The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Endosomal Proteolysis of the Ebola Virus Glycoprotein Is Necessary for Infection
Open accessAbstract
Ebola virus (EboV) causes rapidly fatal hemorrhagic fever in humans and there is currently no effective treatment. We found that the infection of African green monkey kidney (Vero) cells by vesicular stomatitis viruses bearing the EboV glycoprotein (GP) requires the activity of endosomal cysteine proteases. Using selective protease inhibitors and protease-deficient cell lines, we identified an essential role for cathepsin B (CatB) and an accessory role for cathepsin L (CatL) in EboV GP-dependent entry. Biochemical studies demonstrate that CatB and CatL mediate entry by carrying out proteolysis of the EboV GP subunit GP1 and support a multistep mechanism that explains the relative contributions of these enzymes to infection. CatB and CatB/CatL inhibitors diminish the multiplication of infectious EboV-Zaire in cultured cells and may merit investigation as anti-EboV drugs.
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Neuronal loss and brain atrophy in mice lacking cathepsins B and L
Felbor, U., Kessler, B., Mothes, W., Goebel, H. H., Ploegh, H. L., Bronson, R. T., & Olsen, B. R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.112632299 · Cited by 334
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Cited by
Mechanisms of SARS-CoV-2 entry into cells
Jackson, C. B., Farzan, M., Chen, B., & Choe, H. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00418-x · Cited by 3,022
Mercer, J., Schelhaas, M., & Helenius, A. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060208-104626 · Cited by 1,057
Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme
White, J. M., Delos, S. E., Brecher, M., & Schornberg, K. (2008) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230802058320 · Cited by 892
Matsuyama, S., Nagata, N., Shirato, K., Kawase, M., Takeda, M., & Taguchi, F. (2010) · Journal of Virology · doi:10.1128/jvi.01542-10 · Cited by 778
Two-pore channels control Ebola virus host cell entry and are drug targets for disease treatment
Sakurai, Y., Kolokoltsov, A. A., Chen, C.-C., Tidwell, M. W., Bauta, W. E., Klugbauer, N., Grimm, C., Wahl-Schott, C., Biel, M., & Davey, R. A. (2015) · Science · doi:10.1126/science.1258758 · Cited by 555
Metadata
- Authors
- Chandran, K., Sullivan, N. J., Felbor, U., Whelan, S. P., & Cunningham, J. M.
- Venue
- Science
- Published
- 2005-06-10
- Volume
- 308
- Issue
- 5728
- Pages
- 1643-1645
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2022339063
- Cited by
- 826
- References
- 1
- FWCI
- 21.01
- Type
- journal article
- Language
- en
- Open access
- green
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- Chandran, K., Sullivan, N. J., Felbor, U., Whelan, S. P., & Cunningham, J. M. (2005). Endosomal Proteolysis of the Ebola Virus Glycoprotein Is Necessary for Infection. Science. https://doi.org/10.1126/science.1110656
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