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Your search keyword '"Rey, Félix A."' showing total 9 results
Start Over Author "Rey, Félix A." Journal journal of virology
9 results on '"Rey, Félix A."'

3. A Druggable Pocket at the Nucleocapsid/Phosphoprotein Interaction Site of Human Respiratory Syncytial Virus

Author

Ouizougun-Oubari, Mohamed, primary, Pereira, Nelson, additional, Tarus, Bogdan, additional, Galloux, Marie, additional, Lassoued, Safa, additional, Fix, Jenna, additional, Tortorici, M. Alejandra, additional, Hoos, Sylviane, additional, Baron, Bruno, additional, England, Patrick, additional, Desmaële, Didier, additional, Couvreur, Patrick, additional, Bontems, François, additional, Rey, Félix A., additional, Eléouët, Jean-François, additional, Sizun, Christina, additional, Slama-Schwok, Anny, additional, and Duquerroy, Stéphane, additional

Published
2015
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9. Glycan Shield and Fusion Activation of a Deltacoronavirus Spike Glycoprotein Fine-Tuned for Enteric Infections.

Author

Xiaoli Xiong, Tortorici, M. Alejandra, Snijder, Joost, Yoshioka, Craig, Walls, Alexandra C., Wentao Li, McGuire, Andrew T., Rey, Félix A., Bosch, Berend-Jan, and Veesler, David

Subjects
*CORONAVIRUS diseases, *GLYCOPROTEINS, *INTESTINAL infections, *GLYCANS, *SARS disease
Abstract

Coronaviruses recently emerged as major human pathogens causing outbreaks of severe acute respiratory syndrome and Middle East respiratory syndrome. They utilize the spike (S) glycoprotein anchored in the viral envelope to mediate host attachment and fusion of the viral and cellular membranes to initiate infection. The S protein is a major determinant of the zoonotic potential of coronaviruses and is also the main target of the host humoral immune response. We report here the 3.5-Å-resolution cryoelectron microscopy structure of the S glycoprotein trimer from the pathogenic porcine deltacoronavirus (PDCoV), which belongs to the recently identified Deltacoronavirus genus. Structural and glycoproteomics data indicate that the glycans of PDCoV S are topologically conserved compared with the human respiratory coronavirus NL63 S, resulting in similar surface areas being shielded from neutralizing antibodies and implying that both viruses are under comparable immune pressure in their respective hosts. The structure further reveals a shortened S2= activation loop, containing a reduced number of basic amino acids, which participates in rendering the spike largely protease resistant. This property distinguishes PDCoV S from recently characterized betacoronavirus S proteins and suggests that the S protein of enterotropic PDCoV has evolved to tolerate the protease-rich environment of the small intestine and to fine-tune its fusion activation to avoid premature triggering and reduction of infectivity. [ABSTRACT FROM AUTHOR]

Published
2018
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