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流感 A 病毒的人（α2→6）和禽类（α2→3）唾液酸受体在溶液中呈现出不同的构象和动态。

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

机构信息

Istituto di Ricerche Chimiche e Biochimiche "G. Ronzoni", Via Giuseppe Colombo, 81, Milano, 20133 Italy.

Department of Structural and Chemical Biology, Biosciences Building, University of Liverpool, Crown Street, Liverpool L69 7ZB, U.K.

出版信息

Biochemistry. 2013 Oct 15;52(41):7217-7230. doi: 10.1021/bi400677n. Epub 2013 Sep 27.

DOI:10.1021/bi400677n
PMID:24015903
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4008123/
Abstract

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.

摘要

流感 A 病毒蛋白血凝素 (HA) 与 α2→3（禽）或 α2→6（人）唾液酸化聚糖受体的差异相互作用在控制病毒的宿主特异性和适应性方面发挥着重要作用。之前对 HA-聚糖相互作用的三糖分析表明，除了末端唾液酸键合之外，聚糖的构象和拓扑结构，在与 HA 结合时，是调节这些相互作用的关键因素。在这里，使用核磁共振和分子动力学模拟研究了两种代表性的禽和人聚糖五糖受体 [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] 的溶液构象和动力学。分析表明，在溶液中，人和禽受体采用不同的构象、拓扑结构和动力学。这些溶液中禽和人受体的独特特征可能代表了 HA 识别的独特分子特征，从而提供了流感中 HA-聚糖相互作用的特异性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b61/4008123/29d769c6d914/nihms-528489-f0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b61/4008123/394881a003b0/nihms-528489-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b61/4008123/0fb53a00fd8c/nihms-528489-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b61/4008123/b26f2cefd3c7/nihms-528489-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b61/4008123/f50ce911058a/nihms-528489-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b61/4008123/4758149d5975/nihms-528489-f0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b61/4008123/29d769c6d914/nihms-528489-f0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b61/4008123/394881a003b0/nihms-528489-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b61/4008123/0fb53a00fd8c/nihms-528489-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b61/4008123/b26f2cefd3c7/nihms-528489-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b61/4008123/f50ce911058a/nihms-528489-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b61/4008123/4758149d5975/nihms-528489-f0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1b61/4008123/29d769c6d914/nihms-528489-f0007.jpg

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