PMID:18287234

Citation	Tahara, M, Takeda, M, Shirogane, Y, Hashiguchi, T, Ohno, S and Yanagi, Y (2008) Measles virus infects both polarized epithelial and immune cells by using distinctive receptor-binding sites on its hemagglutinin. J. Virol. 82:4630-7
Abstract	Measles is one of the most contagious human infectious diseases and remains a major cause of childhood morbidity and mortality worldwide. The signaling lymphocyte activation molecule (SLAM), also called CD150, is a cellular receptor for measles virus (MV), presumably accounting for its tropism for immune cells and its immunosuppressive properties. On the other hand, pathological studies have shown that MV also infects epithelial cells at a later stage of infection, although its mechanism has so far been unknown. In this study, we show that wild-type MV can infect and produce syncytia in human polarized epithelial cell lines independently of SLAM and CD46 (a receptor for the vaccine strains of MV). Progeny viral particles are released exclusively from the apical surface of these polarized epithelial cell lines. We have also identified amino acid residues on the MV attachment protein that are likely to interact with a putative receptor on epithelial cells. All of these residues have aromatic side chains and may form a receptor-binding pocket located in a different position from the putative SLAM- and CD46-binding sites on the MV attachment protein. Thus, our results indicate that MV has an intrinsic ability to infect both polarized epithelial and immune cells by using distinctive receptor-binding sites on the attachment protein corresponding to each of their respective receptors. The ability of MV to infect polarized epithelial cells and its exclusive release from the apical surface may facilitate its efficient transmission via aerosol droplets, resulting in its highly contagious nature.
Links	PubMed PMC2293038 Online version:10.1128/JVI.02691-07
Keywords	Animals; Antigens, CD; Antigens, CD46; Binding Sites; Cell Line; Cell Polarity; Epithelial Cells/virology; Hemagglutinins/metabolism; Humans; Immune System/cytology; Immune System/virology; Lymphocytes/virology; Measles virus/pathogenicity; Receptors, Cell Surface; Receptors, Virus/metabolism; Virus Attachment
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
9PARA:Q83639		GO:0000768: syncytium formation by plasma membrane fusion	ECO:0000315:		P		Different substitutions in the residues of the H protein are shown in figure 5A. While the wild type and some mutant H proteins produced syncytia, some mutants failed to produce syncytia, showing that these residues are important for the function of the H protein, which is to perform syncytia by cell fusion. Figure 4 also shows the cell-to-cell fusion properties of the H protein.	complete CACAO 7337
9PARA:Q83639	involved_in	GO:0000768: syncytium formation by plasma membrane fusion	ECO:0000315: mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete

References

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