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