Measles Virus (MV) Nucleoprotein Binds to a Novel Cell Surface Receptor Distinct from FcγRII via Its C-Terminal Domain: Role in MV-Induced Immunosuppression

Laine, David; Trescol-Biémont, Marie-Claude; Longhi, Sonia; Libeau, Geneviève; Marie, Julien C.; Vidalain, Pierre‐Olivier; Azocar, Olga; Diallo, Adama; Canard, Bruno; Rabourdin–Combe, Chantal; Valentin, Hélène

doi:10.1128/jvi.77.21.11332-11346.2003

Cited by 76 publications

(84 citation statements)

References 63 publications

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“…Avota et al showed that MV envelope proteins inhibit the CD3/CD28-induced proliferation of T cells by affecting the phosphatidylinositol 3-/Akt kinase pathway (5). The nucleocapsid (N) protein of MV was shown to exhibit immunosuppressive activities by binding the Fc␥ receptor type II on antigen-presenting cells (30) or the N protein receptor expressed on a large variety of cell types (28). These studies were performed in vitro.…”

Section: Discussionmentioning

confidence: 99%

Measles Virus Infection of SLAM (CD150) Knockin Mice Reproduces Tropism and Immunosuppression in Human Infection

Ohno¹,

Ono²,

Seki³

et al. 2007

J Virol

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The human signaling lymphocyte activation molecule (SLAM, also called CD150), a regulator of antigendriven T-cell responses and macrophage functions, acts as a cellular receptor for measles virus (MV), and its V domain is necessary and sufficient for receptor function. We report here the generation of SLAM knockin mice in which the V domain of mouse SLAM was replaced by that of human SLAM. The chimeric SLAM had an expected distribution and normal function in the knockin mice. Splenocytes from the SLAM knockin mice permitted the in vitro growth of a virulent MV strain but not that of the Edmonston vaccine strain. Unlike in vitro infection, MV could grow only in SLAM knockin mice that also lacked the type I interferon receptor (IFNAR). After intraperitoneal or intranasal inoculation, MV was detected in the spleen and lymph nodes throughout the body but not in the thymus. Notably, the virus appeared first in the mediastinal lymph node after intranasal inoculation. Splenocytes from MV-infected IFNAR ؊/؊ SLAM knockin mice showed suppression of proliferative responses to concanavalin A. Thus, MV infection of SLAM knockin mice reproduces lymphotropism and immunosuppression in human infection, serving as a useful small animal model for measles.

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Section: Discussionmentioning

confidence: 99%

Measles Virus Infection of SLAM (CD150) Knockin Mice Reproduces Tropism and Immunosuppression in Human Infection

Ohno¹,

Ono²,

Seki³

et al. 2007

J Virol

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“…MV and the F/H complex have a number of effects on lymphocytes, including cell cycle arrest at the G 0 /G 1 phase, reduced expression and activity of cyclin-dependent kinase complexes, delayed degradation of p27Kip, and inhibition of actin remodeling, T-cell polarization, and TcR clustering to the site of T-cell/antigen-presenting cell contact (35,104,108,130). In addition to the MV F/H protein complex, the MV nucleoprotein has been shown to inhibit antigen-specific or mitogen-induced T-cell proliferation, presumably via binding of a putative nucleoprotein binding receptor expressed upon T-cell activation (78,91,92).…”

Section: (And Other Morbilliviruses)mentioning

confidence: 99%

Viral Modulation of T-Cell Receptor Signaling

Jerome

2008

J Virol

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“…A short sequence in the MeV N tail (residues 489 to 506) folds into a dynamic helical structure that is stabilized by binding of the viral phosphoprotein that carries the viral RNA-dependent RNA polymerase (12,13,16). The N tail is also involved in binding host proteins, such as hsp70 (5,26) and interferon regulatory factor 3 (14,15). So far, the location of the N tail on the helix is not known, although it is usually shown on the outside in cartoons that illustrate transcription and replication of paramyxoviruses (see Fig.…”

mentioning

confidence: 99%

Nucleoprotein-RNA Orientation in the Measles Virus Nucleocapsid by Three-Dimensional Electron Microscopy

Desfosses

Goret

Estrozi

et al. 2011

J Virol

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Recombinant measles virus nucleoprotein-RNA (N-RNA) helices were analyzed by negative-stain electron microscopy. Three-dimensional reconstructions of trypsin-digested and intact nucleocapsids coupled to the docking of the atomic structure of the respiratory syncytial virus (RSV) N-RNA subunit into the electron microscopy density map support a model that places the RNA at the exterior of the helix and the disordered C-terminal domain toward the helix interior, and they suggest the position of the six nucleotides with respect to the measles N protomer.The RNA genome of nonsegmented negative-strand RNA viruses is tightly and regularly encapsidated by the viral nucleoprotein N, providing flexible helical templates for viral transcription and replication. Upon heterologous expression, nucleoproteins associate not only with long cellular RNAs to form helical nucleocapsids undistinguishable from the viral ones but also with short cellular RNAs that noncovalently close up into N-RNA rings. In the rings, N-RNA is sterically constrained in a biologically inactive form, but the rings have an advantage of being rigid enough for X-ray crystallography. Conversely, the helical assemblies are challenging for electron microscopy (EM) analysis because of their flexibility but are the biologically relevant ones.The atomic structures of N-RNA rings of rabies virus and vesicular stomatitis virus (both rhabdoviruses) (1, 10) reveal the shielding of RNA between two domains of N in a positively charged cleft situated inside the rings. Extended N-and Cterminal domains reach out to neighboring N protomers in order to stabilize and rigidify the structure. Recently, the structure of N-RNA rings of respiratory syncytial virus (RSV; a paramyxovirus) was determined (24). The global architecture of the nucleoprotein is very similar to that of the rhabdoviruses, although there are 7 ribonucleotides (nt) instead of 9 bound to each N protomer. However, the lateral contacts between adjacent N subunits of the ring confer to it an opposite curvature, which results in an outward RNA groove location. RSV N has an N-terminal exchange domain similar to that of rhabdovirus N, but the C-terminal domain is slightly different, as it is not clearly involved in contacts between subsequent N protomers. Is this inversion of the subunit orientation due simply to steric constraints in the ring, or does it also take place in a helical nucleocapsid? Tawar and coworkers modeled an RSV N-RNA helix but could not directly dock the atomic structure of RSV N into their helical EM reconstruction (24).A sequence alignment between RSV N and measles virus N (MeV N), both paramyxovirus nucleoproteins, is difficult to interpret because of the lack of amino acid identity. However, a comparison of the secondary structure elements observed in the RSV N structure, with a secondary structure prediction for MeV N (6) (Fig. 1), shows even more similarity than that between rhabdovirus and RSV N. This comparison also shows that the ␤-hairpin projecting from the distal end of the RSV N ...

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Measles Virus (MV) Nucleoprotein Binds to a Novel Cell Surface Receptor Distinct from FcγRII via Its C-Terminal Domain: Role in MV-Induced Immunosuppression

Abstract: During acute measles virus (MV) infection

Cited by 76 publications

References 63 publications

Measles Virus Infection of SLAM (CD150) Knockin Mice Reproduces Tropism and Immunosuppression in Human Infection

Measles Virus Infection of SLAM (CD150) Knockin Mice Reproduces Tropism and Immunosuppression in Human Infection

Viral Modulation of T-Cell Receptor Signaling

Nucleoprotein-RNA Orientation in the Measles Virus Nucleocapsid by Three-Dimensional Electron Microscopy

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