Moesin Is Not a Receptor for Measles Virus Entry into Mouse Embryonic Stem Cells

ABSTRACT The involvement of moesin in measles virus (MV) entry was investigated with moesin-positive and -negative mouse embryonic stem (ES) cells. MV infection of these cells was very ineffective and was independent of moesin expression. Furthermore, when these cells were transfected to express human CD46, a 100-fold increase in syncytium formation was observed with these cells and was independent of the expression of moesin. The only obvious difference between moesin-positive and -negative ES cells was the shape of the syncytia formed. Moesin-negative ES cells expressing or not expressing human CD46 formed separate pieces of fragmented syncytia which were torn apart during spreading, whereas ES cells expressing moesin exhibited typical syncytia. In addition, moesin was not detected on the surface of any murine cells or cell lines that we have tested by a flow cytometric assay with moesin-specific antibodies. These findings indicate that murine moesin is neither a receptor nor a CD46 coreceptor for MV entry into mouse ES cells. Moesin is involved in actin filament-plasma membrane interactions as a cross-linker, and it affects only the spreading and shape of MV-mediated syncytia.

[1]  D. Gerlier,et al.  Antibody cross-reactivity with CD46 and lack of cell surface expression suggest that moesin might not mediate measles virus binding , 1997, Journal of virology.

[2]  A. Griesmacher,et al.  A heparin-binding protein involved in inhibition of smooth-muscle cell proliferation. , 1988, The Biochemical journal.

[3]  G. Trinchieri,et al.  Mechanism of Suppression of Cell-Mediated Immunity by Measles Virus , 1996, Science.

[4]  M. Wiles,et al.  Hematopoietic commitment during embryonic stem cell differentiation in culture. , 1993, Molecular and cellular biology.

[5]  R. Buckland,et al.  Is CD46 the cellular receptor for measles virus? , 1997, Virus research.

[6]  C. Rabourdin-Combe,et al.  Cell-to-cell contact via measles virus haemagglutinin-CD46 interaction triggers CD46 downregulation. , 1995, The Journal of general virology.

[7]  H. Ariga,et al.  Diversity of Sites for Measles Virus Binding and for Inactivation of Complement C3b and C4b on Membrane Cofactor Protein CD46 (*) , 1995, The Journal of Biological Chemistry.

[8]  Rudolf Jaenisch,et al.  Targeted mutation of the DNA methyltransferase gene results in embryonic lethality , 1992, Cell.

[9]  L. Dunster,et al.  Physical association of moesin and CD46 as a receptor complex for measles virus , 1995, Journal of virology.

[10]  U. Francke,et al.  Structure and localization on the X chromosome of the gene coding for the human filopodial protein moesin (MSN). , 1994, Genomics.

[11]  D. Gerlier,et al.  Human membrane cofactor protein (CD46) acts as a cellular receptor for measles virus , 1993, Journal of virology.

[12]  N. Sato,et al.  Perturbation of cell adhesion and microvilli formation by antisense oligonucleotides to ERM family members , 1994, The Journal of cell biology.

[13]  M. Dehoff,et al.  Mouse Crry/p65. Characterization of monoclonal antibodies and the tissue distribution of a functional homologue of human MCP and DAF. , 1993, Journal of immunology.

[14]  J. Atkinson,et al.  Measles virus and C3 binding sites are distinct on membrane cofactor protein (CD46). , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[15]  W. Braun,et al.  A 3D model for the measles virus receptor CD46 based on homology modeling, Monte Carlo simulations, and hemagglutinin binding studies , 1997, Protein science : a publication of the Protein Society.

[16]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.

[17]  Y. Yanagi,et al.  Blocking measles virus infection with a recombinant soluble form of, or monoclonal antibodies against, membrane cofactor protein of complement (CD46). , 1995, Immunology.

[18]  J. Atkinson,et al.  The N-glycan of the SCR 2 region is essential for membrane cofactor protein (CD46) to function as a measles virus receptor , 1996, Journal of virology.

[19]  A. Bretscher,et al.  Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells. , 1993, Journal of cell science.

[20]  M. Arpin,et al.  Membrane-actin microfilament connections: an increasing diversity of players related to band 4.1. , 1994, Current opinion in cell biology.

[21]  L. Dunster,et al.  Moesin: a cell membrane protein linked with susceptibility to measles virus infection. , 1994, Virology.

[22]  Arindam Banerjee,et al.  Submitted for publication , 1981 .

[23]  S. Yant,et al.  Identification of a cytoplasmic Tyr-X-X-Leu motif essential for down regulation of the human cell receptor CD46 in persistent measles virus infection , 1997, Journal of virology.

[24]  R. Compans,et al.  Adaptation of measles virus to polarized epithelial cells: alterations in virus entry and release. , 1997, Virology.

[25]  K. Tanaka,et al.  The CD46 transmembrane domain is required for efficient formation of measles-virus-mediated syncytium. , 1997, The Biochemical journal.

[26]  Christopher D. Richardson,et al.  The human CD46 molecule is a receptor for measles virus (Edmonston strain) , 1993, Cell.

[27]  V. Holers,et al.  The evolution of mouse and human complement C3-binding proteins: divergence of form but conservation of function. , 1992, Immunology today.

[28]  Jens,et al.  Induction of maturation of human blood dendritic cell precursors by measles virus is associated with immunosuppression. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[29]  S. Tsukita,et al.  ERM proteins: head-to-tail regulation of actin-plasma membrane interaction. , 1997, Trends in biochemical sciences.

[30]  S. Tsukita,et al.  ERM (ezrin/radixin/moesin) family: from cytoskeleton to signal transduction. , 1997, Current opinion in cell biology.

[31]  S. Yant,et al.  Human cell receptor CD46 is down regulated through recognition of a membrane-proximal region of the cytoplasmic domain in persistent measles virus infection , 1996, Journal of virology.

[32]  A. Bretscher.  Microfilament structure and function in the cortical cytoskeleton. , 1991, Annual review of cell biology.

[33]  Ron Kwok,et al.  A Mini-Surge on the Ryder Glacier, Greenland, Observed by Satellite Radar Interferometry , 1996, Science.

[34]  D. Gerlier,et al.  Interactions between the ectodomains of haemagglutinin and CD46 as a primary step in measles virus entry. , 1996, The Journal of general virology.

[35]  N. Sato,et al.  ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actin-based cytoskeletons , 1994, The Journal of cell biology.

[36]  D. Hourcade,et al.  Mouse complement regulatory protein Crry/p65 uses the specific mechanisms of both human decay-accelerating factor and membrane cofactor protein , 1995, The Journal of experimental medicine.

[37]  M. Amieva,et al.  Subcellular localization of moesin in dynamic filopodia, retraction fibers, and other structures involved in substrate exploration, attachment, and cell-cell contacts. , 1995, Experimental cell research.

[38]  L. Dunster,et al.  Moesin, and not the murine functional homologue (Crry/p65) of human membrane cofactor protein (CD46), is involved in the entry of measles virus (strain Edmonston) into susceptible murine cell lines. , 1995, The Journal of general virology.

[39]  H. Ariga,et al.  Modulation of complement regulatory function and measles virus receptor function by the serine-threonine-rich domains of membrane cofactor protein (CD46). , 1994, The Biochemical journal.

[40]  H. Furthmayr,et al.  Moesin: a member of the protein 4.1-talin-ezrin family of proteins. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[41]  C. Broder,et al.  Functional and structural interactions between measles virus hemagglutinin and CD46 , 1995, Journal of virology.

[42]  N. Sato,et al.  A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites. , 1992, Journal of cell science.

[43]  E. Mekada,et al.  Membrane-anchored heparin-binding EGF-like growth factor (HB-EGF) and diphtheria toxin receptor-associated protein (DRAP27)/CD9 form a complex with integrin alpha 3 beta 1 at cell-cell contact sites , 1995, The Journal of cell biology.

[44]  T. Seya,et al.  Quantitative analysis of membrane cofactor protein (MCP) of complement. High expression of MCP on human leukemia cell lines, which is down-regulated during cell differentiation. , 1990, Journal of immunology.

[45]  V. ter meulen,et al.  CD9, a tetraspan transmembrane protein, renders cells susceptible to canine distemper virus , 1997, Journal of virology.