tetano
Editor, Senior Moderator
J Innate Immun. 2012 Mar 1. [Epub ahead of print]
L-Ficolin Binds to the Glycoproteins Hemagglutinin and Neuraminidase and Inhibits Influenza A Virus Infection Both in vitro and in vivo.
Pan Q, Chen H, Wang F, Jeza VT, Hou W, Zhao Y, Xiang T, Zhu Y, Endo Y, Fujita T, Zhang XL.
Source
State Key Laboratory of Virology, Department of Immunology and Hubei Province, Key Laboratory of Allergy and Immune-Related Diseases, Wuhan University School of Medicine, Wuhan, PR China.
Abstract
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 complement pathway. To our knowledge, this is the first report demonstrating that L-ficolin can block 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.
Copyright ? 2012 S. Karger AG, Basel.
PMID:
22399010
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22399010
L-Ficolin Binds to the Glycoproteins Hemagglutinin and Neuraminidase and Inhibits Influenza A Virus Infection Both in vitro and in vivo.
Pan Q, Chen H, Wang F, Jeza VT, Hou W, Zhao Y, Xiang T, Zhu Y, Endo Y, Fujita T, Zhang XL.
Source
State Key Laboratory of Virology, Department of Immunology and Hubei Province, Key Laboratory of Allergy and Immune-Related Diseases, Wuhan University School of Medicine, Wuhan, PR China.
Abstract
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 complement pathway. To our knowledge, this is the first report demonstrating that L-ficolin can block 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.
Copyright ? 2012 S. Karger AG, Basel.
PMID:
22399010
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/22399010