resources
Full Text Sources