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. 2010 Jul 22;5(7):e11694. doi: 10.1371/journal.pone.0011694

Figure 2. Surface hydrophobicity and antigenic structure of protein HA63–286-RBD.

Figure 2

(A) Hydrophobic (red) and hydrophilic regions (blue) at the surface of protein HA63–286-RBD calculated by simulations; (B) The hydrophobicity map of the HA1 subunit expressed by Chiu et al (10) is presented for comparison. (C) Simulation results show that protein HA63–286-RBD preserves the conformational antigenic sites Sa, Sb, Ca1, Ca2, Cb computationally predicted by Igarashi et al. [22] for the HA of the influenza A H1N1/CA2009 virus. Three dimensional structures were obtained using Swiss-model. The full length HA of the Influenza A H1N1/1918 virus [23] was taken as a template for the estimation of the most probable structure of protein HA63–286-RBD. Visualization and highlighting of immunogenic sites was done using UCSF-Chimera. The structure of the antigenic epitopes of the HA of the influenza A H1N1/CA2009 virus was taken from Igarashi et al. [22]. They are also consistent with structural data published recently by Xu et al [41].