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Journal of Virology, May 2001, p. 4499-4505, Vol. 75, No. 10
Institut für Virologie und
Immunbiologie, D-97078 Würzburg, Germany
Received 17 November 2000/Accepted 5 February 2001
Measles virus (MV) interacts with cellular receptors on the surface
of peripheral blood lymphocytes (PBL) which mediate virus binding and
uptake. Simultaneously, the direct contact of the viral glycoproteins
with the cell surface induces a negative signal blocking progression to
the S phase of the cell cycle, resulting in a pronounced proliferation
inhibition. We selected a monoclonal antibody (MAb 5C6) directed to the
surface of highly MV-susceptible B cells (B95a), which inhibits binding
to and infection of cells with MV wild-type and vaccine strains. By
screening a retroviral cDNA library from human splenocytes (ViraPort;
Stratagene) with this antibody, we cloned and identified the recognized
molecule as signaling lymphocytic activation molecule (SLAM; CD150),
which is identical to the MV receptor recently found by H. Tatsuo et al. (Nature 406:893-897, 2000). After infection of cells, and after
surface contact with MV envelope proteins, SLAM is downregulated from
the cell surface of activated PBL and cell lines. Although anti-SLAM
and/or anti-CD46 antibodies block virus binding, they do not interfere
with the contact-mediated proliferation inhibition. In addition, the
cell-type-specific expression of SLAM does not correlate with the
sensitivity of cells for proliferation inhibition. The data indicate
that proliferation inhibition induced by MV contact is independent of
the presence or absence of the virus-binding receptors SLAM and CD46.
Measles virus (MV) is among the most
widespread human pathogens, causing approximately 1 million deaths
worldwide each year mainly due to its immunosuppressive potential (for
reviews, see references 4, 11, and 37). During and weeks
after acute measles, delayed-type hypersensitivity skin test responses
to recall antigens are suppressed, and there is an increased
susceptibility to opportunistic infections, which aggravates the course
of the disease. One aspect of the viral immunosuppression is the
proliferation inhibition in response to mitogens, T-cell receptor
cross-linking, or recall antigens of peripheral blood mononuclear cells
(PBMC) isolated from patients (ex vivo) and in vitro. Recently, we
found that direct contact of the MV glycoproteins hemagglutinin (H) and
fusion protein (F) with the cell surface of lymphocytes or lymphoid
cell lines induces a dominant negative signal in the contacted cells,
leading to this proliferative inhibition (33, 44). It is
likely that this negative signal is transduced by a receptor present on
the surface of lymphoid cells.
Using MV vaccine strains such as Edmonston (Edm), CD46 was identified
as a cellular receptor for MV (8, 30). However, MV
wild-type isolates do not or only with low affinity interact with CD46
(3, 16, 23). It has been demonstrated that MV can
efficiently be isolated from patients using B-cell lines, such as B95a
(19), which lack a complete CD46 (15, 28), indicating the presence of another receptor. To identify this receptor,
we selected a monoclonal antibody (MAb) directed to the surface of B95a
cells which inhibits MV binding and infection and identified the
recognized molecule as SLAM (CD150). Thus, it is identical to the MV
receptor recently found by Tatsuo et al. by different means
(40).
SLAM is a glycoprotein belonging to the CD2 subset of the
immunoglobulin (Ig) superfamily and is expressed on the surface of a
proportion of primary B cells and Epstein-Barr virus (EBV)-transformed B cells, activated T cells, memory T cells, T-cell clones, and immature
thymocytes (39). It is rapidly induced on naive
lymphocytes after activation, and cross-linking antibodies to SLAM
stimulate B-and T-cell proliferation (2, 7, 32). Since
SLAM is a signal-transducing molecule, the antiproliferative effect
exerted by MV contact to the cell surface of lymphocytes could possibly be mediated by SLAM. We therefore assessed the involvement of SLAM in
this process. We investigated the virus-mediated SLAM modulation and
the effect of SLAM engagement on the viral contact-mediated proliferation inhibition of lymphocytes.
Antibodies, cells, and viruses.
To raise MAbs to enriched
surface proteins of B95a cells, we biotinylated 107 cells
with sulfo-D-biotin-N-hydroxysuccinimide ester
(sulfo-NHS-LC-biotin; Pierce) and prepared a lysate with
radioimmunoprecipitation assay buffer (150 mM NaCl, 10 mM Tris, 0.1%
sodium dodecyl sulfate [SDS], 1% sodium desoxy cholate, 1% Triton
X-100). The biotinylated proteins were precipitated using 50 µl of
streptavidin-agarose (Pierce) and washed four times with
phosphate-buffered saline (PBS). BALB/c mice were immunized
intraperitoneally three times with the beads in 500 µl of PBS before
spleen cells were fused with SP2/0 myeloma cells.
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.10.4499-4505.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
CD150 (SLAM) Is a Receptor for Measles Virus but Is Not Involved
in Viral Contact-Mediated Proliferation Inhibition
ABSTRACT
Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
INTRODUCTION
Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
MATERIALS AND METHODS
Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
80°C. All viruses were titrated using
B95a cells.
Expression cloning using a retroviral cDNA library. The cDNA gene bank containing cDNA of a pool of five normal human spleen tissue specimens cloned unidirectional into the ViraPort pFB-XR vector (Stratagene), a replication-defective Moloney MLV-based vector, was purchased from Stratagene. The retrovirus was produced by transiently transfecting tissue culture cells with the pFB-XR plasmid cDNA library together with two additional vectors from which the Gag-Pol and vesicular stomatitis virus G (VSV-G) proteins are expressed (pVPack-GP and pVPack-VSV-G). Virus produced using the plasmid libraries is pseudotyped with the VSV-G envelope protein and is thus capable of infecting most dividing cell types, including CHO cells. After infection of cells with the retroviral supernatants, the cDNAs inserted between two long terminal repeats integrate in the host genome. CHO cells (106) were transduced with an MOI of approximately 1; 48 h postinfection, cells expressing the 5C6 epitope were selected by fluorescence-activated cell sorting (FACS) using a FACS Vantage (Becton Dickinson). Sorted cells were expanded and resorted four times. The cDNA insert was then recovered from genomic DNA of sorted cells by PCR using the vector-specific primers (5' retro primer 5'-GGCTGCCGACCCCGGGGGTGG-3' and 3' pFB primer 5'-CGAACCCCAGAGTCCCGCTCA-3'; provided by Stratagene). Amplified cDNA was sequenced using an Abi Prism 310 genetic analyzer (Perkin-Elmer).
Virus-cell binding assay. Cells (5 × 104) in 100 µl of PBS were incubated at 37°C for 1 h with viruses at a given MOI (titrated using B95a cells), washed with FACS buffer (PBS containing 0.4% bovine serum albumin and 0.02% sodium azide), and stained with MAb L77 against MV-H and FITC-conjugated goat anti-mouse antibodies. Bound virus was determined by analysis with a FACscan (Becton Dickinson). In case of the virus binding inhibition assay, cells were preincubated with increasing concentrations of MAbs to SLAM and/or CD46. Bound virus was then detected with biotinylated MAb K4 to MV-H and streptavidin-FITC. The concentrations of SLAM and CD46 antibodies alone were as indicated in the figure legends. In case of both antibodies together, SLAM and CD46 antibodies were used added in half amounts to sum up to the indicated concentrations.
SLAM downregulation assays. To measure the infection-induced receptor modulation, cells were infected with an MOI of 1 for 2 to 3 days. Cells were fixed with 3.7% paraformaldehyde and stained with antibodies to SLAM (MAb 5C6) or to MV-H (MAb L77) as control of infection. For contact-mediated downregulation, persistently MV-infected BJAB cells (BJAB-pEdm or BJAB-pWTF) were mixed 1:1 with uninfected cells for 1 to 4 h at 37°C. Cells were chilled on ice and fixed with 3.7% paraformaldehyde. As control, cells were chilled on ice, fixed, and then mixed. The surface expression of SLAM was detected with MAb 5C6 and FITC-conjugated second antibody by flow cytometry using a FACscan (Becton Dickinson).
Proliferation assay. The assay was done as described elsewhere (33). Briefly, responder cells (105/well/100 µl; PBL, B95a, BJAB, or Jurkat) were incubated with antibodies to SLAM and/or CD46 (2, 10, or 50 µg/ml) for 45 min at room temperature before mixing with UV-inactivated viruses. PBL were activated with 2.5 µg of phytohemagglutinin (PHA; Sigma) per ml at the start of the test or 24 h before, with no difference in results. Inhibition of proliferation was induced by adding MV strain Edm or WTFb in various amounts, which were inactivated by UV irradiation (1.5 J/cm2) to prevent infection of cells. After incubation of the cells at 37°C for 48 h, the cells were incubated for 16 h with [3H]thymidine (0.5 µCi/ml). The cells were harvested, and [3H]thymidine incorporation in DNA was measured using a scintillation counter (1205 Betaplate; LKB). All assays were performed as triplicates.
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RESULTS |
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Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
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Selection of a receptor blocking antibody.
We raised MAbs to
enriched surface proteins of B95a cells and selected a MAb (5C6) which
inhibits syncytium formation and infection of these cells with MV. The
binding of both wild-type MV (WTFb and Wü5679), and vaccine
strains (Edm and EdmZag) to the surface of B95a cells was nearly
completely inhibited by MAb 5C6 (Fig. 1a to
h). An antibody directed to the truncated
form of CD46 present on B95a cells (MAb 10/88) had no effect on virus binding, and both antibodies together inhibited virus binding like MAb
5C6 alone. In case of human PBMC, which express CD46 and the molecule
recognized by MAb 5C6, MAb 5C6 blocked the binding of wild-type MV
(WTFb and Wü5679) (Fig. 1i, j, m, and n) but not the binding of
strains interacting with high affinity with CD46 (Edm and EdmZag) (Fig.
1k, l, o, and p). In contrast, binding of the vaccine strains to PBMC
was inhibited by MAb 13/42 directed to the first domain of CD46. Both
antibodies together had no detectable additive effects. These results
suggest that MAb 5C6 recognizes the only receptor present on B95a cells
for MV and a receptor for wild-type MV on human PBMC.
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Analysis of cell surface proteins binding to wild-type MV.
Surface proteins of B95a cells binding to MV strain WTFb were assessed
by a coprecipitation assay, a method independent of antibody 5C6. The
cell surface of B95a cells was biotinylated, the cells were incubated
with MV strain WTFb at 4 or 37°C overnight, and virus-receptor
complexes were precipitated using a MAb to MV-H (K4). The
immunoprecipitated proteins were separated by SDS-polyacrylamide gel
electrophoresis (PAGE) and blotted, and bands were visualized with
streptavidin-peroxidase (Fig. 2). Bound
proteins were detected using increasing doses of virus (Fig. 2, lanes 1 to 3 and 5 to 7). Virus binding at 37°C (Fig. 2, lanes 5 to 7) was
more efficient than that at 4°C (Fig. 2, lanes 1 to 3). For
comparison, an immunoprecipitation using MAb 5C6 is shown (Fig. 2, lane
10). The diffuse band of biotinylated surface protein bound to MV
appeared to have the same molecular weight as the band precipitated
with MAb 5C6.
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Expression cloning and identification of the protein recognized by
MAb 5C6.
Using MAb 5C6, we screened a retroviral cDNA library from
human splenocytes transduced in CHO cells by selecting positive cells
by FACS. Selected cells were expanded and reselected four times. After
recloning of the sorted 5C6-positive cells, we obtained a stably
transduced cell line, since the retrovirus integrates in the cellular
genome. Using retrovirus-specific primers complementary to the
boundaries between which the cDNA inserts were cloned, we could amplify
a 1.7-kb band present in the DNA of the FACS-sorted transduced CHO
cells. This amplified 1.7-kb DNA fragment was sequenced and identified
as encoding the signaling lymphocytic activation molecule (SLAM,
CD150), which was recently identified also by Tatsuo et al. as an MV
receptor (40). The sequence was identical to the published
sequence for the transmembrane form of human SLAM (7). We
analyzed by Western blotting the proteins recognized by MAb 5C6. HeLa,
Vero, and CHO cells did not provide specific signals, whereas MAb 5C6
recognized proteins in lysates of B95a, BJAB cells, human
activated PBMC and PBL, and the FACS-sorted SLAM-transduced
CHO (CHO-SLAM) cells (Fig. 3). SLAM was
most strongly expressed by B95a cells. The band appeared as a broad
smear since SLAM is highly glycosylated. In addition, SLAM can interact
with itself to form homodimers and trimers (24), as seen
in BJAB cells (Fig. 3, lane 4). Similar bands were detected with a
commercial anti-SLAM antibody (IPO-3 [not shown]). Thus, MAb 5C6
recognizes SLAM of monkey and human lymphoid cells and the selected
transduced CHO cells.
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MV susceptibility of CHO-SLAM cells.
The FACS-sorted
transduced CHO cells express high amounts of SLAM and were designated
CHO-SLAM cells (Fig. 4a). CHO-SLAM cells gained the capacity to bind and replicate both wild-type and vaccine MV. The MV vaccine-like strain Edm bound with high affinity to CHO-CD46
cells and with lower affinity to CHO-SLAM cells (Fig. 4b), whereas
wild-type strain WTFb bound only to CHO-SLAM cells (Fig. 4c). After
infection with Edm or WTFb, the CHO-SLAM cells formed large syncytia
(Fig. 4d and e), whereas the parental CHO cells did not support
syncytium formation (Fig. 4f and g). These data demonstrate that SLAM
mediates viral binding, uptake, and syncytium formation and is a
cellular receptor for wild-type and vaccine-like MV.
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SLAM downregulation after infection or contact with MV-infected
cells.
Since SLAM is a costimulatory molecule, the virus-SLAM
interaction could possibly interfere with the stimulation of
lymphocytes and contribute to immunosuppression during acute
measles. This could happen either by blocking a costimulatory signal or
by inducing a negative signal via SLAM. The first aspect, blocking
costimulatory signaling, could be achieved by binding of virus or
virus-infected cells blocking the binding of natural ligands or by the
induction of receptor modulation. We therefore investigated whether
SLAM is downregulated from the surface of cells after infection or contact with MV-infected cells. SLAM was strongly downregulated from
the surface of BJAB cells persistently infected with WTFb or Edm (Fig.
5a). Infection of primary human PBL led
to the specific downregulation of SLAM from the cell surface, whereas
the activation marker CD69 was simultaneously upregulated (Fig. 5b and
c). Infection of cell lines such as BJAB and B95a with WTFb or Edm also
induced the receptor modulation (not shown).
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Role of SLAM in contact-mediated proliferation inhibition of
lymphocytes.
The direct contact of MV-infected cells or virus with
target cells leads not only to receptor modulation but also to a
proliferative inhibition of these contacted cells (responder cells)
(33). To test whether SLAM is involved in the induction of
this negative signal, we assessed the influence of MV receptor
antibodies in proliferation inhibition tests. We showed above that the
anti-SLAM antibody 5C6 (50 µg/ml) efficiently blocks high-affinity
binding of MV to SLAM. However, also high concentrations of MAb 5C6 had no significant influence on the proliferative inhibition of the tested
cells induced by either wild-type or vaccine MV (Fig. 6). Using human
PBL or BJAB cells as responder cells which express both virus
receptors, CD46 and SLAM, antibodies to both receptors together (Fig.
6a and b) and to SLAM or CD46 alone (not
shown) had no significant effect on the induction of proliferative
inhibition by MV WTFb and Edm. In the case of B95a cells expressing
only SLAM as receptor, 5C6 had also no effect on proliferation
inhibition induced by WTFb and a slight enhancing effect on the
proliferation inhibition induced by Edm (Fig. 6c). Using CD46-positive,
SLAM-negative Jurkat cells, both viruses induced the proliferative
inhibition also in the absence of SLAM, and anti-CD46 antibodies had no
effect on proliferation inhibition (Fig. 6d). Antibodies were used in concentrations of 2, 10, and 50 µg/ml without effects (the data with
50 µg/ml are shown in Fig. 6). As controls, the cells were treated
with antibodies in the absence of virus. Under these conditions, anti-SLAM antibodies led to a slight (up to 8%) stimulation of proliferation, and anti-CD46 had no effect on proliferation.
Furthermore, we have described earlier that the monocytic U937 cells
are susceptible to proliferative inhibition by MV contact
(33), although these cells lack SLAM. The absence of SLAM
in Jurkat and U937 cells was confirmed by reverse transcription-PCR and
flow cytometry (not shown). These data indicate that the proliferative
inhibition induced by MV contact is independent of the presence or
absence of the MV-binding receptors SLAM and CD46.
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DISCUSSION |
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Top
Abstract
Introduction
Materials and Methods
Results
Discussion
References
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CD46 was identified as an MV receptor with high affinity for MV vaccine-like strains Edm and Hallé (8, 30) and has low or no affinity to a number of wild-type isolates (3, 16, 23, 27). Using an antibody which blocks virus binding and infection of B95a cells, we selected transduced CHO cells expressing the molecule and identified it as the costimulatory molecule SLAM. The binding of wild-type and vaccine MV to B95a cells was inhibited by MAb 5C6 in a dose-dependent manner and nearly completely at 50 µg/ml. This suggests that SLAM is the only accessible binding receptor for MV on these cells. When CD46 is present in addition to SLAM on cells such as human PBL, the binding of MV with high affinity to CD46 was not influenced by anti-SLAM antibodies. Vice versa, anti-CD46 antibodies did not disturb the binding of wild-type viruses to SLAM. This indicates that both receptors can interact independently with MV. Since B95a cells have been used successfully to isolate a number of MV strains from patients and are susceptible for infection with MV laboratory strains, and since SLAM-expressing CHO cells are infected by all MV strains tested, SLAM is presumably a receptor for all MV strains. Our results fully confirm the data published recently by Tatsuo et al. (40).
We were interested in whether the virus-SLAM interaction (in the absence of infection) can induce contact-mediated proliferative inhibition of cells. Sensitive responder cells for contact-mediated proliferation inhibition in vitro are primary PBL and cell lines of hematopoietic origin such as B95a, BJAB, Jurkat, Molt4, U937, and HL60 (33, 44). In both contacted (9, 38) and infected (29) cells, progression to the S phase of the cell cycle is prevented by a dominant negative signal. The fact that several of these cell lines are SLAM negative (or SLAM and CD46 negative, like murine lymphoid cells) in conjunction with our data using SLAM-blocking antibodies indicate that SLAM is not involved in the induction of this negative signal. In addition, the published findings and data presented here demonstrate that this is also the case for CD46. Thus, both MV-binding receptors SLAM and CD46 are not required, and cell surface structures mediating the virus contact-mediated inhibition of proliferation have not been identified. On the viral side, it is known that a complex of the MV H and F proteins is required for this interaction and that activation of the F protein by cleavage is essential for contact-mediated proliferation inhibition (33, 44).
MV-induced immunosuppression is a multifactorial process to which the infection of certain subpopulations of regulatory cells, the direct contact between MV envelope proteins with cell surface receptors (31, 33, 44), and soluble factors such as interleukin (IL-12) (18) may contribute. Measles patients suffer from pronounced lymphopenia and an unresponsiveness of lymphocytes to mitogens, CD3-cross-linking agents, and secondary and recall antigens (for a review, see reference 4). Since SLAM is a signaling transmembrane molecule present on the surface of memory and activated T and B lymphocytes (2, 7, 32, 39), its engagement in virus binding and subsequent downregulation may well influence the immune response in vivo. Our finding that the contact-mediated proliferative inhibition of lymphocytes is not mediated by SLAM does not exclude involvement of SLAM in other virally caused disturbances of the immune response.
It is interesting that SLAM is not expressed by monocytes/macrophages
(for a review, see reference 39), although these cells are
primary target cells for MV (10, 14), which besides other cytokines produce IL-12. This interleukin is critical for the development of the cell-mediated immune response as inducer of gamma
interferon (IFN-
) from T and NK cells, required for the development
of Th1 responses, and is required as a comitogen for T and NK cells
(41). IL-12 has been found to be diminished after infection of monocytes with MV or cross-linking of CD46, and this may
play a role for suppression of cell-mediated immunity
(18). In the light of receptor usage by various MV
strains, this raises the question as to how wild-type MV isolates,
which do not interact with CD46, may infect SLAM-negative monocytes and
reduce IL-12 levels. On these cells, MV might use either CD46, although
with a low binding affinity not detected by standard methods, another unknown receptor, or another uptake mechanism.
Interaction of activated human lymphocytes with MV simultaneously induced both proliferative inhibition and downregulation of SLAM. In B lymphocytes, ligation of SLAM induces the rapid dephosphorylation of both Src homology 2-containing inositol phosphatase and SLAM, as well as the association of Lyn and Fgr kinases with this phosphatase, and enhances CD95-mediated apoptosis (26). MV infection was found earlier to induce apoptosis in stimulated PBMC and T-cell cultures (17) and in SCID mice engrafted with human thymus/liver implants (1, 42). It remains to be elucidated whether MV-induced apoptosis is related to SLAM signaling.
During acute measles, there is an initial Th1 response with release of
IFN- and IL-2, followed by a prolonged presence of IL-4 in the
plasma of patients when the rash subsides (12, 13). In
vitro, stimulation of PBMC from patients with T-cell mitogens such as
PHA or anti-CD3 antibodies elicits little IFN- and IL-2 but large
amounts of IL-4 (43). Interestingly, engagement of SLAM
induces IFN- in T cells and redirects the Th2 phenotype of helper T
lymphocytes to a Th1/Th0 phenotype (6). Vice versa, absence of SLAM may bias the immune response in the opposite direction to a Th2 type. One mechanism leading to absence of SLAM or blocking SLAM signaling in lymphocytes is the virus-induced downregulation of
SLAM. Thus, MV-induced downregulation of SLAM may contribute to the
prolonged Th2 response in measles patients at times postinfection (after the rash) when sufficient MV-infected cells and glycoproteins are produced to contact a significant number of lymphocytes.
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ACKNOWLEDGMENTS |
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We thank Franziska Dimpfel for technical assistance and Sonja Rotzoll for assistance with the fluorescence-activated cell sorter.
We thank the Deutsche Forschungsgemeinschaft for financial support.
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FOOTNOTES |
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* Corresponding author. Mailing address: Institut für Virologie und Immunbiologie, Versbacher Str. 7, D-97078 Würzburg, Germany. Phone: 49-931-2015954. Fax: 49-931-2013934. E-mail: jss{at}vim.uni-wuerzburg.de.
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Abstract
Introduction
Materials and Methods
Results
Discussion
References
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Journal of Virology, May 2001, p. 4499-4505, Vol. 75, No. 10
0022-538X/01/$04.00+0 DOI: 10.1128/JVI.75.10.4499-4505.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
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