Mapping of the receptor-binding domain and amino acids critical for attachment in the spike protein of avian coronavirus infectious bronchitis virus.

Mapping of the receptor-binding domain and amino acids critical for attachment in the spike protein of avian coronavirus infectious bronchitis virus.
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DOI:
10.1016/j.virol.2013.09.018
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发表时间:
2014-01-05
期刊:
影响因子:
3.7
通讯作者:
Verheije MH
Verheije MH
中科院分区:
医学3区
文献类型:
--
作者:
Promkuntod N;van Eijndhoven RE;de Vrieze G;Gröne A;Verheije MH

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禽冠状病毒传染性支气管炎病毒(IBV)的感染是由刺突糖蛋白S与鸡宿主细胞上的唾液酸结合引起的。在这项研究中,我们鉴定了IBV原型株M41刺突的受体结合域(RBD)。通过分析重组表达的嵌合和截断的刺突蛋白与鸡组织的结合能力,我们证明了刺突n端253个氨基酸以α-2,3-唾液酸依赖的方式与鸡呼吸道结合是必需的和充分的。M41穗附着的关键氨基酸存在于n端残基19-69中,这与S1基因的高变区重叠。我们的结果可能有助于了解IBV S1基因型之间的差异以及IBV在鸡中的最终发病机制。IBV M41刺突的RBD映射到n端253个残基。NTD是α-2,3-唾液酸结合的必要条件和充分条件。M41穗附着的关键残基包括N38、H43、P63和T69。
The infection of the avian coronavirus infectious bronchitis virus (IBV) is initiated by the binding of the spike glycoprotein S to sialic acids on the chicken host cell. In this study we identified the receptor-binding domain (RBD) of the spike of the prototype IBV strain M41. By analyzing the ability of recombinantly expressed chimeric and truncated spike proteins to bind to chicken tissues, we demonstrate that the N-terminal 253 amino acids of the spike are both required and sufficient for binding to chicken respiratory tract in an α-2,3-sialic acid-dependent manner. Critical amino acids for attachment of M41 spike are present within the N-terminal residues 19–69, which overlap with a hypervariable region in the S1 gene. Our results may help to understand the differences between IBV S1 genotypes and the ultimate pathogenesis of IBV in chickens. The RBD of the IBV M41 spike maps to the N-terminal 253 residues. The NTD is both required and sufficient for α-2,3-sialic acid binding. Critical residues for attachment of the M41 spike include N38, H43, P63 and T69.
DOI: 10.1016/0168-1702(88)90039-1
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