CLC number: S855.3
On-line Access: 2024-08-27
Received: 2023-10-17
Revision Accepted: 2024-05-08
Crosschecked: 2017-07-18
Cited: 1
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Li-bao Ma, Bao-yang Xu, Min Huang, Lv-hui Sun, Qing Yang, Yi-jie Chen, Ya-lin Yin, Qi-gai He, Hui Sun. Adjuvant effects mediated by the carbohydrate recognition domain of Agrocybe aegerita lectin interacting with avian influenza H9N2 viral surface glycosylated proteins[J]. Journal of Zhejiang University Science B, 2017, 18(8): 653-661.
@article{title="Adjuvant effects mediated by the carbohydrate recognition domain of Agrocybe aegerita lectin interacting with avian influenza H9N2 viral surface glycosylated proteins",
author="Li-bao Ma, Bao-yang Xu, Min Huang, Lv-hui Sun, Qing Yang, Yi-jie Chen, Ya-lin Yin, Qi-gai He, Hui Sun",
journal="Journal of Zhejiang University Science B",
volume="18",
number="8",
pages="653-661",
year="2017",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.B1600106"
}
%0 Journal Article
%T Adjuvant effects mediated by the carbohydrate recognition domain of Agrocybe aegerita lectin interacting with avian influenza H9N2 viral surface glycosylated proteins
%A Li-bao Ma
%A Bao-yang Xu
%A Min Huang
%A Lv-hui Sun
%A Qing Yang
%A Yi-jie Chen
%A Ya-lin Yin
%A Qi-gai He
%A Hui Sun
%J Journal of Zhejiang University SCIENCE B
%V 18
%N 8
%P 653-661
%@ 1673-1581
%D 2017
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B1600106
TY - JOUR
T1 - Adjuvant effects mediated by the carbohydrate recognition domain of Agrocybe aegerita lectin interacting with avian influenza H9N2 viral surface glycosylated proteins
A1 - Li-bao Ma
A1 - Bao-yang Xu
A1 - Min Huang
A1 - Lv-hui Sun
A1 - Qing Yang
A1 - Yi-jie Chen
A1 - Ya-lin Yin
A1 - Qi-gai He
A1 - Hui Sun
J0 - Journal of Zhejiang University Science B
VL - 18
IS - 8
SP - 653
EP - 661
%@ 1673-1581
Y1 - 2017
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B1600106
Abstract: Objective: To evaluate the potential adjuvant effect of Agrocybe aegerita lectin (AAL), which was isolated from mushroom, against a virulent H9N2 strain in vivo and in vitro. Methods: In trial 1, 50 BALB/c male mice (8 weeks old) were divided into five groups (n=10 each group) which received a subcutaneous injection of inactivated H9N2 (control), inactivated H9N2+0.2% (w/w) alum, inactivated H9N2+0.5 mg recombinant AAL/kg body weight (BW), inactivated H9N2+1.0 mg AAL/kg BW, and inactivated H9N2+2.5 mg AAL/kg BW, respectively, four times at 7-d intervals. In trial 2, 30 BALB/c male mice (8 weeks old) were divided into three groups (n=10 each group) which received a subcutaneous injection of inactivated H9N2 (control), inactivated H9N2+2.5 mg recombinant wild-type AAL (AAL-wt)/kg BW, and inactivated H9N2+2.5 mg carbohydrate recognition domain (CRD) mutant AAL (AAL-mutR63H)/kg BW, respectively, four times at 7-d intervals. Seven days after the final immunization, serum samples were collected from each group for analysis. Hemagglutination assay, immunogold electron microscope, lectin blotting, and co-immunoprecipitation were used to study the interaction between AAL and H9N2 in vitro. Results: IgG, IgG1, and IgG2a antibody levels were significantly increased in the sera of mice co-immunized with inactivated H9N2 and AAL when compared to mice immunized with inactivated H9N2 alone. No significant increase of the IgG antibody level was detected in the sera of the mice co-immunized with inactivated H9N2 and AAL-mutR63H. Moreover, AAL-wt, but not mutant AAL-mutR63H, adhered to the surface of H9N2 virus. The interaction between AAL and the H9N2 virus was further demonstrated to be associated with the CRD of AAL binding to the surface glycosylated proteins, hemagglutinin and neuraminidase. Conclusions: Our findings indicated that AAL could be a safe and effective adjuvant capable of boosting humoral immunity against H9N2 viruses in mice through its interaction with the viral surface glycosylated proteins, hemagglutinin and neuraminidase.
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