Identification of sialic acid-binding function for the Middle East respiratory syndrome coronavirus spike glycoprotein
By Wentao Li, R. Hulswit, Ivy Widjaja, V. S. Raj, Ryan McBride, Wenjie Peng, W. Widagdo, M. A. Tortorici, Brenda van Dieren, Yifei Lang and 7 more. 2017
318 citations recorded by the source corpus.
Subfields: Animal Science and Zoology, Infectious Diseases
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The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Animal Science and Zoology
In Infectious Diseases
- D. Veesler
- A. Walls
- M. A. Tortorici
- Hannah Kleine-Weber
- A. Tortoricia
- David Veeslera
- Andrew T. McGuire
- S. Pöhlmann
Citations in the corpus
- Towards a solution to MERS: protective human monoclonal antibodies targeting different domains and functions of the MERS-coronavirus spike glycoprotein (2019, unknown): “This Sia binding activity serves as an attachment factor for MERS CoV infection in a cell type dependent manner [16].”
- Structural insights into coronavirus entry (2019, background): “The sialoside-binding site identified in HCoV-OC43 S is not conserved among CoVs which are also known to interact with sialoglycans to initiate host cell infection but are outside of the lineage A of β-CoVs, such as MERS-CoV (β-CoV, lineage C) or infectious bronchitis virus (IBV, δ-CoV) (Li et al., ”
- Human coronaviruses OC43 and HKU1 bind to 9-O-acetylated sialic acids via a conserved receptor-binding site in spike protein domain A (2019, methodology): “In nanoparticle sp-LBA experiments, BSM-bound nanoparticles were detected with StrepMAb-HRP via the C-terminally appended Strep-tag of the pA-LS proteins, as described previously (40).”
- Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein (2020, background): “MERS-CoV S, however, uses domain A to recognize non-acetylated sialoside attachment receptors (Li et al., 2017; Park et al., 2019), which likely promote subsequent binding of domain B (S) to the entry receptor, dipeptidyl-peptidase 4 (Lu et al.”
- SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor (2020, background): “This could comprise binding to cellular glycans, a function ascribed to the S1 domain of certain coronaviruses (Li et al., 2017; Park et al., 2019).”