TY - JOUR
T1 - The mechanism of Axl-mediated ebola virus infection
AU - Shimojima, Masayuki
AU - Ikeda, Yasuhiro
AU - Kawaoka, Yoshihiro
N1 - Funding Information:
Financial support: Core Research for Evolutional Science and Technology Agency of the Japan Science and Technology Agency; Japanese Ministry of Education, Culture, Sports Science and Technology; Japanese Ministry of Health, Labor and Welfare; National Institutes of Health (NIH)/National Institute of Allergy and Infectious Diseases (NIAID) (Public Health Service research grant); NIH/NIAID Regional Center of Excellence for Biodefense and Emerging Infectious Diseases Research Program. Supplement sponsorship is detailed in the Acknowledgments.
Funding Information:
Supplement sponsorship. This article was published as part of a supplement entitled “Filoviruses: Recent Advances and Future Challenges,” sponsored by the Public Health Agency of Canada, the National Institutes of Health, the Canadian Institutes of Health Research, Cangene, CUH2A, Smith Carter, Hemisphere Engineering, Crucell, and the International Centre for Infectious Diseases.
PY - 2007/11/15
Y1 - 2007/11/15
N2 - 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.
AB - 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.
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U2 - 10.1086/520594
DO - 10.1086/520594
M3 - Article
C2 - 17940958
AN - SCOPUS:38449119465
SN - 0022-1899
VL - 196
SP - S259-S263
JO - Journal of Infectious Diseases
JF - Journal of Infectious Diseases
IS - SUPPL. 2
ER -