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.
journal_name
Naturejournal_title
Natureauthors
Mühlebach MD,Mateo M,Sinn PL,Prüfer S,Uhlig KM,Leonard VH,Navaratnarajah CK,Frenzke M,Wong XX,Sawatsky B,Ramachandran S,McCray PB Jr,Cichutek K,von Messling V,Lopez M,Cattaneo Rdoi
10.1038/nature10639subject
Has Abstractpub_date
2011-11-02 00:00:00pages
530-3issue
7378eissn
0028-0836issn
1476-4687pii
nature10639journal_volume
480pub_type
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