Understanding HSV‐1 entry glycoproteins

Reske, Adi; Pollara, Gabriele; Krummenacher, Claude; Chain, Benjamin M.; Katz, David R.

doi:10.1002/rmv.531

Cited by 96 publications

(92 citation statements)

References 99 publications

(112 reference statements)

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“…Despite the absence of a transmembrane domain predicted using the usual prediction software, this protein was classified as a putative membrane protein on the basis of previous predictions for CyHV-3 proteins by Aoki et al (2007), which depended on the experimental findings of Davison & Davison (1995) for IcHV-1. It is possible that this protein associates with another membrane protein to form a complex exposed on the viral envelope, as observed for glycoprotein L of mammalian herpesviruses (Reske et al, 2007). A family of four paralogous proteins was detected in Table 1).…”

Section: B Michel and Othersmentioning

confidence: 92%

The genome of cyprinid herpesvirus 3 encodes 40 proteins incorporated in mature virions

Michel

Leroy

Raj

et al. 2009

Journal of General Virology

112

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Koi herpesvirus, also known as cyprinid herpesvirus 3 (CyHV-3), is the aetiological agent of an emerging and mortal disease in common and koi carp. CyHV-3 virions present the characteristic morphology of other members of the order Herpesvirales, being composed of an envelope, a capsid containing the genome and a tegument. This study identified CyHV-3 structural proteins and the corresponding encoding genes using liquid chromatography tandem mass spectrometrybased proteomic approaches. In addition, exponentially modified protein abundance index analyses were used to estimate the relative abundance of the identified proteins in CyHV-3 virions. These analyses resulted in the identification of 40 structural proteins, which were classified based on bioinformatic analyses as capsid (three), envelope (13), tegument (two) and unclassified (22) structural proteins. Finally, a search for host proteins in purified CyHV-3 virions indicated the potential incorporation of up to 18 distinct cellular proteins. The identification of the proteins incorporated into CyHV-3 virions and determination of the viral genes encoding these proteins are key milestones for further fundamental and applied research on this virus.

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Section: B Michel and Othersmentioning

confidence: 92%

The genome of cyprinid herpesvirus 3 encodes 40 proteins incorporated in mature virions

Michel

Leroy

Raj

et al. 2009

Journal of General Virology

112

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“…It is mediated by the sequential interaction of viral glycoproteins with their cognate receptors in the various organelles and compartments of the target cells as recently reviewed (5,20,34,35,38). Herpesviruses undergo fusion with different types of cell membranes.…”

Section: Epstein-barr Virus (Ebv) Infection Is Mediated By Several VImentioning

confidence: 99%

Primary B-Cell Infection with a ΔBALF4 Epstein-Barr Virus Comes to a Halt in the Endosomal Compartment yet Still Elicits a Potent CD4-Positive Cytotoxic T-Cell Response

Nęuhierl

Feederle

Adhikary

et al. 2009

J Virol

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Epstein-Barr virus (EBV) infection is mediated by several viral envelope glycoproteins.We have assessed gp110's functions during the virus life cycle using a mutant that lacks BALF4 (⌬BALF4). Exposure of various cell lines and primary cell samples of epithelial or lymphoid lineages to the ⌬BALF4 mutant failed to establish stable infections. The ⌬BALF4 virus, however, did not differ from wild-type EBV in its ability to bind and become internalized into primary B cells, in which it elicited a potent T-cell-specific immune reaction against virion constituents. These findings show that ⌬BALF4 viruses can reach the endosome-lysosome compartment and dovetail nicely with the previously identified contribution of gp110 to virus-cell fusion. Other essential steps of the virus life cycle were unaffected in the viral mutant; DNA lytic replication and viral titers were not altered in the absence of gp110, and ⌬BALF4 viruses complemented in trans transformed infected B cells with an efficiency indistinguishable from that observed with wild-type viruses. All of the steps of virus maturation could be observed in lytically induced 293/⌬BALF4 cells. Induction of lymphoblastoid cells generated with transiently complemented ⌬BALF4 virus led to the production of rare mature virions. We therefore infer that gp110 is not required for virus maturation and egress in 293 cells or in B cells. The ⌬BALF4 virus's phenotypic traits, an inability to infect human cells coupled with potent antigenicity, potentially qualify this mutant as a live vaccine. It will provide a useful tool for the detailed study of EBV-cell interactions in a physiological context.Herpesvirus cell entry is a multistep process that includes virus binding and fusion with its target cell as well as transport of the viral DNA to the cell nucleus. It is mediated by the sequential interaction of viral glycoproteins with their cognate receptors in the various organelles and compartments of the target cells as recently reviewed (5,20,34,35,38). Herpesviruses undergo fusion with different types of cell membranes. Herpes simplex virus 1 (HSV-1) classically fuses with the plasma membrane of its target cell, but an alternative infection route through the endosomal compartment may involve fusion with the endosomal-lysosomal membranes (6). The EpsteinBarr herpesvirus (EBV) invades primary B cells after attaching to CD21, which sets off internalization and transport to the endosome within vesicles (30). B-cell lines, such as Burkitt's lymphoma cell line Raji, however, differ from their primary cell correspondents in that both cell membrane binding and fusion take place at the plasma membrane surface (28,36). How EBV infects primary epithelial cells is less well documented, but fusion with the plasma cell membrane is the currently favored model (20,31). The extensive differences in the biochemical composition of plasma and endosomal membranes renders it likely that the process of fusion of these two membrane types with virions is mediated by distinct cellular or even viral interactio...

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“…Viral structural proteins have vital roles in cell targeting, viral entry, assembly, and budding (52), as well as triggering host antiviral defenses (53). Some WSSV envelope proteins involved in shrimp infection have been identified (54).…”

Section: Discussionmentioning

confidence: 99%

Prohibitin Interacts with Envelope Proteins of White Spot Syndrome Virus and Prevents Infection in the Red Swamp Crayfish, Procambarus clarkii

Lan

Sun

et al. 2013

J Virol

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b Prohibitins (PHBs) are ubiquitously expressed conserved proteins in eukaryotes that are associated with apoptosis, cancer formation, aging, stress responses, cell proliferation, and immune regulation. However, the function of PHBs in crustacean immunity remains largely unknown. In the present study, we identified a PHB in Procambarus clarkii red swamp crayfish, which was designated PcPHB1. PcPHB1 was widely distributed in several tissues, and its expression was significantly upregulated by white spot syndrome virus (WSSV) challenge at the mRNA level and the protein level. These observations prompted us to investigate the role of PcPHB1 in the crayfish antiviral response. Recombinant PcPHB1 (rPcPHB1) significantly reduced the amount of WSSV in crayfish and the mortality of WSSV-infected crayfish. The quantity of WSSV in PcPHB1 knockdown crayfish was increased compared with that in the controls. The effects of RNA silencing were rescued by rPcPHB1 reinjection. We further confirmed the interaction of PcPHB1 with the WSSV envelope proteins VP28, VP26, and VP24 using pulldown and far-Western overlay assays. Finally, we observed that the colloidal gold-labeled PcPHB1 was located on the outer surface of the WSSV, which suggests that PcPHB1 specifically binds to the envelope proteins of WSSV. VP28, VP26, and VP24 are structural envelope proteins and are essential for attachment and entry into crayfish cells. Therefore, PcPHB1 exerts its anti-WSSV effect by binding to VP28, VP26, and VP24, preventing viral infection. This study is the first report on the antiviral function of PHB in the innate immune system of crustaceans.

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Understanding HSV‐1 entry glycoproteins

Cited by 96 publications

References 99 publications

The genome of cyprinid herpesvirus 3 encodes 40 proteins incorporated in mature virions

The genome of cyprinid herpesvirus 3 encodes 40 proteins incorporated in mature virions

Primary B-Cell Infection with a ΔBALF4 Epstein-Barr Virus Comes to a Halt in the Endosomal Compartment yet Still Elicits a Potent CD4-Positive Cytotoxic T-Cell Response

Prohibitin Interacts with Envelope Proteins of White Spot Syndrome Virus and Prevents Infection in the Red Swamp Crayfish, Procambarus clarkii

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