tetano
Editor, Senior Moderator
Biochemistry. 2013 Sep 9. [Epub ahead of print]
Human (α2→6) and avian (α2→3) sialylated receptors of influenza A virus show distinct conformations and dynamics in solution.
Sassaki GL, Elli S, Rudd TR, Macchi E, Yates EA, Naggi A, Shriver Z, Raman R, Sasisekharan R, Torri G, Guerrini M.
Abstract
Differential interactions between influenza A virus protein haemagglutinin (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 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 and LSTc: (Neu5Ac-α(2→6)-Gal-β(1→4)-GlcNAc-β(1→3)-Gal-β(1→4)-Glc) have been explored using NMR 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.
PMID:
24015903
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24015903
Human (α2→6) and avian (α2→3) sialylated receptors of influenza A virus show distinct conformations and dynamics in solution.
Sassaki GL, Elli S, Rudd TR, Macchi E, Yates EA, Naggi A, Shriver Z, Raman R, Sasisekharan R, Torri G, Guerrini M.
Abstract
Differential interactions between influenza A virus protein haemagglutinin (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 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 and LSTc: (Neu5Ac-α(2→6)-Gal-β(1→4)-GlcNAc-β(1→3)-Gal-β(1→4)-Glc) have been explored using NMR 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.
PMID:
24015903
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/24015903