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. Author manuscript; available in PMC: 2017 Nov 21.
Published in final edited form as: Virology. 2015 Jan 22;477:18–31. doi: 10.1016/j.virol.2014.12.024

Fig 2.

Fig 2

A) Structural overlap of A(H3N2) HA monomers. HA monomers, HK68 (Grey), PtChalmers73 (Green) and Victoria11 (orange) are shown as tubes and the locations of glycosylation sites are highlighted with Asn side chain as red spheres. These sites if present on specific HAs are marked with squares colored according to the same HA coloring. B) RBS overlap of HK68 (Grey), PtChalmers73 (Green), Perth09 (magenta), Christchurch11 (cyan) and Victoria11 (orange). Previously published H3 HAs, Norway04 (blue) and Malaysia05 (yellow) (Lin et al., 2012) were also used in the alignment. C) SDS-PAGE of various recombinant H3 HA proteins indicates an increase in MW as the predicted number of glycosylation sites increase with time.