Supplement to "Relevance of potential endocytosis motifs in Cedar virus glycoprotein G for its biological activity"

The glycoprotein (G) and fusion protein (F) of henipaviruses play crucial roles in receptor binding and entry into host cells, also enabling virus spread from cell to cell without the release of infectious particles. For Cedar virus (CedV), the proteolytic activation of the F protein precursor into F1 and F2 - and thus, its biological activity - depends on clathrin-mediated endocytosis driven by classical endocytosis motifs YXXΦ and YY in the cytoplasmic tail of the F protein. Similar motifs are present in the cytoplasmic tail of CedV G protein. In this study, we investigated whether these motifs influence CedV G protein expression and transport, endocytosis from the plasma membrane, and overall the biological activity - more specifically receptor binding and mediation of fusion together with the fusion protein. Our data show that the expression of CedV G mutants is comparable to parental G in MDCK cells. Endocytosis can be detected for both parental G and its mutants. However, some G protein mutants show reduced biological activity, as indicated by a decrease in fusion when G mutants are co-expressed with CedV F protein. Interestingly, neither co-expression of CedV F and G mutants on the cell surface nor the binding of G mutants to EFNB2 receptors appears to be compromised. Consequently, the putative endocytosis motifs are not relevant for biological activity of CedV G.This supplementary dataset contains raw data files of the study and supplemental figures contained in zip files, an overview of zip files, and a list of included files.