L-Ficolin Binds to the Glycoproteins Hemagglutinin and Neuraminidase and Inhibits Influenza A Virus Infection Both in vitro and in vivo

PAN Qin; WANG Feng; CHEN Hadan; HOU Wei; Victor Tunje Jeza; ZHAO Yinglan; ZHANG Xiao-Lian

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L-Ficolin Binds to the Glycoproteins Hemagglutinin and Neuraminidase and Inhibits Influenza A Virus Infection Both in vitro and in vivo

PAN Qin 1,WANG Feng 2,CHEN Hadan 2,HOU Wei 3,Victor Tunje Jeza 2,ZHAO Yinglan 4,ZHANG Xiao-Lian 5 *

1.Department of Immunology, Wuhan University School of Medicine, Wuhan 430071

2.Department of Immunology, Wuhan University School of Medicine

3.Institute of Virology, Wuhan University School of Medicine

4.Department of Immunology, Wuhan University School of Medicine,Wuhan , PR China

5.State Key Laboratory of Virology, Department of Immunology and Hubei Province, Key Laboratory of Allergy,and Immune-Related Diseases, and Institute of Virology, Wuhan University School of Medicine, and State Key Laboratory of Virology, Wuhan University College of Life Sciences, Wuhan , PR China

*Correspondence author

#Submitted by

Subject:

Funding: the Program for Changjiang Scholars and Innovative Research Team at University, the 211 program （No.No. 303-581045）, The National Outstanding Youth Foundation of China （No.No. 81025008）, the 973 Program of China （No.No. 2009CB522507）, the National Special Fund of China for Important Infectious Disease （No.No. 2012ZX-10003-002）, the National Natural Science Foundation of China （No.No. 30921001 and 30800038）

Opened online:28 March 2013

Accepted by: none

Citation: PAN Qin,WANG Feng,CHEN Hadan.L-Ficolin Binds to the Glycoproteins Hemagglutinin and Neuraminidase and Inhibits Influenza A Virus Infection Both in vitro and in vivo[OL]. [28 March 2013] http://en.paper.edu.cn/en_releasepaper/content/4531323

L-ficolin, one of the complement lectins found in human serum, is a novel pattern recognition molecule that can specifically bind to microbial carbohydrates, thereby activating the lectin complement pathway and mounting a protective innate immune response. However, little is known about the role of L-ficolin during viral infections in vivo. In the present study, we used a mouse model of influenza A virus infection to demonstrate that the administration of exogenous L-ficolin or ficolin A (FCNA - an L-ficolin-like molecule in the mouse) is protective against the virus. Furthermore, FCNA-null mice have a greatly increased susceptibility to infection with the influenza A virus. Moreover, we found recombinant human L-ficolin inhibited influenza A virus entry into Madin-Darby canine kidney cells. More importantly, L-ficolin can recognize and bind hemagglutinin (HA) and neuraminidase (NA) glycoproteins and different subtypes of influenza A virus,and these interactions can be competitively inhibited by N-acetyl-D-glucosamine. In addition, the binding of L-ficolin and FCNA may lead to the activation of the lectin complem e nt p athw ay. To o ur k n ow l e d g e, this is th e f ir s t re p o r t d e m onstrating that L-ficolin can bl ock influenza virus infections both in vitro and in vivo using FCNA-knockout mice, possibly by interacting with the carbohydrates of HA and NA. Therefore, these data may provide new immunotherapeutic strategies based on the innate immune molecule L-ficolin against the influenza A virus.

Keywords:Complement; L-ficolin; Influenza infection; Hemagglutinin; Neuraminidase; Glycoprotein

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