Two Mutations Were Critical for Bat-to-Human Transmission of Middle East Respiratory Syndrome Coronavirus
By Yang Yang, Chang Liu, L. Du, Shibo Jiang, Zhènglì Shí, Ralph S. Baric, Fang Li. 2015
123 citations recorded by the source corpus.
Subfields: Animal Science and Zoology, Infectious Diseases
How researchers see this paper
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
- Elicitation of Potent Neutralizing Antibody Responses by Designed Protein Nanoparticle Vaccines for SARS-CoV-2 (2020, neutral): “, 1998) and for modulating accessibility to host proteases and neutralizing Abs (Walls et al., 2016b; 2017; 2019; Watanabe et al., 2020; Xiong et al., 2018; Yang et al., 2015).”
- Structure, Function, and Evolution of Coronavirus Spike Proteins (2016, background): “Interestingly, despite recognizing the same receptor DPP4, MERS-CoV and HKU4 spikes differ in their activities to mediate virus entry: HKU4 spike mediates virus entry into bat cells but not human cells, whereas MERS-CoV spike mediates virus entry into both bat and human cells (152).”
- Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy (2016, methodology): “On the basis of these findings, a final search was performed with COMET75 on the same data with the following list of variable modifications of asparagine residues: +HexNAc(2)Hex(3), +HexNAc(2)Hex(3)dHex(1), +HexNAc(2)Hex(3)dHex(2), +HexNAc(2)Hex(4), +HexNAc(2)Hex(5), +HexNAc(2)Hex(6), +HexNAc(2)Hex”
- Structural insights into coronavirus entry (2019, background): “Liu, 2009) and/or substitutions of residues at the S1/S2 or S2’ cleavage sites (Belouzard et al., 2009; Li et al., 2015; Millet and Whittaker, 2014; Wicht et al., 2014; Yang et al., 2015).”
- Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion (2020, unknown): “Studies of the S glycoproteins of MERS-CoV and the bat-specific HKU4 coronavirus suggested that glycans also impact zoonosis by modulating cleavage-site accessibility to proteases for membrane-fusion activation (Yang et al., 2015).”
- Glycan Shield and Fusion Activation of a Deltacoronavirus Spike Glycoprotein Fine-Tuned for Enteric Infections (2017, methodology): “infecting HKU4-CoV S protein to mediate entry into human cells(14).”
- SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor (2020, background): “Notably, the cleavage site sequence can determine the zoonotic potential of coronaviruses (Menachery et al., 2020; Yang et al., 2014 Yang et al., , 2015 , and a multibasic cleavage site was not present in RaTG13, the coronavirus most closely related to SARS-CoV-2.”
- Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein (2020, background): “Subsequent work suggested that a glycan present near the S1/S2 boundary accounted for the lack of proteolytic priming of HKU4 S and that its removal enhanced pseudovirus entry in human cells (Yang et al., 2015b).”