Selected article for: "acid substitution and receptor binding"
Author: Chu, Daniel K. W.; Hui, Kenrie P. Y.; Perera, Ranawaka A. P. M.; Miguel, Eve; Niemeyer, Daniela; Zhao, Jincun; Channappanavar, Rudragouda; Dudas, Gytis; Oladipo, Jamiu O.; Traoré, Amadou; Fassi-Fihri, Ouafaa; Ali, Abraham; Demissié, Getnet F.; Muth, Doreen; Chan, Michael C. W.; Nicholls, John M.; Meyerholz, David K.; Kuranga, Sulyman A.; Mamo, Gezahegne; Zhou, Ziqi; So, Ray T. Y.; Hemida, Maged G.; Webby, Richard J.; Roger, Francois; Rambaut, Andrew; Poon, Leo L. M.; Perlman, Stanley; Drosten, Christian; Chevalier, Veronique; Peiris, Malik
Title: MERS coronaviruses from camels in Africa exhibit region-dependent genetic diversity
  • Document date: 2018_3_20
    • ID: riitjx0f_9
    Snippet: The amino acid residues of AH13, Nig1657, and BF785 that differ from the prototype clade A MERS-CoV strain EMC occur throughout the virus genome (Dataset S2). The amino acid sequence of the Egyptian virus NRCE-HKU270, an East African virus most closely related to the West African clade C1 viruses, is also included for comparison. The amino acid residues in the receptor-binding domain of the spike proteins of the BF785 had amino acid substitution .....
    Document: The amino acid residues of AH13, Nig1657, and BF785 that differ from the prototype clade A MERS-CoV strain EMC occur throughout the virus genome (Dataset S2). The amino acid sequence of the Egyptian virus NRCE-HKU270, an East African virus most closely related to the West African clade C1 viruses, is also included for comparison. The amino acid residues in the receptor-binding domain of the spike proteins of the BF785 had amino acid substitution T424I, while Nig1657 had amino acid substitutions L495F and L588F. None of these amino acid substitutions was at the receptor-interacting interface of the spike protein and thus likely did not affect the affinity of the protein for the host receptor, although L495F is close to the interacting interface.

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