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Journal of Virology, April 2000, p. 3909-3917, Vol. 74, No. 8
Department of Experimental Pathology, Section
on Microbiology and Virology, University of Bologna, 40126 Bologna,
Italy,1 and Institute of Cancerology and
Immunology, INSERM U.119, 13009 Marseille,
France2
Received 2 December 1999/Accepted 20 January 2000
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 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
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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)
ABSTRACT
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and -
and Nectin2 were originally designated HIgR, PRR1/HveC, and PRR2/HveB, respectively. We report the following. (i) Wild-type HSV-1 spreads from cell to cell in J cells
expressing nectin1 or nectin1 but not in parental J cells that
are devoid of entry receptors. A monoclonal antibody to nectin1, which
blocks entry, also blocked cell-to-cell spread in nectin1-expressing J
cells. Moreover, wild-type virus did not spread from a
receptor-positive to a receptor-negative cell. (ii) The antibody to
nectin1 blocked transmission of wild-type virus in a number of human
cell lines, with varying efficiencies, suggesting that nectin1 is the
principal mediator of wild-type virus spread in a variety of human
cell lines. (iii) Nectin1 did not mediate cell fusion induced by the
syncytial strains HSV-1(MP) and HFEM-syn. (iv) Nectin2 could serve
as a receptor for spread of a mutant virus carrying the L25P
substitution in glycoprotein D, but not of wild-type virus,
in agreement with its ability to mediate entry of the mutant but not of
wild-type virus.
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, 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
gD-binding 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).
TABLE 1.
The immunoglobulin-like receptors of alphaherpesviruses:
past and present nomenclaturea
(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 cell-to-cell transmission of virus; this is enabled by transfection of HveA (herpesvirus entry mediator A) (34), a mediator of HSV entry that belongs to the tumor necrosis factor receptor family (43, 51).
(iii) HSV strains may be divided into two groups with respect to the
mechanism of cell-to-cell transmission. Wild-type strains (also
designated syn+) spread across the junctions
between the membranes of adjacent cells and cause infected cells to
aggregate into clumps. Syncytial mutant strains
(syn
) spread by fusion of the infected
cell with adjacent uninfected cells and form multinucleated
polykaryocytes or syncytia (see references 42 and
48). Both strains enter cells by the same mechanisms
(7, 15). A key question is whether cell-to-cell spread of
cytoaggregating strains and cell fusion by syncytial strains involves
identical or different cellular functions.
(iv) The four virion glycoproteins required for virion entry into the cells, gD, gB, gH, and gL, also participate in cell-to-cell transmission. 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. Soluble forms of gD or anti-idiotypic antibodies mimicking gD inhibit both virus entry and cell-to-cell transmission (21, 22, 36).
(v) The entry of free virion and cell-to-cell spread differ with respect to the role of the two virion glycoproteins, gE and gI, which form a heterocomplex. The complex localizes to the cell-cell junctions and favors virus spread across the junctions in cell cultures and in neurons in vivo (9, 10, 23). In its absence, the rate of HSV entry into cells is not altered (8). Also for the animal alphaherpesvirus pseudorabies virus (PrV), the gE-gI complex mediates cell-to-cell spread and transmission to specific neuronal circuits (5, 52, 54). Other HSV membrane proteins, gG, gM, and UL45, appear to play a role in cell-to-cell spread of syncytial strains but not in virion entry (2, 18, 31).
In these studies, we show that nectin1 mediates cell-to-cell spread of
wild-type HSV-1, but not of syncytial strains, both in cells expressing
the cDNA of the receptor as a transgene and in a variety of human cell
lines. Nectin2 serves for cell-to-cell spread of a mutant virus
carrying an L25P substitution in gD but not of wild-type virus.
Nectin1 and nectin1 mediate cell-to-cell spread of
HSV-1(F).
To investigate whether nectin1 and nectin1 play a
role in cell-to-cell transmission of HSV-1, we compared the abilities of HSV-1(F) (12) and its derivative R8102 (7) to
form plaques in cells defective in receptors for virus entry (J cells)
or in clonal derivatives of J cells, which constitutively express
nectin1 or nectin1 cDNA (designated as nectin1 or nectin1
cells) (7). Three series of experiments were performed. In
the first, since J cells cannot be infected with HSV-1 because of the
lack of receptors for entry, the DNA of HSV-1(F) was transfected into J
cells (1 µg of DNA/well of a six-well dish) and, for comparison, in
nectin1 cells. The cultures were monitored for plaque formation 2 to
3 days later by immunostaining with a polyclonal antibody to gM (1). The results in Fig. 1A
show that, in monolayers of J cells, infected cells consisted of single
cells or very small aggregates and plaques were not formed, whereas in
monolayers of nectin1 cells plaques were readily formed. In the
second experiment, nectin1 or nectin1 cells were infected with
R8102, which carries a lacZ gene under the 27 promoter.
Infection with this virus is readily monitored as 
-galactosidase
(-Gal) activity by X-Gal
(5-bromo-4-chloro-3-indolyl--D-galactoside) staining (34). In nectin1 or nectin1 cells,
plaques were readily formed (Fig. 1B) and were undistinguishable from
those formed in nectin1 cells transfected with the HSV-1(F)
DNA (compare panels b and e of Fig. 1). We note that throughout the
study we found a general agreement between results obtained with
wild-type virus and those obtained with the R8102 recombinant, whose
infection can be readily quantified as -Gal activity. In the third
series of experiments, an infectious center assay was performed, as
described in reference 43. Nectin1 cells,
infected with R8102, were trypsinized 4 h after infection and
seeded onto recipient monolayers of J, CHO (also defective in entry
receptors) (34), or nectin1 cells. The seeded cells and
the recipient monolayers were constantly maintained in the presence of
pooled human gamma globulins, to block the infectivity of virions
possibly released and to ensure that the detected plaques were formed
only by cell-to-cell spread. The seeded cells became attached to the
monolayer within 5 h or less in these as well as in all subsequent
infectious center assays, with an efficiency estimated at >95%. The
results in Fig. 1A show that plaques were not formed when infected
nectin1 cells were seeded onto recipient monolayers of J or CHO
cells but were formed when they were seeded onto recipient monolayers
of nectin1 cells (data not shown). Taken together, these experiments
indicate that plaque formation does not ensue in cells defective in
virus entry receptors (J or CHO), that nectin1 or nectin1 can
mediate cell-to-cell spread of HSV-1, and that virus was not
transmitted from a receptor-positive to a receptor-negative cell. No
major difference was observed between cells expressing the and
cells expressing the isoform of nectin1.
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and nectin1 cells was indeed
dependent upon expression of the receptors, as incubation of infected cells with monoclonal antibody (MAb) R1.302 to nectin1 (30), from 4 h after infection till fixation, reduced the plaque size to
small aggregates (Fig. 1B). An irrelevant MAb (MAb 6E2 to p48 of human
herpesvirus 6B), which does not cross-react to any cellular or HSV
protein (13), had almost no effect (data not shown). As
expected, the number of plaques in nectin1 and nectin1 cells exposed to MAb R1.302, scored by counting the single cells and the
small aggregates, did not differ from the number of plaques scored in
the cultures not treated or exposed to the irrelevant MAb (data not
shown). The effect of MAb R1.302 was quantified by exposing
R8102-infected nectin1 cells, grown in 96 wells, to increasing
amounts of purified immunoglobulins G (IgGs) from MAb R1.302, added at
4 h after infection. Plaque formation was monitored 48 h
later as -Gal expression, with ONPG
(o-nitrophenyl--D-galactopyranoside) as
substrate (34). Figure 2A
shows that MAb R1.302 inhibited plaque formation in a dose-dependent
fashion; 50% inhibition occurred at 0.08 mg/ml. At the same
concentration, the control pooled mouse immunoglobulins had no
significant effect. We note that the MAb concentrations required
to inhibit plaque formation were higher than those required to block
HSV infectivity in the same cells (7). In replicate
samples, MAb R1.302 (ascites fluid, 1:25) inhibited plaque
formation approximately to the same extent as did purified IgGs at 0.32 mg/ml. The remaining experiments were carried out under the former
conditions.
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), control mouse IgG (
), or R1.302 ascites fluid (
),
from 4 h after infection. Infection was detected 48 h later
by permeabilization with 0.5% NP-40 and quantitative detection of
The V domain of nectin1 is functional in cell-to-cell spread.
The region of nectin1 and nectin1 functional in binding to gD and
in virion entry is located in the V domain (6, 25). The
first evidence that the V domain of nectin1 also plays a key role in
the spread of the virus was provided by the inhibitory effect of MAb
R1.302, which recognizes an epitope located in the V domain
(6). Additional evidence was provided in two series of
experiments. First, cell-to-cell spread occurred in cells
which expressed a chimeric form of nectin1, originally named
V(HIgR)-PVR (6), consisting of the V domain of
nectin1 fused to the C domains and transmembrane and cytoplasmic
regions of the poliovirus receptor (PVR; also CD155 or HveD)
(15, 32) (Fig. 2C). Second, a soluble form of nectin1
carrying the entire ectodomain (VCC1-Fc), or the single V domain
(V1-Fc) fused to the Fc portion of IgG (6), could compete
with cell-bound receptor and thereby block cell-to-cell spread of
virus. In this experiment, infected nectin1 cells
were incubated with VCC1-Fc or V1-Fc from 4 h after infection.
This caused a dose-dependent inhibition and about 50% reduction at the highest concentration used (600 nM) (Fig. 2B). Higher
concentrations of VCC1-Fc or V1-Fc were not tested, because of
limitations in the quantities of recombinant proteins that could be
produced. As noted above for MAb R1.302, the concentrations of
VCC1-Fc and V1-Fc which inhibit cell-to-cell spread were higher than
those required to inhibit virus infectivity in the same cells
(6). This may reflect a limited accessibility of the
antibodies, or soluble receptor, to receptors located at adherens
junctions, as opposed to full accessibility to receptors located in
regions of the plasma membrane not engaged in cell-cell junctions.
Nectin1 or nectin1 mediates cell-to-cell spread of wild-type
virus in a variety of human cell lines.
A variety of human cell
lines express nectin1 and are susceptible to HSV infection (7,
15). The pathway of entry is via nectin1, and infection is
inhibited by MAb R1.302 (7). The antibody could be expected
to block virus transmission, provided that nectin1 is the principal
receptor serving also for virus spread. The effect of antibody R1.302
on formation of plaques and infectious centers was assessed in a number
of human cell lines of different origin, namely, HEp-2 (epithelial
carcinoma), 143tk (a derivative of human sarcoma), 5637 (epithelial bladder carcinoma), and Lan5 (neuroblastoma).
Representative results in Fig. 3A show that, in 143tk and HEp-2 cells, R8102 plaques were
decreased in size, although to a lower extent in HEp-2 cells than in
the nectin1 cells or in 143tk cells. The inhibitory
effect of MAb R1.302 was quantified in an infectious center assay.
Infected nectin1 cells were trypsinized at 4 h after infection
and seeded onto recipient monolayers of human cell lines in the
presence or absence of MAb R1.302. The number of stained cells in the
monolayer was determined by means of Photoshop software, as detailed in
the figure legend. This type of measure accounts for the overall number
of stained cells in a monolayer and was expressed as percentage
relative to the overall number of stained cells in the corresponding
monolayer not exposed to the antibody. As shown in Fig. 3B, the extent
of inhibition was 98% in recipient monolayers of nectin1 cells and ranged from 80 to 67% in the other recipient monolayers. While the
partial inhibition may reflect the concomitant activity of additional
receptors, the results clearly indicate that nectin1 is the principal
receptor available for virus transmission in a number of human cell
lines.
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Nectin1 and nectin1- do not mediate cell fusion induced by
syncytial strains.
Nectin1, 143tk, and HEp-2
cells were infected with the syncytial strain HSV-1(MP) (20)
or HFEM-syn (55), and incubated with MAb R1.302, from 4 h after infection. Representative results illustrated in Fig.
4 show that the two syncytial strains
behaved quite differently from the wild-type virus. The antibody did
not significantly affect the plaque size of either virus in any of the
cells tested. The number of plaques was also not affected (data
not shown). The results indicate that cell fusion by HSV-1(MP) and
HFEM-syn is mostly independent of nectin1.
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Nectin2 mediates cell-to-cell spread of an HSV-1 gD-mutant.
Nectin2 and nectin1 can serve as entry receptors for
gD-unrestricted mutants carrying substitutions in gD at residues 25 to
27, but not for wild-type virus (28, 53) (Table 1). To test
the ability of nectin2 to serve in cell-to-cell spread, nectin2
cells (28) were infected with HSV-1(U10), which carries the
L25P substitution in gD and can enter nectin2 cells (4, 28).
The infected cultures were incubated in the absence or presence of MAb
R2.525, a MAb to nectin2 which blocks HSV-1(U10) entry (28,
30). The results in Fig. 5 show
that HSV-1(U10) could form plaques in nectin2 cells. They were
reduced in size by MAb R2.525. These results were confirmed and
extended in an infectious center assay, where HSV-1(U10)-infected
nectin1 cells were trypsinized and seeded onto a monolayer of
nectin2 cells in the absence or presence of MAb R2.525. Plaques were
formed and were reduced in size by the antibody (data not shown). To ascertain whether nectin2 can serve as a receptor for the spread of
wild-type virus, nectin2 cells were transfected with the DNA of
HSV-1(F), to overcome the need for a receptor. This resulted in singly
infected cells or small aggregates but not in plaques (Fig. 5C). Taken
together, the results indicate that nectin2 can serve as a receptor
for cell-to-cell spread of HSV-1(U10) but not of wild-type HSV-1.
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and
nectin1 as cellular functions involved in cell-to-cell transmission of wild-type HSV-1, both in cells expressing nectin1 cDNA as a transgene and in a variety of human cell lines. Cell-to-cell spread, like entry, involved the V domain of nectin1. In addition, transmission could not take place from receptor-positive to receptor-negative cells.
Nectin1 is expressed in human tissues, including central nervous system
and tissues of epithelial origin (7). Taken together, these
properties make this molecule a likely candidate that mediates virus
spread to tissues that are the target of HSV infection in humans. With
respect to the function of nectin1, HSV differs from PrV. In the case
of PrV, which needs gD for virus entry, but not for cell-to-cell
transmission (40, 41, 45), the human HveC/nectin,
HveB/nectin2, and HveD enabled entry of virions into the resistant
CHO cells, but typical plaques were not formed (37). The
small clusters of infected cells formed in cultures expressing these
receptors were similar to those formed in CHO cells lacking receptors
(37).
(ii) They identify nectin2 as a mediator of cell-to-cell
transmission for an HSV gD mutant carrying a substitution at residue 25, but not for wild-type virus. Nectin2 shows, therefore, the same
restricted range as a mediator of virus transmission and as a mediator
of virion entry (28, 53). Both activities are consistent
with its ability to interact physically with mutant gD and failure to
interact with wild-type gD (28).
(iii) They show that cell fusion induced by syncytial strains occurs
independently of nectin1. This was a surprising result, in view of the
ability of the syncytial viruses to enter cells via nectin1 (7,
15). Syncytial and cell-aggregating strains were reported to be
able to use HveA for cell-to-cell transmission in cells transfected
with the cDNA of the mediator (43, 51). However, given that
its expression is limited to highly specific cell lineages, this
molecule cannot represent the principal mediator for transmission of
syncytial strains in the majority of human cell lines. Recently,
3-O-sulfated heparan sulfate has been shown to provide a binding site
for gD and initiate HSV entry (47). Whether human cell lines
can actually be infected with HSV through this moiety has not been
determined. It remains also to be determined whether it can mediate
cell fusion of syncytial strains. In the past, it has been speculated
that cell fusion induced by syncytial strains of HSV mimics and
represents a good model for the fusion event between virion and plasma
membrane in the entry process. The results presented here underscore a
notable difference between the two activities and identify the usage of
cellular receptors as yet another difference between the two processes.
Current findings raise the possibility that cell fusion induced by the
syncytial strains involves different cellular components than does the
spread of wild-type cell-aggregating HSV.
(iv) Nectin1, nectin2, and nectin2 are intercellular adhesion
molecules that act by homophilic interaction and are recruited to
adherens junctions (27, 50). Nectin1 differs from
nectin1, nectin2, and nectin2 in that it does not carry the
conserved C-terminal motif (A/ExYV) that binds the latter molecules to
the PDZ domain of L-afadin, an F-actin binding protein. It
is nonetheless expressed at the cell surface and also at cell-cell
contact sites, although at reduced efficiency (our unpublished
observations). Consistently, engineered forms of nectin1 and
nectin2 that lack the C-terminal motif maintain the ability to
localize at cell-cell contact sites (33, 50). Current
data indicate that nectin1 serves in cell-to-cell spread of HSV, as
does its isoform nectin1. Therefore, binding to L-afadin
does not seem to be a prerequisite to promote cell-to-cell spread
of HSV. Of note, the two viral glycoproteins that play a
role in cell-to-cell transmission of virus, but not in entry of free
virions, gE and gI, also localize at cell-cell junctions
(10). Previously, one of our laboratories showed that
homophilic interaction of nectin2, or nectin2, correlates with
the cis dimerization of the molecules at the cell surface and that this function requires a domain different from that functional in HSV entry (27, 28). It can be proposed that the
nectin1 and nectin1 and nectin2 and nectin1 molecules
promote cell-to-cell spread by establishing the necessary intercellular
contacts between juxtaposed cells, both by engaging in homophilic
interaction and by interaction with viral gD, the viral ligand of
nectin1 and nectin2. In turn, the viral gD that engages with nectin1,
or nectin2, may be expressed at the surface of the infected cell and/or
in progeny virions. The intercellular contacts created by nectin1, or
nectin2, might contribute to encasing the progeny virus within the
intercellular junctions and to shielding it, in part, from molecules present in medium. These may be the human gamma
globulins normally used to allow plaque formation or the molecules used in this study, i.e., antibodies to nectin1 or nectin2 or soluble forms
of nectin1. This hypothesis would explain why high concentrations of
the antibodies or soluble receptor were necessary to exert an
inhibitory effect.
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APPENDIX |
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HveC/PRR1, HIgR, HveB/PRR2, and PRR2 are members of an
immunoglobulin family whose function has been recently identified as
that of intercellular adhesion molecules (27, 50). The molecules were renamed nectin1 and nectin2, replacing PRR1 and PRR2,
respectively (50). Knowledge of the natural function of these proteins may help in understanding the mechanism by which they
fulfill their function as viral receptors. Furthermore, receptor designations in virology should be comprehensible to broad audiences in
cell biology and not merely to the workers in the field. To this aim,
we propose to maintain, for the alphaherpesvirus immunoglobulin-like receptors, the designation that describes their biological function. Examples of this rule are numerous, e.g., intercellular adhesion molecule, vascular cell adhesion molecule 1, CD4, chemokine receptors CCR5 and CXCR4, integrins, amino acid transporter, carboxypeptidase D,
fibronectin, etc. Table 1 lists the names given to members of the
immunoglobulin subfamily and the viruses for which they serve as
receptors. The and suffixes are those used in the literature to
designate the different isoforms of poliovirus receptor. Where
appropriate, the prefixes h, m, etc., can be used to designate the
species of origin (human, murine, etc., respectively).
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ACKNOWLEDGMENTS |
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We thank Elisabetta Romagnoli for invaluable assistance with cell cultures. We thank N. S. Markovitz and B. Roizman (Chicago, Ill.) for the gift of R8102.
The work done at the University of Bologna was supported by grants from Target Project in Biotechnology/CNR, Telethon grant A141, MURST 40%, University of Bologna 60%, and pluriannual plan. The studies at INSERM U119, Marseille, were aided by INSERM, the Association pour la Récherche Contre le Cancer (ARC), and the Ligue Nationale Française Contre le Cancer (LNFCC).
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FOOTNOTES |
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* Corresponding author. Mailing address: Dipartimento di Patologia Sperimentale, Sezione di Microbiologia e Virologia, Via San Giacomo, 12, 40126 Bologna, Italy. Phone: 39 51 2094733/34. Fax: 39 51 2094747. E-mail: campadel{at}alma.unibo.it.
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REFERENCES |
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Text
Appendix
References
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|---|
| 1. |
Baines, J. D., and B. Roizman.
1993.
The UL10 gene of herpes simplex virus 1 encodes a novel viral glycoprotein, gM, which is present in the virion and in the plasma membrane of infected cells.
J. Virol.
67:1441-1452 |
| 2. |
Balan, P.,
N. Davis-Poynter,
H. Atkinson,
H. Browne, and T. Minson.
1994.
An analysis of the in vitro and in vivo phenotypes of mutants of herpes simplex virus type 1 lacking glycoprotein gG, gE, gI or the putative gJ.
J. Gen. Virol.
75:1245-1258 |
| 3. |
Cai, W. Z.,
S. Person,
S. C. Warner,
J. H. Zhou, and N. A. De Luca.
1987.
Linker-insertion nonsense and restriction-site deletion mutations of the gB glycoprotein gene of herpes simplex virus type 1.
J. Virol.
61:714-721 |
| 4. |
Campadelli-Fiume, G.,
S. Qi,
E. Avitabile,
L. Foà-Tomasi,
R. Brandimarti, and B. Roizman.
1990.
Glycoprotein D of herpes simplex virus encodes a domain which precludes penetration of cells expressing the glycoprotein by superinfecting herpes simplex virus.
J. Virol.
64:6070-6079 |
| 5. | Card, J. P., and L. W. Enquist. 1995. Neurovirulence of pseudorabies virus. Crit. Rev. Neurobiol. 9:137-162[Medline]. |
| 6. |
Cocchi, F.,
M. Lopez,
L. Menotti,
M. Aoubala,
P. Dubreuil, and G. Campadelli-Fiume.
1998.
The V domain of herpesvirus Ig-like receptor (HIgR) contains a major functional region in herpes simplex virus-1 entry into cells and interacts physically with the viral glycoprotein D.
Proc. Natl. Acad. Sci. USA
95:15700-15705 |
| 7. |
Cocchi, F.,
L. Menotti,
P. Mirandola,
M. Lopez, and G. Campadelli-Fiume.
1998.
The ectodomain of a novel member of the immunoglobulin superfamily related to the poliovirus receptor has the attributes of a bona fide receptor for herpes simplex viruses 1 and 2 in human cells.
J. Virol.
72:9992-10002 |
| 8. |
Dingwell, K. S.,
C. R. Brunetti,
R. L. Hendricks,
Q. Tang,
M. Tang,
A. J. Rainbow, and D. C. Johnson.
1994.
Herpes simplex virus glycoproteins E and I facilitate spread in vivo and across junctions of cultured cells.
J. Virol.
68:834-845 |
| 9. | Dingwell, K. S., L. C. Doering, and D. C. Johnson. 1995. Glycoproteins E and I facilitate neuron-to-neuron spread of herpes simplex virus. J. Virol. 69:7087-7098[Abstract]. |
| 10. |
Dingwell, K. S., and D. C. Johnson.
1998.
The herpes simplex virus gE-gI complex facilitates cell-to-cell spread and binds to components of cell junctions.
J. Virol.
72:8933-8942 |
| 11. | Eberlé, F., P. Dubreuil, M. G. Mattei, E. Devilard, and M. Lopez. 1995. The human PRR2 gene, related to the human poliovirus receptor gene (PVR), is the true homolog of the murine MPH gene. Gene 159:267-272[CrossRef][Medline]. |
| 12. |
Ejercito, P. M.,
E. D. Kieff, and B. Roizman.
1968.
Characterization of herpes simplex virus strains differing in their effects on social behaviour of infected cells.
J. Gen. Virol.
2:357-364 |
| 13. | Foà-Tomasi, L., E. Avitabile, and G. Campadelli-Fiume. 1995. Selection of a monoclonal antibody specific for variant B human herpesvirus 6-infected mononuclear cells. J. Virol. Methods 51:289-296[CrossRef][Medline]. |
| 14. |
Forrester, A.,
H. Farrell,
G. Wilkinson,
J. Kaye,
N. Davis-Poynter, and T. Minson.
1992.
Construction and properties of a mutant of herpes simplex virus type 1 with glycoprotein H coding sequences deleted.
J. Virol.
66:341-348 |
| 15. |
Geraghty, R. J.,
C. Krummenacher,
G. H. Cohen,
R. J. Eisenberg, and P. G. Spear.
1998.
Entry of alphaherpesviruses mediated by poliovirus receptor-related protein 1 and poliovirus receptor.
Science
280:1618-1620 |
| 16. | Gompels, U., and A. Minson. 1986. The properties and sequence of glycoprotein H of herpes simplex virus type 1. Virology 153:230-247[CrossRef][Medline]. |
| 17. |
Gruenheid, S.,
L. Gatzke,
H. Meadows, and F. Tufaro.
1993.
Herpes simplex virus infection and propagation in a mouse L cell mutant lacking heparan sulfate proteoglycans.
J. Virol.
67:93-100 |
| 18. |
Haanes, E. J.,
C. M. Nelson,
C. L. Soule, and J. L. Goodman.
1994.
The UL45 gene product is required for herpes simplex virus type 1 glycoprotein-B-induced cell fusion.
J. Virol.
68:5825-5834 |
| 19. |
Highlander, S. L.,
S. L. Sutherland,
P. J. Gage,
D. C. Johnson,
M. Levine, and J. C. Glorioso.
1987.
Neutralizing monoclonal antibodies specific for herpes simplex virus glycoprotein D inhibit virus penetration.
J. Virol.
61:3356-3364 |
| 20. | Hoggan, M. D., and B. Roizman. 1959. The isolation and properties of a variant of herpes simplex producing multinucleated giant cells in monolayer cultures in the presence of antibody. Am. J. Hyg. 70:208-219. |
| 21. |
Huang, T., and G. Campadelli-Fiume.
1996.
Anti-idiotypic antibodies mimicking glycoprotein D of herpes simplex virus identify a cellular protein required for virus spread from cell to cell and viral induced polykaryocytosis.
Proc. Natl. Acad. Sci. USA
93:1836-1840 |
| 22. |
Johnson, D. C.,
R. L. Burke, and T. Gregory.
1990.
Soluble forms of herpes simplex virus glycoprotein D bind to a limited number of cell surface receptors and inhibit virus entry into cells.
J. Virol.
64:2569-2576 |
| 23. |
Johnson, D. C.,
M. C. Frame,
M. W. Ligas,
A. M. Cross, and N. D. Stow.
1988.
Herpes simplex virus immunoglobulin G Fc receptor activity depends on a complex of two viral glycoproteins, gE and gI.
J. Virol.
62:1347-1354 |
| 24. |
Krummenacher, C.,
A. V. Nicola,
J. C. Whitbeck,
H. Lou,
W. Hou,
J. D. Lambris,
R. J. Geraghty,
P. G. Spear,
G. H. Cohen, and R. J. Eisenberg.
1998.
Herpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry.
J. Virol.
72:7064-7074 |
| 25. |
Krummenacher, C.,
A. H. Rux,
J. C. Whitbeck,
M. Ponce-de-Leon,
H. Lou,
I. Baribaud,
W. Hou,
C. Zou,
R. J. Geraghty,
P. G. Spear,
R. J. Eisenberg, and G. H. Cohen.
1999.
The first immunoglobulin-like domain of HveC is sufficient to bind herpes simplex virus gD with full affinity, while the third domain is involved in oligomerization of HveC.
J. Virol.
73:8127-8137 |
| 26. |
Ligas, M. W., and D. C. Johnson.
1988.
A herpes simplex virus mutant in which glycoprotein D sequences are replaced by -galactosidase sequences binds to but is unable to penetrate into cells.
J. Virol.
62:1486-1494 |
| 27. |
Lopez, M.,
M. Aoubala,
F. Jordier,
D. Isnardon,
S. Gomez, and P. Dubreuil.
1998.
The human poliovirus receptor related 2 protein is a new hematopoietic/endothelial homophilic adhesion molecule.
Blood
92:4602-4611 |
| 28. |
Lopez, M.,
F. Cocchi,
L. Menotti,
E. Avitabile,
P. Dubreuil, and G. Campadelli-Fiume.
2000.
Nectin2 (PRR2 or HveB) and nectin2 are low-efficiency mediators for entry of herpes simplex virus mutants carrying the Leu25Pro substitution in glycoprotein D.
J. Virol.
74:1267-1274 |
| 29. | Lopez, M., F. Eberlé, M. G. Mattei, J. Gabert, F. Birg, F. Bardin, C. Maroc, and P. Dubreuil. 1995. Complementary DNA characterization and chromosomal localization of a human gene related to the poliovirus receptor-encoding gene. Gene 155:261-265[CrossRef][Medline]. |
| 30. | Lopez, M., F. Jordier, F. Bardin, L. Coulombel, C. Chabannon, and P. Dubreuil. 1997. Identification of a new class of IgG superfamily antigens expressed in hemopoiesis, p. 1081-1083. In T. Kishimoto, H. Kikutani, A. von der Borne, D. Y. Mason, M. Miyasaka, A. Moretta, K. Okumura, S. Shaw, T. A. Springer, K. Sugumura, and H. Zola (ed.), Leukocyte typing VI: white cell differentiation antigens. Garland Publishing, Inc., New York, N.Y. |
| 31. |
MacLean, C. A.,
L. M. Robertson, and F. E. Jamieson.
1993.
Characterization of the UL10 gene product of herpes simples virus type 1 and investigation of its role in vivo.
J. Gen. Virol.
74:975-983 |
| 32. | Mendelsohn, C. L., E. Wimmer, and V. R. Racaniello. 1989. Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily. Cell 56:855-865[CrossRef][Medline]. |
| 33. |
Miyahara, M.,
H. Nakanishi,
K. Takahashi,
K. Satoh-Horikawa,
K. Tachibana, and Y. Takai.
2000.
Interaction of nectin with afadin is necessary for its clustering at cell-cell contact sites but not for its cis dimerization or trans interaction.
J. Biol. Chem.
275:613-618 |
| 34. | Montgomery, R. I., M. S. Warner, B. J. Lum, and P. G. Spear. 1996. Herpes simplex virus-1 entry into cells mediated by a novel member of the TNF/NGF receptor family. Cell 87:427-436[CrossRef][Medline]. |
| 35. | Navarro, D., P. Paz, and L. Pereira. 1992. Domains of herpes simplex virus glycoprotein B that function in virus penetration, cell-to-cell spread, and cell fusion. Virology 186:99-112[CrossRef][Medline]. |
| 36. | Nicola, A. V., S. H. Willis, N. N. Naidoo, R. J. Eisenberg, and G. H. Cohen. 1996. Structure-function analysis of soluble forms of herpes simplex virus glycoprotein D. J. Virol. 70:3815-3822[Abstract]. |
| 37. |
Nixdorf, R.,
J. Schmidt,
A. Karger, and T. Mettenleiter.
1999.
Infection of Chinese hamster ovary cells by pseudorabies virus.
J. Virol.
73:8019-8026 |
| 38. | Noble, A. G., G. T. Lee, R. Sprague, M. L. Parish, and P. G. Spear. 1983. Anti-gD monoclonal antibodies inhibit cell fusion induced by herpes simplex virus type 1. Virology 129:218-224[CrossRef][Medline]. |
| 39. | Novotny, M. J., M. L. Parish, and P. G. Spear. 1996. Variability of herpes simplex virus 1 gL and anti-gL antibodies that inhibit cell fusion but not viral infectivity. Virology 221:1-13[CrossRef][Medline]. |
| 40. |
Peeters, B.,
N. De Wind,
M. Hooisma,
F. Wagenaar,
A. Gielkens, and R. Moormann.
1992.
Pseudorabies virus envelope glycoproteins gp50 and gII are essential for virus penetration, but only gII is involved in membrane fusion.
J. Virol.
66:894-905 |
| 41. |
Rauh, I., and T. C. Mettenleiter.
1991.
Pseudorabies virus glycoproteins gII and gp50 are essential for virus penetration.
J. Virol.
65:5348-5356 |
| 42. | Roizman, B., and A. E. Sears. 1996. Herpes simplex viruses and their replication, p. 2231-2295. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology, 3rd ed., vol. 2. Lippincott-Raven Publishers, Philadelphia, Pa. |
| 43. |
Roller, J. R., and D. Rauch.
1998.
Herpesvirus entry mediator HVEM mediates cell-cell spread in BHK(TK) cell clones.
J. Virol.
72:1411-1417 |
| 44. |
Roop, C.,
L. Hutchinson, and D. C. Johnson.
1993.
A mutant herpes simplex virus type 1 unable to express glycoprotein L cannot enter cells, and its particles lack glycoprotein H.
J. Virol.
67:2285-2297 |
| 45. | Schmidt, J., B. G. Klupp, A. Karger, and T. C. Mettenleiter. 1997. Adaptability in herpesviruses: glycoprotein D-independent infectivity of pseudorabies virus. J. Virol. 71:17-24[Abstract]. |
| 46. |
Shieh, M. T., and P. G. Spear.
1994.
Herpesvirus-induced cell fusion that is dependent on cell surface heparan sulfate or soluble heparin.
J. Virol.
68:1224-1228 |
| 47. | Shukla, D., J. Liu, P. Blaiklock, N. W. Shworak, X. Bai, J. D. Esko, G. H. Cohen, R. J. Eisenberg, R. D. Rosenberg, and P. G. Spear. 1999. A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry. Cell 99:13-22[CrossRef][Medline]. |
| 48. | Spear, P. G. 1993. Membrane fusion induced by herpes simplex virus, p. 201-232. In J. Bentz (ed.), Viral fusion mechanisms. CRC Press, Inc., Boca Raton, Fla. |
| 49. | Spear, P. G., M. T. Shieh, B. C. Herold, D. WuDunn, and T. I. Koshy. 1992. Heparan sulfate glycosaminoglycans as primary cell surface receptors for herpes simplex virus. Adv. Exp. Med. Biol. 313:341-353[Medline]. |
| 50. |
Takahashi, K.,
H. Nakanishi,
M. Miyahara,
K. Mandai,
K. Satoh,
A. Satoh,
H. Nishioka,
J. Aoki,
A. Nomoto,
A. Mizoguchi, and Y. Takai.
1999.
Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with afadin, a PDZ domain-containing protein.
J. Cell Biol.
145:539-549 |
| 51. |
Terry-Allison, T.,
R. I. Montgomery,
J. C. Whitbeck,
R. Xu,
G. H. Cohen,
R. J. Eisenberg, and P. G. Spear.
1998.
HveA (herpesvirus entry mediator A), a coreceptor for herpes simplex virus entry, also participates in virus-induced cell fusion.
J. Virol.
72:5802-5810 |
| 52. | Tirabassi, R. S., R. A. Townley, M. G. Eldridge, and L. W. Enquist. 1997. Characterization of pseudorabies virus mutants expressing carboxy-terminal truncations of gE: evidence for envelope incorporation, virulence, and neurotropism domains. J. Virol. 71:6455-6464[Abstract]. |
| 53. | Warner, M. S., R. J. Geraghty, W. M. Martinez, R. I. Montgomery, J. C. Whitbeck, R. Xu, R. J. Eisenberg, G. H. Cohen, and P. G. Spear. 1998. A cell surface protein with herpesvirus entry activity (HveB) confers susceptibility to infection by mutants of herpes simplex virus type 1, herpes simplex virus type 2, and pseudorabies virus. Virology 246:179-189[CrossRef][Medline]. |
| 54. |
Whealy, M. E.,
J. P. Card,
A. K. Robbins,
J. R. Dubin,
H. J. Rziha, and L. W. Enquist.
1993.
Specific pseudorabies virus infection of the rat visual system requires both gI and gp63 glycoproteins.
J. Virol.
67:3786-3797 |
| 55. | Wildy, P., W. C. Russel, and R. W. Horne. 1960. The morphology of herpes virus. Virology 12:204-222[CrossRef][Medline]. |
Journal of Virology, April 2000, p. 3909-3917, Vol. 74, No. 8
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