Human (α2→6) and avian (α2→3) sialylated receptors of influenza A virus show distinct conformations and dynamics in solution

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, i...

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Veröffentlicht in:	Biochemistry (Easton) Jg. 52; H. 41; S. 7217
Hauptverfasser:	Sassaki, Guilherme L, Elli, Stefano, Rudd, Timothy R, Macchi, Eleonora, Yates, Edwin A, Naggi, Annamaria, Shriver, Zachary, Raman, Rahul, Sasisekharan, R, Torri, Giangiacomo, Guerrini, Marco
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	United States 15.10.2013
Schlagworte:	Animals Birds Hemagglutinin Glycoproteins, Influenza Virus - genetics Hemagglutinin Glycoproteins, Influenza Virus - metabolism Humans Influenza A virus - genetics Influenza A virus - metabolism Influenza in Birds - metabolism Influenza in Birds - virology Influenza, Human - metabolism Influenza, Human - virology Models, Molecular N-Acetylneuraminic Acid - metabolism Polysaccharides - chemistry Polysaccharides - metabolism Receptors, Virus - chemistry Receptors, Virus - metabolism
ISSN:	1520-4995, 1520-4995
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Zusammenfassung:	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.
Bibliographie:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23
ISSN:	1520-4995 1520-4995
DOI:	10.1021/bi400677n