Fig. 5: The binding footprints of the mAbs to the DD are highly conserved across betaCoVs. | Nature Communications

Fig. 5: The binding footprints of the mAbs to the DD are highly conserved across betaCoVs.

From: Structural stabilization of the intrinsically disordered SARS-CoV-2 N by binding to RNA sequences engineered from the viral genome fragment

Fig. 5

A Binding footprints for Fab NP3-B4 (grey) and Fab NP1-E9 (cyan) from antigenic sites DD-I and DD-II, respectively. Residues of the DD involved in interacting with the corresponding Fab are specified. B Multiple sequence alignment of the DD across variants of concerns of SARS-CoV-2 virus and other highly pathogenic members of the betaCoVs. The interacting residues described in (A) are highlighted. Strictly conserved residues are indicated by stars, conserved residues with strong similar properties are indicated by a colon, and conserved residues with weak similar properties are indicated by the period under the alignment according to ClustalW nomenclature.

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