This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Schneider-Schaulies, J. Articles by ter Meulen, V. Search for Related Content PubMed PubMed Citation Articles by Schneider-Schaulies, J. Articles by ter Meulen, V.

 Previous Article  |  Next Article 

J. Virol., Apr 1995, 2248-2256, Vol 69, No. 4
Copyright © 1995, American Society for Microbiology

Physical association of moesin and CD46 as a receptor complex for measles virus

J Schneider-Schaulies, LM Dunster, R Schwartz-Albiez, G Krohne and V ter Meulen
Institut fur Virologie und Immunbiologie, Wurzburg, Germany.

Recently, two cellular membrane proteins, the membrane cofactor protein CD46 and the membrane-organizing external spike protein, moesin, have been identified to be functionally associated with measles virus (MV) infectivity of cells. We investigated the functional consequences of binding of monoclonal antibodies to both molecules individually and combined on MV attachment, fusion, and plaque formation and the putative direct physical interaction of moesin and CD46. We found that antibodies to moesin or CD46 separately inhibited MV-cell interactions to a high percentage in the plaque test, by approximately 85 and 75%, respectively. The inhibition by combinations of antibodies was additive at low concentrations and complete at high concentrations. This indicates that similar sites of interaction were blocked by steric hindrance. Furthermore, antimoesin antibodies blocked the infection of CD46-negative mouse cell lines with MV. Chemical cross-linking of cell surface proteins indicated the close proximity of CD46 and moesin in the membrane of human cells, and coimmunoprecipitation of moesin with CD46 suggested their physical interaction. Immunohistochemically by electron microscopy, CD46 and moesin were found to be localized at sites of the cellular membrane where MV particles adsorbed. These data support a model of direct interaction of CD46 and moesin in the cellular membrane and suggest that this complex is functionally involved in the uptake of MV into cells.

This article has been cited by other articles:

• Schneider-Schaulies, S., Dittmer, U. (2006). Silencing T cells or T-cell silencing: concepts in virus-induced immunosuppression. J. Gen. Virol. 87: 1423-1438 [Abstract] [Full Text]  
• Newcombe, N. G., Johansson, E. S., Au, G., Lindberg, A. M., Barry, R. D., Shafren, D. R. (2004). Enterovirus Capsid Interactions with Decay-Accelerating Factor Mediate Lytic Cell Infection. J. Virol. 78: 1431-1439 [Abstract] [Full Text]  
• Erlenhoefer, C., Wurzer, W. J., Löffler, S., Schneider-Schaulies, S., ter Meulen, V., Schneider-Schaulies, J. (2001). CD150 (SLAM) Is a Receptor for Measles Virus but Is Not Involved in Viral Contact-Mediated Proliferation Inhibition. J. Virol. 75: 4499-4505 [Abstract] [Full Text]  
• Hammond, A. L., Plemper, R. K., Zhang, J., Schneider, U., Russell, S. J., Cattaneo, R. (2001). Single-Chain Antibody Displayed on a Recombinant Measles Virus Confers Entry through the Tumor-Associated Carcinoembryonic Antigen. J. Virol. 75: 2087-2096 [Abstract] [Full Text]  
• Kurita-Taniguchi, M., Fukui, A., Hazeki, K., Hirano, A., Tsuji, S., Matsumoto, M., Watanabe, M., Ueda, S., Seya, T. (2000). Functional Modulation of Human Macrophages Through CD46 (Measles Virus Receptor): Production of IL-12 p40 and Nitric Oxide in Association with Recruitment of Protein-Tyrosine Phosphatase SHP-1 to CD46. J. Immunol. 165: 5143-5152 [Abstract] [Full Text]  
• Triantafilou, K., Triantafilou, M., Takada, Y., Fernandez, N. (2000). Human Parechovirus 1 Utilizes Integrins alpha vbeta 3 and alpha vbeta 1 as Receptors. J. Virol. 74: 5856-5862 [Abstract] [Full Text]  
• Maisner, A., Mrkic, B., Herrler, G., Moll, M., Billeter, M. A., Cattaneo, R., Klenk, H.-D. (2000). Recombinant measles virus requiring an exogenous protease for activation of infectivity. J. Gen. Virol. 81: 441-449 [Abstract] [Full Text]  
• Tohme, Z. N., Amar, S., Van Dyke, T. E. (1999). Moesin Functions as a Lipopolysaccharide Receptor on Human Monocytes. Infect. Immun. 67: 3215-3220 [Abstract] [Full Text]  
• Skoudy, A, Nhieu, G., Mantis, N, Arpin, M, Mounier, J, Gounon, P, Sansonetti, P (1999). A functional role for ezrin during Shigella flexneri entry into epithelial cells. J. Cell Sci. 112: 2059-2068 [Abstract]  
• Galbraith, S. E., Tiwari, A., Baron, M. D., Lund, B. T., Barrett, T., Cosby, S. L. (1998). Morbillivirus Downregulation of CD46. J. Virol. 72: 10292-10297 [Abstract] [Full Text]  
• Takeda, M., Kato, A., Kobune, F., Sakata, H., Li, Y., Shioda, T., Sakai, Y., Asakawa, M., Nagai, Y. (1998). Measles Virus Attenuation Associated with Transcriptional Impediment and a Few Amino Acid Changes in the Polymerase and Accessory Proteins. J. Virol. 72: 8690-8696 [Abstract] [Full Text]  
• Doi, Y., Kurita, M., Matsumoto, M., Kondo, T., Noda, T., Tsukita, S., Tsukita, S., Seya, T. (1998). Moesin Is Not a Receptor for Measles Virus Entry into Mouse Embryonic Stem Cells. J. Virol. 72: 1586-1592 [Abstract] [Full Text]  
• Buchholz, C. J., Koller, D., Devaux, P., Mumenthaler, C., Schneider-Schaulies, J., Braun, W., Gerlier, D., Cattaneo, R. (1997). Mapping of the Primary Binding Site of Measles Virus to Its Receptor CD46. J. Biol. Chem. 272: 22072-22079 [Abstract] [Full Text]  
• Schlender, J., Schnorr, J.-J., Spielhofer, P., Cathomen, T., Cattaneo, R., Billeter, M. A., ter Meulen, V., Schneider-Schaulies, S. (1996). Interaction of measles virus glycoproteins with the surface of uninfected peripheral blood lymphocytes induces immunosuppression in vitro. Proc. Natl. Acad. Sci. USA 93: 13194-13199 [Abstract] [Full Text]