Entry of alphaherpesviruses into the cell

Campadelli-Fiume, Gabriella; Menotti, Laura

doi:10.1017/cbo9780511545313.008

Cited by 23 publications

(37 citation statements)

References 150 publications

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“…In HSV-1 infected cells, various compartments are modified in order to render the cell a suitable microenvironment for virus replication, envelopment, and release (1,14,34). We searched for modifications of the late endosomes or MVB compartment by immunofluorescence with an antibody directed to LAMP-1, a marker of this organelle (27).…”

Section: Resultsmentioning

confidence: 99%

“…Herpesviridae are large DNA-containing enveloped viruses that share a number of properties, including basic mechanisms of virus entry, progeny virus assembly, and exit from the cell. Herpesviruses enter the cell by direct fusion with the plasma membrane or endocytic membranes (13,14). Progeny nucleocapsids are assembled in the nucleus and exit this compartment by budding at the inner nuclear membrane (51)(52)(53)(54).…”

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confidence: 99%

“…Progeny nucleocapsids are assembled in the nucleus and exit this compartment by budding at the inner nuclear membrane (51)(52)(53)(54). The subsequent steps in virus assembly and release remain controversial (12,14,54). The currently most credited view envisions that virions are de-enveloped at the outer nuclear membrane and that the de-enveloped capsids released into the cytoplasm undergo a second envelopment (51)(52)(53)(54).…”

mentioning

confidence: 99%

“…The site of cytoplasmic envelopment has not been completely characterized. The Golgi apparatus, trans-Golgi network (TGN) membranes, and occasionally endosomes are usually indicated as platforms for envelopment (1,6,14,34,46,54).…”

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confidence: 99%

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Intracellular Trafficking and Maturation of Herpes Simplex Virus Type 1 gB and Virus Egress Require Functional Biogenesis of Multivesicular Bodies

Calistri

Sette

Salata

et al. 2007

J Virol

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110

108

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Intracellular Trafficking and Maturation of Herpes Simplex Virus Type 1 gB and Virus Egress Require Functional Biogenesis of Multivesicular Bodies

Calistri

Sette

Salata

et al. 2007

J Virol

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110

108

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“…Alphaherpesviruses have been shown to enter cells by a number of different pathways that, with a few notable exceptions that include varicella zoster virus, are dependent on the same subset of viral glycoproteins, namely, glycoprotein D (gD), gB, gH, and gL, as well as cellular receptors and coreceptors (3,(6)(7)(8)(9). Previous studies with herpes simplex virus type 1 (HSV-1) have shown that the virus can enter many cell types, including primary neurons and Vero cells, via fusion with the plasma membrane at neutral pH (10)(11)(12).…”

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confidence: 99%

Glycoprotein H and α4β1 Integrins Determine the Entry Pathway of Alphaherpesviruses

Azab

Lehmann

Osterrieder

2013

J Virol

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c Herpesviruses enter cells either by direct fusion at the plasma membrane or from within endosomes, depending on the cell type and receptor(s). We investigated two closely related herpesviruses of horses, equine herpesvirus type 1 (EHV-1) and EHV-4, for which the cellular and viral determinants routing virus entry are unknown. We show that EHV-1 enters equine epithelial cells via direct fusion at the plasma membrane, while EHV-4 does so via an endocytic pathway, which is dependent on dynamin II, cholesterol, caveolin 1, and tyrosine kinase activity. Exchange of glycoprotein H (gH) between EHV-1 and EHV-4 resulted in rerouting of EHV-1 to the endocytic pathway, as did blocking of ␣4␤1 integrins on the cell surface. Furthermore, a point mutation in the SDI integrin-binding motif of EHV-1 gH also directed EHV-1 to the endocytic pathway. Cumulatively, we show that viral gH and cellular ␣4␤1 integrins are important determinants in the choice of alphaherpesvirus cellular entry pathways.

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The multipartite system that mediates entry of herpes simplex virus into the cell

Campadelli-Fiume

Amasio

Avitabile

et al. 2007

Reviews in Medical Virology

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130

106

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The multipartite entry-fusion system of herpes simplex virus is made of a quartet of glycoproteins-gD, gB, gH.gL-and three alternative gD receptors, herpesvirus entry mediator (HVEM), nectin1 and modified sites on heparan sulphate. This multipartite system recapitulates the basic steps of virus-cell fusion, i.e. receptor recognition, triggering of fusion and fusion execution. Specifically, in addition to serving as the receptor-binding glycoprotein, gD triggers fusion through a specialised domain, named pro-fusion domain (PFD), located C-terminally in the ectodomain. In the unliganded gD the C-terminal region folds around the N-terminal region, such that gD adopts a closed autoinhibited conformation. In HVEM- and nectin1-bound gD the C-terminal region is displaced (opened conformation). gD is the tool for modification of HSV tropism, through insertion of ligands to heterologous tumour-specific receptors. It is discussed whether gD responds to the interaction with the natural and the heterologous receptors by adopting similar conformations, and whether the closed-to-open switch in conformation is a generalised mechanism of activation. A peculiar recombinant highlighted that the central Ig-folded core of gD may not encode executable functions for entry and that the 219-314 aa segment may be sufficient to trigger fusion. With respect to fusion execution, gB appears to be a prospective fusogen based on its coiled-coil trimeric structure, similar to that of another fusion glycoprotein. On the other hand, gH exhibits molecular elements typical of class 1 fusion glycoproteins, in particular heptad repeats and strong tendency to interact with lipids. Whether fusion execution is carried out by gB or gH.gL, or both glycoproteins in complex or sequentially remains to be determined.

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Entry of alphaherpesviruses into the cell

Cited by 23 publications

References 150 publications

Intracellular Trafficking and Maturation of Herpes Simplex Virus Type 1 gB and Virus Egress Require Functional Biogenesis of Multivesicular Bodies

Intracellular Trafficking and Maturation of Herpes Simplex Virus Type 1 gB and Virus Egress Require Functional Biogenesis of Multivesicular Bodies

Glycoprotein H and α4β1 Integrins Determine the Entry Pathway of Alphaherpesviruses

The multipartite system that mediates entry of herpes simplex virus into the cell

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