RT Journal Article SR Electronic(1) A1 Weis, Michael A1 Behner, Laura A1 Hoffmann, Markus A1 Krüger, Nadine A1 Herrler, Georg A1 Drosten, Christian A1 Drexler, Jan Felix A1 Dietzel, Erik A1 Maisner, AndreaYR 2014 T1 Characterization of African bat henipavirus GH-M74a glycoproteins JF Journal of General Virology, VO 95 IS 3 SP 539 OP 548 DO https://doi.org/10.1099/vir.0.060632-0 PB Microbiology Society, SN 1465-2099, AB In recent years, novel henipavirus-related sequences have been identified in bats in Africa. To evaluate the potential of African bat henipaviruses to spread in non-bat mammalian cells, we compared the biological functions of the surface glycoproteins G and F of the prototype African henipavirus GH-M74a with those of the glycoproteins of Nipah virus (NiV), a well-characterized pathogenic member of the henipavirus genus. Glycoproteins are central determinants for virus tropism, as efficient binding of henipavirus G proteins to cellular ephrin receptors and functional expression of fusion-competent F proteins are indispensable prerequisites for virus entry and cell-to-cell spread. In this study, we analysed the ability of the GH-M74a G and F proteins to cause cell-to-cell fusion in mammalian cell types readily permissive to NiV or Hendra virus infections. Except for limited syncytium formation in a bat cell line derived from Hypsignathus monstrosus, HypNi/1.1 cells, we did not observe any fusion. The highly restricted fusion activity was predominantly due to the F protein. Whilst GH-M74a G protein was found to interact with the main henipavirus receptor ephrin-B2 and induced syncytia upon co-expression with heterotypic NiV F protein, GH-M74a F protein did not cause evident fusion in the presence of heterotypic NiV G protein. Pulse–chase and surface biotinylation analyses revealed delayed F cleavage kinetics with a reduced expression of cleaved and fusion-active GH-M74a F protein on the cell surface. Thus, the F protein of GH-M74a showed a functional defect that is most likely caused by impaired trafficking leading to less efficient proteolytic activation and surface expression., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.060632-0