PDF(Pubmed)
Abstract：
The hemagglutinin-esterase-fusion (HEF) protein binds 9-O-acetylated sialic acids-containing glycans on the cell surface and drives influenza D virus (IDV) entry. The HEF is a primary determinant of the exceptional thermal and acid stability observed in IDV infection biology. Here, we expressed and purified the receptor binding domain (RBD) of the IDV HEF protein in Escherichia coli and characterized its receptor binding and antigenic properties. The data from these experiments indicate that (i) the RBD can bind with specificity to turkey red blood cells (RBC), and its binding can be specifically inhibited by IDV antibody; (ii) the RBD efficiently binds to the cell surface of MDCK cells expressing the receptor of IDV; and (iii) anti-RBD antibodies are capable of blocking RBD attachment to MDCK cells as well as of inhibiting the virus from agglutinating RBCs. These observations support the utility of this RBD in future receptor and entry studies of IDV.
摘要：
血凝素-酯酶-融合(HEF)蛋白结合细胞表面上的含9-O-乙酰化唾液酸的聚糖并驱动D型流感病毒(IDV)进入。HEF是在IDV感染生物学中观察到的异常的热和酸稳定性的主要决定因素。这里,我们在大肠杆菌中表达并纯化了IDVHEF蛋白的受体结合域（RBD），并表征了其受体结合和抗原特性。来自这些实验的数据表明（i）RBD可以与火鸡红细胞（RBC）特异性结合，并且其结合可被IDV抗体特异性抑制;(ii)RBD有效地结合表达IDV受体的MDCK细胞的细胞表面;和(iii)抗RBD抗体能够阻断RBD与MDCK细胞的附着以及抑制病毒凝集RBC。这些观察结果支持该RBD在未来的IDV受体和入门研究中的实用性。
