Sendai virus intra-host population dynamics and host immunocompetence influence viral virulence during in vivo passage

Peña, José; Chen-Harris, Haiyin; Allen, Jonathan E.; Hwang, Mona; Elsheikh, Maher; Mabery, Shalini; Bielefeldt-Ohmann, Helle; Zemla, Adam T.; Bowen, Richard A.; Borucki, Monica K.

Constructed structural models allowed us to characterize location of identified mutation points (A454V, E461K, K525Q) within functional complex of HN protein of SeV as well as among HN proteins from other related viruses. Results showed that these positions are located on the protein surface on the top of the receptor-binding domain next to sialic acid-binding regions and don't overlap with interfaces of the tetramer formation (Fig. 8) . Additionally, the mutation positions are located in the regions identified as variable in sequence according to calculated multiple sequence alignments between HN proteins of paramyxovirus sequences from UniProt. Results from calculated structural alignments between structural models of HN proteins currently available in PDB suggest that two mutation positions (454, 461) are located in the regions conserved in structure (conserved backbone conformation), while 525 is located in the structurally variable region.