Mechanism of Glycan Receptor Recognition and Specificity Switch for Avian, Swine, and Human Adapted Influenza Virus Hemagglutinins: A Molecular Dynamics Perspective
Identifieur interne : 001076 ( Main/Exploration ); précédent : 001075; suivant : 001077Mechanism of Glycan Receptor Recognition and Specificity Switch for Avian, Swine, and Human Adapted Influenza Virus Hemagglutinins: A Molecular Dynamics Perspective
Auteurs : E. Irene Newhouse ; Dong Xu ; Phineus R. L. Markwick ; Rommie E. Amaro ; Hsing C. Pao ; Kevin J. Wu ; Maqsudul Alam ; J. Andrew Mccammon ; Wilfred W. LiSource :
- Journal of the American Chemical Society [ 0002-7863 ] ; 2009.
Abstract
Hemagglutinins (HA’s) from duck, swine, and human influenza viruses have previously been shown to prefer avian and human glycan receptor analogues with distinct topological profiles, pentasaccharides LSTa (α-2,3 linkage) and LSTc (α-2,6 linkage), in comparative molecular dynamics studies. On the basis of detailed analyses of the dynamic motions of the receptor binding domains (RBDs) and interaction energy profiles with individual glycan residues, we have identified ∼30 residue positions in the RBD that present distinct profiles with the receptor analogues. Glycan binding constrained the conformational space sampling by the HA. Electrostatic steering appeared to play a key role in glycan binding specificity. The complex dynamic behaviors of the major SSE and trimeric interfaces with or without bound glycans suggested that networks of interactions might account for species specificity in these low affinity and high avidity (multivalent) interactions between different HA and glycans. Contact frequency, energetic decomposition, and H-bond analyses revealed species-specific differences in HA−glycan interaction profiles, not readily discernible from crystal structures alone. Interaction energy profiles indicated that mutation events at the set of residues such as 145, 156, 158, and 222 would favor human or avian receptor analogues, often through interactions with distal asialo-residues. These results correlate well with existing experimental evidence, and suggest new opportunities for simulation-based vaccine and drug development.
Url:
DOI: 10.1021/ja904052q
PubMed: 19891427
PubMed Central: 2782351
Affiliations:
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<p>Hemagglutinins (HA’s) from duck, swine, and human influenza viruses have previously been shown to prefer avian and human glycan receptor analogues with distinct topological profiles, pentasaccharides LSTa (α-2,3 linkage) and LSTc (α-2,6 linkage), in comparative molecular dynamics studies. On the basis of detailed analyses of the dynamic motions of the receptor binding domains (RBDs) and interaction energy profiles with individual glycan residues, we have identified ∼30 residue positions in the RBD that present distinct profiles with the receptor analogues. Glycan binding constrained the conformational space sampling by the HA. Electrostatic steering appeared to play a key role in glycan binding specificity. The complex dynamic behaviors of the major SSE and trimeric interfaces with or without bound glycans suggested that networks of interactions might account for species specificity in these low affinity and high avidity (multivalent) interactions between different HA and glycans. Contact frequency, energetic decomposition, and H-bond analyses revealed species-specific differences in HA−glycan interaction profiles, not readily discernible from crystal structures alone. Interaction energy profiles indicated that mutation events at the set of residues such as 145, 156, 158, and 222 would favor human or avian receptor analogues, often through interactions with distal asialo-residues. These results correlate well with existing experimental evidence, and suggest new opportunities for simulation-based vaccine and drug development.</p>
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<tree><noCountry><name sortKey="Alam, Maqsudul" sort="Alam, Maqsudul" uniqKey="Alam M" first="Maqsudul" last="Alam">Maqsudul Alam</name>
<name sortKey="Amaro, Rommie E" sort="Amaro, Rommie E" uniqKey="Amaro R" first="Rommie E." last="Amaro">Rommie E. Amaro</name>
<name sortKey="Li, Wilfred W" sort="Li, Wilfred W" uniqKey="Li W" first="Wilfred W." last="Li">Wilfred W. Li</name>
<name sortKey="Markwick, Phineus R L" sort="Markwick, Phineus R L" uniqKey="Markwick P" first="Phineus R. L." last="Markwick">Phineus R. L. Markwick</name>
<name sortKey="Mccammon, J Andrew" sort="Mccammon, J Andrew" uniqKey="Mccammon J" first="J. Andrew" last="Mccammon">J. Andrew Mccammon</name>
<name sortKey="Newhouse, E Irene" sort="Newhouse, E Irene" uniqKey="Newhouse E" first="E. Irene" last="Newhouse">E. Irene Newhouse</name>
<name sortKey="Pao, Hsing C" sort="Pao, Hsing C" uniqKey="Pao H" first="Hsing C." last="Pao">Hsing C. Pao</name>
<name sortKey="Wu, Kevin J" sort="Wu, Kevin J" uniqKey="Wu K" first="Kevin J." last="Wu">Kevin J. Wu</name>
<name sortKey="Xu, Dong" sort="Xu, Dong" uniqKey="Xu D" first="Dong" last="Xu">Dong Xu</name>
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