CD147/EMMPRIN Acts as a Functional Entry Receptor for Measles Virus on Epithelial Cells

Watanabe, Akira; Yoneda, Misako; Ikeda, Fusako; Terao-Muto, Yuri; Sato, Hiroki; Kai, Chieko

doi:10.1128/jvi.02168-09

Cited by 104 publications

(86 citation statements)

References 36 publications

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“…This may relate to low-level infection mediated by the recently reported MV receptor CD147 (20). MV infection occurring via CD147 is independent of binding to MV H and occurs via and virion-associated cyclophilin B.…”

Section: Discussionmentioning

confidence: 99%

Attenuated, Oncolytic, but Not Wild-Type Measles Virus Infection Has Pleiotropic Effects on Human Neutrophil Function

Zhang

Patel

Dey

et al. 2012

The Journal of Immunology

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We previously showed that neutrophils play a role in regression of human tumor xenografts in immunodeficient mice following oncolytic vaccine measles virus (MV-Vac) treatment. In this study, we sought, using normal human neutrophils, to identify potential neutrophil-mediated mechanisms for the attenuated MV-Vac induced effects seen in vivo, by comparison with those consequent on wild-type (WT-MV) infection. Both MV-Vac and WT-MV infected and replicated within neutrophils, despite lack of SLAM expression. In both cases, neutrophils survived longer ex vivo postinfection. Furthermore, MV-Vac (but not WT-MV) infection activated neutrophils and stimulated secretion of several specific antitumor cytokines (IL-8, TNF-α, MCP-1, and IFN-α) via induction of de novo RNA and protein synthesis. In addition, MV-Vac (but not WT-MV) infection caused TRAIL secretion in the absence of de novo synthesis by triggering release of prefabricated TRAIL, via a direct effect upon degranulation. The differences between the outcome of infection by MV-Vac and WT-MV were not entirely explained by differential infection and replication of the viruses within neutrophils. To our knowledge, this is the first demonstration of potential mechanisms of oncolytic activity of an attenuated MV as compared with its WT parent. Furthermore, our study suggests that neutrophils have an important role to play in the antitumor effects of oncolytic MV.

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Section: Discussionmentioning

confidence: 99%

Attenuated, Oncolytic, but Not Wild-Type Measles Virus Infection Has Pleiotropic Effects on Human Neutrophil Function

Zhang

Patel

Dey

et al. 2012

The Journal of Immunology

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“…Interestingly, Watanabe et al (51) reported in 2010 that MV particles incorporate cyclophilins into their membrane. They 6 ) transiently transfected with pCG-H⌬18, pCG-H mut ⌬18, or pCG-H mut ⌬18-DARPin-9.29 were stained with K29, K71, Nc32, or L77.…”

Section: Discussionmentioning

confidence: 99%

The Receptor Attachment Function of Measles Virus Hemagglutinin Can Be Replaced with an Autonomous Protein That Binds Her2/ neu While Maintaining Its Fusion-Helper Function

Rasbach

Abel²,

Münch³

et al. 2013

J Virol

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cCell entry of enveloped viruses is initiated by attachment to the virus receptor followed by fusion between the virus and host cell membranes. Measles virus (MV) attachment to its receptor is mediated by the hemagglutinin (H), which is thought to produce conformational changes in the membrane fusion protein (F) that trigger insertion of its fusion peptide into the target cell membrane. Here, we uncoupled receptor attachment and the fusion-helper function of H by introducing Y481A, R533A, S548L, and F549S mutations into the viral attachment protein that made it blind to its normal receptors. An artificial receptor attachment protein specific for Her2/neu was incorporated into the membranes of pseudotyped lentivirus particles as a separate transmembrane protein along with the F protein. Surprisingly, these particles entered efficiently into Her2/neu-positive SK-OV-3 as well as CHO-Her2 cells. Cell entry was independent of endocytosis but strictly dependent on the presence of H. H-specific monoclonal antibodies, as well as a mutation in H interfering with H/F cooperation, blocked cell entry. The particles mediated stable and specific transfer of reporter genes into Her2/neu-positive human tumor cells also in vivo, while exhibiting improved infectivity and higher titers than Her2/neu-targeted vectors displaying the targeting domain on H. Extending the current model of MV cell entry, the data suggest that receptor binding of H is not required for its fusion-helper function but that particle-cell contact in general may be sufficient to induce the conformational changes in the H/F complex and activate membrane fusion.

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“…The anti-human peroxiredoxin 1 rabbit polyclonal antibody (Hycult Biotechnologies) was purchased. (32) in 300 l of binding buffer (10 mM HEPES [pH 7.4], 150 mM NaCl, 0.1% NP-40, protease inhibitor cocktails) at 4°C overnight. Two milligrams of chemical cross-linker 3,3Ј-dithiobis(sulfosuccinimidylpropionate) (DTSSP) (Pierce) was added to the mixture and reacted on ice for 2 h. Unreacted cross-linkers were inactivated by adding 30 l of 1 M Tris-HCl (pH 8.0), and then NaCl and imidazole were added to the mixtures, whose final concentrations were 0.5 M and 25 mM, respectively.…”

Section: Methodsmentioning

confidence: 99%

Peroxiredoxin 1 Is Required for Efficient Transcription and Replication of Measles Virus

Watanabe

Yoneda

Ikeda

et al. 2011

J Virol

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Measles is a highly contagious human disease caused by the measles virus (MeV). In this study, by proteomic analysis, we identified peroxiredoxin 1 (Prdx1) as a host factor that binds to the C-terminal region of the nucleoprotein (N; N TAIL ) of MeV. Glutathione S-transferase (GST) pulldown experiments showed that the Prdx1-binding site overlapped with the MeV phosphoprotein (P)-binding site on N TAIL and that Prdx1 competed for the binding to N TAIL with the P protein, which is a component of RNA-dependent RNA polymerase (RdRp). Furthermore, RNA interference for Prdx1 resulted in a significant reduction in MeV growth in HEK293-SLAM cells. A minigenome assay indicated that Prdx1 suppression affected the viral RNA transcription and/or replication step. Relative quantification of viral RNA by real-time PCR (RT-PCR) showed that Prdx1 suppression not only reduced viral RNA transcription and replication but also enhanced polar attenuation in viral mRNA transcription. Surface plasmon resonance analysis showed that the binding affinity of Prdx1 to MeV-N was 40-fold lower than that of MeV-P to MeV-N, which suggested that Prdx1 might be involved in the early stage of MeV infection, when the expression level of Prdx1 was much higher than that of MeV-P. Since Prdx1 was expressed abundantly and constitutively in various cells, the results in this study indicate that Prdx1 is one of the inherent host factors implicated in MeV RNA synthesis.Measles is a highly contagious and very serious human disease caused by the measles virus (MeV). MeV infection causes immunosuppression, which induces secondary infection and several complications, such as diarrhea, pneumonia, and encephalitis. Presently, measles can be prevented by administering live vaccines that are derived mainly from the MeV Edmonston strain (MeV-Ed); however, measles has still been the leading cause of death in children, particularly in developing countries, for the past 40 years (6).MeV is an enveloped virus with a negative single-stranded RNA genome and belongs to the genus Morbillivirus in the family Paramyxoviridae. MeV is composed of six structural proteins: nucleoprotein (N), phosphoprotein (P), matrix protein (M), fusion protein (F), hemagglutinin protein (H), and large protein (L). Among these structural proteins, the N, P, and L proteins are essential for viral RNA transcription and replication. The L protein exhibits RNA dependent-RNA polymerase (RdRp) activity and forms a complex with the P protein, which acts as a cofactor of RdRp. The N protein consists of two portions: the N-terminal portion, which is termed the core region, is a highly conserved region and is involved in the oligomerization and encapsidation of genomic RNA, and the C-terminal portion, which is termed the tail region, is a relatively variable and disordered region that binds to the P protein. In paramyxoviruses, the N-genomic RNA complex serves as a template for viral RNA transcription and replication by RdRp composed of P and L proteins. During viral RNA synthesis, the P protein binds ...

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CD147/EMMPRIN Acts as a Functional Entry Receptor for Measles Virus on Epithelial Cells

Cited by 104 publications

References 36 publications

Attenuated, Oncolytic, but Not Wild-Type Measles Virus Infection Has Pleiotropic Effects on Human Neutrophil Function

Attenuated, Oncolytic, but Not Wild-Type Measles Virus Infection Has Pleiotropic Effects on Human Neutrophil Function

The Receptor Attachment Function of Measles Virus Hemagglutinin Can Be Replaced with an Autonomous Protein That Binds Her2/ neu While Maintaining Its Fusion-Helper Function

Peroxiredoxin 1 Is Required for Efficient Transcription and Replication of Measles Virus

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