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Adherens junction protein nectin-4 is the epithelial receptor for measles virus.

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Title: Adherens junction protein nectin-4 is the epithelial receptor for measles virus.
Authors: Mühlebach, Michael D., Mateo, Mathieu, Sinn, Patrick L., Prüfer, Steffen, Uhlig, Katharina M., Leonard, Vincent H. J., Navaratnarajah, Chanakha K., Frenzke, Marie, Wong, Xiao X., Sawatsky, Bevan, Ramachandran, Shyam, McCray, Paul B., Cichutek, Klaus, von Messling, Veronika, Lopez, Marc, Cattaneo, Roberto
Source: Nature. 12/22/2011, Vol. 480 Issue 7378, p530-533. 4p. 1 Color Photograph, 3 Graphs.
Subjects: Macrophages, Dendritic cells, Immunoglobulins, Epithelial cells, Green fluorescent protein
Abstract: Measles virus is an aerosol-transmitted virus that affects more than 10 million children each year and accounts for approximately 120,000 deaths. Although it was long believed to replicate in the respiratory epithelium before disseminating, it was recently shown to infect initially macrophages and dendritic cells of the airways using signalling lymphocytic activation molecule family member 1 (SLAMF1; also called CD150) as a receptor. These cells then cross the respiratory epithelium and transport the infection to lymphatic organs where measles virus replicates vigorously. How and where the virus crosses back into the airways has remained unknown. On the basis of functional analyses of surface proteins preferentially expressed on virus-permissive human epithelial cell lines, here we identify nectin-4 (ref. 8; also called poliovirus-receptor-like-4 (PVRL4)) as a candidate host exit receptor. This adherens junction protein of the immunoglobulin superfamily interacts with the viral attachment protein with high affinity through its membrane-distal domain. Nectin-4 sustains measles virus entry and non-cytopathic lateral spread in well-differentiated primary human airway epithelial sheets infected basolaterally. It is downregulated in infected epithelial cells, including those of macaque tracheae. Although other viruses use receptors to enter hosts or transit through their epithelial barriers, we suggest that measles virus targets nectin-4 to emerge in the airways. Nectin-4 is a cellular marker of several types of cancer, which has implications for ongoing measles-virus-based clinical trials of oncolysis. [ABSTRACT FROM AUTHOR]
Copyright of Nature is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
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  Data: <searchLink fieldCode="AR" term="%22Mühlebach%2C+Michael+D%2E%22">Mühlebach, Michael D.</searchLink><br /><searchLink fieldCode="AR" term="%22Mateo%2C+Mathieu%22">Mateo, Mathieu</searchLink><br /><searchLink fieldCode="AR" term="%22Sinn%2C+Patrick+L%2E%22">Sinn, Patrick L.</searchLink><br /><searchLink fieldCode="AR" term="%22Prüfer%2C+Steffen%22">Prüfer, Steffen</searchLink><br /><searchLink fieldCode="AR" term="%22Uhlig%2C+Katharina+M%2E%22">Uhlig, Katharina M.</searchLink><br /><searchLink fieldCode="AR" term="%22Leonard%2C+Vincent+H%2E+J%2E%22">Leonard, Vincent H. J.</searchLink><br /><searchLink fieldCode="AR" term="%22Navaratnarajah%2C+Chanakha+K%2E%22">Navaratnarajah, Chanakha K.</searchLink><br /><searchLink fieldCode="AR" term="%22Frenzke%2C+Marie%22">Frenzke, Marie</searchLink><br /><searchLink fieldCode="AR" term="%22Wong%2C+Xiao+X%2E%22">Wong, Xiao X.</searchLink><br /><searchLink fieldCode="AR" term="%22Sawatsky%2C+Bevan%22">Sawatsky, Bevan</searchLink><br /><searchLink fieldCode="AR" term="%22Ramachandran%2C+Shyam%22">Ramachandran, Shyam</searchLink><br /><searchLink fieldCode="AR" term="%22McCray%2C+Paul+B%2E%22">McCray, Paul B.</searchLink><br /><searchLink fieldCode="AR" term="%22Cichutek%2C+Klaus%22">Cichutek, Klaus</searchLink><br /><searchLink fieldCode="AR" term="%22von+Messling%2C+Veronika%22">von Messling, Veronika</searchLink><br /><searchLink fieldCode="AR" term="%22Lopez%2C+Marc%22">Lopez, Marc</searchLink><br /><searchLink fieldCode="AR" term="%22Cattaneo%2C+Roberto%22">Cattaneo, Roberto</searchLink>
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  Data: Measles virus is an aerosol-transmitted virus that affects more than 10 million children each year and accounts for approximately 120,000 deaths. Although it was long believed to replicate in the respiratory epithelium before disseminating, it was recently shown to infect initially macrophages and dendritic cells of the airways using signalling lymphocytic activation molecule family member 1 (SLAMF1; also called CD150) as a receptor. These cells then cross the respiratory epithelium and transport the infection to lymphatic organs where measles virus replicates vigorously. How and where the virus crosses back into the airways has remained unknown. On the basis of functional analyses of surface proteins preferentially expressed on virus-permissive human epithelial cell lines, here we identify nectin-4 (ref. 8; also called poliovirus-receptor-like-4 (PVRL4)) as a candidate host exit receptor. This adherens junction protein of the immunoglobulin superfamily interacts with the viral attachment protein with high affinity through its membrane-distal domain. Nectin-4 sustains measles virus entry and non-cytopathic lateral spread in well-differentiated primary human airway epithelial sheets infected basolaterally. It is downregulated in infected epithelial cells, including those of macaque tracheae. Although other viruses use receptors to enter hosts or transit through their epithelial barriers, we suggest that measles virus targets nectin-4 to emerge in the airways. Nectin-4 is a cellular marker of several types of cancer, which has implications for ongoing measles-virus-based clinical trials of oncolysis. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Nature is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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