Anti-idiotypic antibodies mimicking glycoprotein D of herpes simplex virus identify a cellular protein required for virus spread from cell to cell and virus-induced polykaryocytosis.

Huang, Tianmin; Campadelli-Fiume, Gabriella

doi:10.1073/pnas.93.5.1836

Cited by 28 publications

(17 citation statements)

References 24 publications

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“…The fusion of the viral envelope with the plasma membrane requires gD, gB, gH, and gL (49-51). These four viral glycoproteins also participate in cell-cell spread (3,11,20,28,36,40). Cell-cell spread furthermore requires gE and gI (1, 8-10), but these glycoproteins are not required for entry (8).…”

mentioning

confidence: 99%

Requirement of Interaction of Nectin-1α/HveC with Afadin for Efficient Cell-Cell Spread of Herpes Simplex Virus Type 1

Sakisaka

Taniguchi

Nakanishi

et al. 2001

J Virol

122

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We recently found a novel cell-cell adhesion system at cadherin-based adherens junctions (AJs), consisting at least of nectin, a Ca 2؉ -independent homophilic immunoglobulin-like adhesion molecule, and afadin, an actin filament-binding protein that connects nectin to the actin cytoskeleton. Nectin is associated with cadherin through afadin and ␣-catenin. The cadherin-catenin system increases the concentration of nectin at AJs in an afadin-dependent manner. Nectin constitutes a family consisting of three members: nectin-1, -2, and -3. Nectin-1 serves as an entry and cell-cell spread mediator of herpes simplex virus type 1 (HSV-1). We studied here a role of the interaction of nectin-1␣ with afadin in entry and/or cell-cell spread of HSV-1. By the use of cadherin-deficient L cells overexpressing the full length of nectin-1␣ capable of interacting with afadin and L cells overexpressing a truncated form of nectin-1␣ incapable of interacting with afadin, we found that the interaction of nectin-1␣ with afadin increased the efficiency of cell-cell spread, but not entry, of HSV-1. This interaction did not affect the binding to nectin-1␣ of glycoprotein D, a viral component mediating entry of HSV-1 into host cells. Furthermore, the cadherin-catenin system increased the efficiency of cell-cell spread of HSV-1, although it also increased the efficiency of entry of HSV-1. It is likely that efficient cell-cell spread of HSV-1 is caused by afadin-dependent concentrated localization of nectin-1␣ at cadherin-based AJs.Herpes simplex viruses (HSVs) are members of the neurotropic subfamily (alphaherpesviruses) of the herpesvirus family. Infection with HSV type 1 (HSV-1) is prevalent. HSV-1 infects cells through initial attachment to the plasma membrane and subsequent fusion of the viral envelope with the plasma membrane or through contiguous cell-cell spread. The entry pathway of HSV-1 is divided into three major processes: binding, fusion, and capsid penetration. These processes require several viral envelope glycoproteins (49-51). The initial attachment is mediated through glycoprotein C (gC) and/or gB to cell surface heparan sulfate proteoglycans (17,18,45), but this attachment is not sufficient for virus penetration (3,11,22,27). The fusion of the viral envelope with the plasma membrane requires gD, gB, gH, and gL (49-51). These four viral glycoproteins also participate in cell-cell spread (3,11,20,28,36,40). Cell-cell spread furthermore requires gE and gI (1, 8-10), but these glycoproteins are not required for entry (8). Thus, entry and cell-cell spread of HSV-1 share similar processes, but these pathways also differ in some significant aspects.Recently, expression cloning has led to the identification and isolation of HSV entry mediators (5,12,33,46,51). The human receptors identified include a lymphotoxin receptor (31), designated HVEM (33, 65) or HSV entry mediator A (HveA), which belongs to the tumor necrosis factor receptor family; two members of the immunoglobulin (Ig) superfamily (5,12,48,62); and 3-O-sulfated heparan ...

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confidence: 99%

Requirement of Interaction of Nectin-1α/HveC with Afadin for Efficient Cell-Cell Spread of Herpes Simplex Virus Type 1

Sakisaka

Taniguchi

Nakanishi

et al. 2001

J Virol

122

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“…Thus, mutant viruses with deletions in each glycoprotein are defective in both processes (3,14,26,44). Antibodies to the glycoproteins block both steps (16,19,21,35,38,39). A case in point is gD.…”

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confidence: 99%

“…A case in point is gD. Soluble forms of gD or anti-idiotypic antibodies mimicking gD inhibit both virus entry and cell-tocell transmission (21,22,36).…”

mentioning

confidence: 99%

Cell-to-Cell Spread of Wild-Type Herpes Simplex Virus Type 1, but Not of Syncytial Strains, Is Mediated by the Immunoglobulin-Like Receptors That Mediate Virion Entry, Nectin1 (PRR1/HveC/HIgR) and Nectin2 (PRR2/HveB)

Cocchi

Menotti

Dubreuil

et al. 2000

J Virol

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The immunoglobulin-like receptors that mediate entry of herpes simplex virus type 1 (HSV-1) into human cells were found to mediate the direct cell-to-cell spread of wild-type virus. The receptors here designated Nectin1␣ and -␦ and Nectin2␣ were originally designated HIgR, PRR1/HveC, and PRR2␣/HveB, respectively. We report the following. In cell culture, herpes simplex virus type 1 (HSV-1) infects cells through initial attachment and subsequent fusion of the virion envelope with the plasma membrane, or through contiguous cell-to-cell spread, by a mechanism as yet poorly understood. A very similar situation probably occurs in human tissues. At the time of primary infection, HSV replicates in mucosal tissues and then enters nerve endings for retrograde transport to dorsal root neurons. Upon reactivation from latency, the virus replicates in neuronal cells and then is transported in an anterograde direction to cells innervated by the neuron. The anterograde transport and subsequent lesions occur in the presence of neutralizing antibody. Cell-to-cell transmission represents, therefore, a major route for virus spread to tissues. A central question is whether entry of virions into cells and cell-to-cell spread of virus represent distinct pathways.Relevant to this report are the following.(i) The receptors for HSV entry broadly expressed in human cell lines belong to an immunoglobulin family. For nomenclature, see the appendix and Table 1. Nectin1␦, also named PRR1 (poliovirus receptor-related 1), or HveC (herpesvirus entry mediator C), mediates entry of all HSV-1 and -2 strains tested (15,29,50). Its splice variant isoform HIgR (herpesvirus immunoglobulin-like receptor) (hereafter nectin1␣) shares with nectin1␦ the ectodomain, made of one V and two C2 domains (7). Nectin1␣ and nectin1␦ interact with the virion glycoprotein D (gD) (7,15,24). The region with gDbinding activity and functional in HSV entry is located in the V domain (6,25). The C2 domain is involved in oligomerization (25). Nectin2␣ (also known as PRR2␣ or HveB) and nectin2␦ (PRR2␦) are homologs of nectin1 and are 32% identical to nectin1 in the ectodomain region. They serve as low-efficiency receptors for entry of HSV-1 mutants carrying substitutions in gD at residues 25 to 27, but not of wild-type virus (4,11,27,28,50,53). The cellular function of nectin1␦, nectin2␣, and nectin2␦ is that of intercellular adhesion molecules. They are anchored to the actin cytoskeleton and are recruited to cadherin-based adherens junctions through binding to L-afadin (27, 50).(ii) There is evidence that molecules that mediate HSV attachment to cells, and its entry, participate in cell-to-cell spread. Thus, heparan sulfate proteoglycan, a cell surface glycoprotein carrying glycosaminoglycans, enhances the initial attachment of HSV to cells (49) and enables the spread of syncytial strains (46) but is dispensable for spread of wild-type virus (17). Cells defective in entry receptors do not allow cellto-cell transmission of virus; this is enabled by transfection of HveA (her...

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“…gD, one of the HSV envelope glycoproteins, is essential for virus entry as well as for cell fusion and cell-to-cell spread [31][32][33]. The association of viral glycoproteins with actin filaments and the effect of TPA on the distribution of HSV glycoproteins were examined.…”

Section: Effect Of Tpa On the Localization Of Gd In Hsv-1-infected Ormentioning

confidence: 99%

Enhancement of Herpes Simplex Virus-Induced Polykaryocyte Formation by 12-O-Tetradecanoyl Phorbol 13-Acetate: Association with the Reorganization of Actin Filaments and Cell Motility

Yura

Kusaka²,

Bando³

et al. 2000

Intervirology

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A morphological change induced by syn– herpes simplex virus type 1 (HSV-1), polykaryocyte formation, was enhanced by treatment with 12-O-tetradecanoyl phorbol 13-acetate (TPA) in A431 cells. TPA treatment decreased the number of stress fibers, but led to the development of spike-like filopodia and actin-containing long projections. Similar reorganization of actin filaments was observed in HSV-1-induced polykaryocytes. The actin filament-disrupting drug cytochalasin D, but not the microtubule-disrupting drug nocodazole, inhibited the effect of TPA on polykaryocyte formation, indicating that the actin microfilament system plays a key role in this event. HSV-1 glycoprotein D (gD) was present in the cytoplasm of HSV-1-infected cells and gD gene-transfected cells; its expression became prominent at long cell projections in the presence of TPA. These findings suggest that the reorganization of actin filaments and cell motility are associated with the enhancing effect of TPA on HSV-1-induced polykaryocyte formation.

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Anti-idiotypic antibodies mimicking glycoprotein D of herpes simplex virus identify a cellular protein required for virus spread from cell to cell and virus-induced polykaryocytosis.

Cited by 28 publications

References 24 publications

Requirement of Interaction of Nectin-1α/HveC with Afadin for Efficient Cell-Cell Spread of Herpes Simplex Virus Type 1

Requirement of Interaction of Nectin-1α/HveC with Afadin for Efficient Cell-Cell Spread of Herpes Simplex Virus Type 1

Cell-to-Cell Spread of Wild-Type Herpes Simplex Virus Type 1, but Not of Syncytial Strains, Is Mediated by the Immunoglobulin-Like Receptors That Mediate Virion Entry, Nectin1 (PRR1/HveC/HIgR) and Nectin2 (PRR2/HveB)

Enhancement of Herpes Simplex Virus-Induced Polykaryocyte Formation by 12-O-Tetradecanoyl Phorbol 13-Acetate: Association with the Reorganization of Actin Filaments and Cell Motility

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