tetano
Editor, Senior Moderator
Angew Chem Int Ed Engl. 2018 Sep 20. doi: 10.1002/anie.201807162. [Epub ahead of print]
[h=1]New NMR Avenues to Characterize the Interactions of Extended N-glycans with Proteins: The Influenza Hemagglutinin Case.[/h] Jimenez-Barbero J[SUP]1[/SUP], Fernandez de Toro B[SUP]2[/SUP], Peng W[SUP]3[/SUP], Thompson AJ[SUP]3[/SUP], Dom?nguez G[SUP]4[/SUP], Ca?ada FJ[SUP]4[/SUP], P?rez-Castells J[SUP]4[/SUP], Paulson JC[SUP]3[/SUP], Canales A[SUP]4[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Long chain multiantenna N-glycans are extremely complex molecules from the structural perspective. Their inherent flexibility and the presence of repetitions of monosaccharide units in similar chemical environments hamper their full characterization by X-ray diffraction or standard NMR methodologies. Therefore, the exploration of their interaction properties in solution, especially with regard to branch specificity and molecular recognition features, remains a challenge. Herein, we report the successful conformational and interaction analysis of a sialylated tetradecasaccharide N-glycan presenting two LacNAc repetitions at each arm. This glycan has been identified as the receptor of the hemagglutinin protein of pathogenic influenza viruses. In order to accomplish this study, a N-glycan conjugated with a lanthanide binding tag has been synthesized, enabling analysis of the system by paramagnetic NMR. Under paramagnetic conditions, the NMR signals of each sugar unit in the glycan have been determined. In addition, a detailed binding epitope of the tetradecasaccharide N-glycan in the presence of HK/68 hemagglutinin is described.
[h=4]KEYWORDS:[/h] GLYCANS; HEMAGLUTINNIN; NMR; conformation; molecular recognition
PMID: 30238596 DOI: 10.1002/anie.201807162
[h=1]New NMR Avenues to Characterize the Interactions of Extended N-glycans with Proteins: The Influenza Hemagglutinin Case.[/h] Jimenez-Barbero J[SUP]1[/SUP], Fernandez de Toro B[SUP]2[/SUP], Peng W[SUP]3[/SUP], Thompson AJ[SUP]3[/SUP], Dom?nguez G[SUP]4[/SUP], Ca?ada FJ[SUP]4[/SUP], P?rez-Castells J[SUP]4[/SUP], Paulson JC[SUP]3[/SUP], Canales A[SUP]4[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] Long chain multiantenna N-glycans are extremely complex molecules from the structural perspective. Their inherent flexibility and the presence of repetitions of monosaccharide units in similar chemical environments hamper their full characterization by X-ray diffraction or standard NMR methodologies. Therefore, the exploration of their interaction properties in solution, especially with regard to branch specificity and molecular recognition features, remains a challenge. Herein, we report the successful conformational and interaction analysis of a sialylated tetradecasaccharide N-glycan presenting two LacNAc repetitions at each arm. This glycan has been identified as the receptor of the hemagglutinin protein of pathogenic influenza viruses. In order to accomplish this study, a N-glycan conjugated with a lanthanide binding tag has been synthesized, enabling analysis of the system by paramagnetic NMR. Under paramagnetic conditions, the NMR signals of each sugar unit in the glycan have been determined. In addition, a detailed binding epitope of the tetradecasaccharide N-glycan in the presence of HK/68 hemagglutinin is described.
[h=4]KEYWORDS:[/h] GLYCANS; HEMAGLUTINNIN; NMR; conformation; molecular recognition
PMID: 30238596 DOI: 10.1002/anie.201807162