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
中科院分区:
文献类型:
--
作者:
Promkuntod N;van Eijndhoven RE;de Vrieze G;Gröne A;Verheije MH
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.
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影响因子:
5
作者:
Cavanagh D;Davis PJ;Mockett AP
通讯作者:
Mockett AP
影响因子:
3.7
作者:
KUNKEL, F;HERRLER, G
通讯作者:
HERRLER, G
影响因子:
5.4
作者:
de Haan, CAM;Stadler, K;Rottier, PJM
通讯作者:
Rottier, PJM
DOI:
10.1007/bf01242547
发表时间:
1973-01-01
期刊:
ARCHIV FUR DIE GESAMTE VIRUSFORSCHUNG
影响因子:
--
作者:
GEILHAUSEN, HE;LIGON, FB;LUKERT, PD
通讯作者:
LUKERT, PD
影响因子:
2.8
作者:
El Rahman, S. Abd;El-Kenawy, A. A.;Winter, C.
通讯作者:
Winter, C.