The mechanism of Axl-mediated Ebola virus infection.
We previously reported that expression of the receptor-type tyrosine kinase Axl, which regulates cell survival and activation, enhances both pseudotype and live Ebola virus (EBOV) infection. To clarify the mechanistic basis of this enhancement, we created a series of Axl mutants and identified amino acids/domains necessary for this function, by using a pseudotype virus carrying the EBOV glycoprotein (GP). Analyses of the Axl mutants showed the importance of extracellular and intracellular regions for Axl functions, including ligand binding and signal transduction, in EBOV GP-mediated infection. These data suggest that EBOV uses the physiological functions of Axl to enter cells.
Shimojima
Masayuki
M
Division of Virology, Department of Microbiology and Immunology, University of Tokyo, Tokyo 108-8639, Japan.
Ikeda
Yasuhiro
Y
Kawaoka
Yoshihiro
Y
D002460:Cell Line; D029043:Ebolavirus / Q000235:genetics / Q000472:pathogenicity* / Q000502:physiology*; D006023:Glycoproteins / Q000502:physiology; D006801:Humans; D019169:Jurkat Cells; D007668:Kidney; D016296:Mutagenesis; D015513:Oncogene Proteins / Q000235:genetics / Q000502:physiology*; D010957:Plasmids; D016133:Polymerase Chain Reaction; D011518:Proto-Oncogene Proteins; D020794:Receptor Protein-Tyrosine Kinases / Q000235:genetics / Q000502:physiology*; D011994:Recombinant Proteins / Q000378:metabolism; D014764:Viral Proteins / Q000235:genetics / Q000502:physiology*; D000094963:Axl Receptor Tyrosine Kinase
D006023:Glycoproteins; D015513:Oncogene Proteins; D011518:Proto-Oncogene Proteins; D011994:Recombinant Proteins; D014764:Viral Proteins; D020794:Receptor Protein-Tyrosine Kinases; D000094963:Axl Receptor Tyrosine Kinase