The DOI matches its Crossref record; 216 of the 216 references it cites were found in a registry or an index.
Fc receptors in antibody‐dependent enhancement of viral infections
Open accessAbstract
Summary: Sensitization of the humoral immune response to invading viruses and production of antiviral antibodies forms part of the host antiviral repertoire. Paradoxically, for a number of viral pathogens, under certain conditions, antibodies provide an attractive means of enhanced virus entry and replication in a number of cell types. Known as antibody‐dependent enhancement (ADE) of infection, the phenomenon occurs when virus‐antibody immunocomplexes interact with cells bearing complement or Fc receptors, promoting internalization of the virus and increasing infection. Frequently associated with exacerbation of viral disease, ADE of infection presents a major obstacle to the prevention of viral disease by vaccination and is thought to be partly responsible for the adverse effects of novel antiviral therapeutics such as intravenous immunoglobulins. There is a growing body of work examining the intracellular signaling pathways and epitopes responsible for mediating ADE, with a view to aiding rational design of antiviral strategies. With in vitro studies also confirming ADE as a feature of infection for a growing number of viruses, challenges remain in understanding the multilayered molecular mechanisms of ADE and its effect on viral pathogenesis.
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Vabret, N., Britton, G. J., Gruber, C., Hegde, S., Kim, J., Kuksin, M., Levantovsky, R., Malle, L., Moreira, A., Park, M. D., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.05.002 · Cited by 1,623
De novo design of picomolar SARS-CoV-2 miniprotein inhibitors
Cao, L., Goreshnik, I., Coventry, B., Case, J. B., Miller, L., Kozodoy, L., Chen, R. E., Carter, L., Walls, A. C., Park, Y.-J., et al. (2020) · Science · doi:10.1126/science.abd9909 · Cited by 742
SARS-CoV-2 immunity: review and applications to phase 3 vaccine candidates
Poland, G. A., Ovsyannikova, I. G., & Kennedy, R. B. (2020) · The Lancet · doi:10.1016/s0140-6736(20)32137-1 · Cited by 572
Winkler, E. S., Gilchuk, P., Yu, J., Bailey, A. L., Chen, R. E., Chong, Z., Zost, S. J., Jang, H., Huang, Y., Allen, J. D., et al. (2021) · Cell · doi:10.1016/j.cell.2021.02.026 · Cited by 366
Muralidar, S., Ambi, S. V., Sekaran, S., & Krishnan, U. M. (2020) · Biochimie · doi:10.1016/j.biochi.2020.09.018 · Cited by 346
Metadata
- Authors
- Taylor, A., Foo, S., Bruzzone, R., Vu Dinh, L., King, N. J. C., & Mahalingam, S.
- Venue
- Immunological Reviews
- Publisher
- Wiley
- Published
- 2015-10-26
- Volume
- 268
- Issue
- 1
- Pages
- 340-364
- ISSN
- 0105-2896 (ISSN-L)
- 1600-065X
- OpenAlex
- W2102144534
- Cited by
- 255
- References
- 216
- FWCI
- 1.46
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
