Human (α2→6) and Avian (α2→3) Sialylated Receptors of Influenza A Virus Show Distinct Conformations and Dynamics in Solution Guilherme L. Sassaki Stefano Elli Timothy R. Rudd Eleonora Macchi Edwin A. Yates Annamaria Naggi Zachary Shriver Rahul Raman R. Sasisekharan Giangiacomo Torri Marco Guerrini 10.1021/bi400677n.s001 https://acs.figshare.com/articles/journal_contribution/Human_2_6_and_Avian_2_3_Sialylated_Receptors_of_Influenza_A_Virus_Show_Distinct_Conformations_and_Dynamics_in_Solution/2366392 Differential interactions between influenza A virus protein hemagglutinin (HA) and α2→3 (avian) or α2→6 (human) sialylated glycan receptors play an important role in governing host specificity and adaptation of the virus. Previous analysis of HA–glycan interactions with trisaccharides showed that, in addition to the terminal sialic acid linkage, the conformation and topology of the glycans, while they are bound to HA, are key factors in regulating these interactions. Here, the solution conformation and dynamics of two representative avian and human glycan pentasaccharide receptors [LSTa, Neu5Ac-α(2→3)-Gal-β(1→3)-GlcNAc-β(1→3)-Gal-β(1→4)-Glc; LSTc, (Neu5Ac-α(2→6)-Gal-β(1→4)-GlcNAc-β(1→3)-Gal-β(1→4)-Glc] have been explored using nuclear magnetic resonance and molecular dynamics simulation. Analyses demonstrate that, in solution, human and avian receptors sample distinct conformations, topologies, and dynamics. These unique features of avian and human receptors in solution could represent distinct molecular characteristics for recognition by HA, thereby providing the HA–glycan interaction specificity in influenza. 2013-10-15 00:00:00 influenza Virus Show Distinct Conformations glycan pentasaccharide receptors Neu 5Ac HA host specificity SolutionDifferential interactions solution conformation terminal sialic acid linkage virus protein hemagglutinin receptors sample dynamics simulation sialylated glycan receptors Previous analysis Neu 5Ac LSTc