Specifically Binding of L-ficolin to N-glycans of HCV Envelope Glycoproteins E1 and E2 Leads to Complement Activation  

作　　者：Jun Liu Mohammed A.M. Ali Yinghua Shi Yinglan Zhao Fenglin Luo Jin Yu Tian Xiang Jie Tang Dongqing Li Quan Hu Wenzhe Ho Xiaolian Zhang 

机构地区：[1]The 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 430071, China [2]Center for Disease Control and Prevention of Wuhan, Wuhan 430071, China [3]Division of Allergy-Immunology, the Children＇s Hospital of Philadelphia, Department of Pediatrics, University of Pennsylvania School of Medicine, Philadelphia, PA, USA [4]Central Hospital of Enshi Prefecture, Hubei 445000, China [5]These two authors contribute equally to this work as first authors [6]Department of Immunology, Wuhan University School of Medicine, 165 Donghu Road, Wuhan 430071, China

出　　处：《Cellular & Molecular Immunology》2009年第4期235-244,共10页中国免疫学杂志（英文版）

基　　金：Acknowledgments This work was supported by grants to X.-L. Zhang from the National Natural Science Foundation of China （30870122, 30670098 and 20532020）, 973 Program of China 2006CB 504300 and 2009CB522507, National Grand Program on Key Infectious Disease （2008ZX10003-005）, Hubei Province Science Technology Department （2006ABD007, 2007ABC 010） and Hubei Ministry of Public Health of （JX1B074）.

摘　　要：L-ficolin, one of lectin families, is a recently identified complement factor that initiates lectin pathway of complement. Little is known about its role in viral hepatitis. In the present study, we found that L-ficolin in serum from 103 patients with hepatitis C virus （HCV）, were significantly higher than that in 150 healthy controls. We further found that L-ficolin expressions were significantly increased in vitro study by HCV JFH-1 infected human hepatocyte cell line Huh7.5.1. Investigation of the mechanisms of the L-ficolin action on HCV demonstrated that L-ficolin protein could recognize and bind to envelope glycoproteins E1 and E2 of HCV, activating the lectin complement pathway-mediated cytolytic activity in HCV-infected hepatocyte. This interaction between L-ficolin and HCV E1 and E2 glycoproteins was attributed to the N-glycans of E1 and E2. These findings provide new insights into the biological functions of L-ficolin in clinically important hepatic viral diseases.L-ficolin, one of lectin families, is a recently identified complement factor that initiates lectin pathway of complement. Little is known about its role in viral hepatitis. In the present study, we found that L-ficolin in serum from 103 patients with hepatitis C virus （HCV）, were significantly higher than that in 150 healthy controls. We further found that L-ficolin expressions were significantly increased in vitro study by HCV JFH-1 infected human hepatocyte cell line Huh7.5.1. Investigation of the mechanisms of the L-ficolin action on HCV demonstrated that L-ficolin protein could recognize and bind to envelope glycoproteins E1 and E2 of HCV, activating the lectin complement pathway-mediated cytolytic activity in HCV-infected hepatocyte. This interaction between L-ficolin and HCV E1 and E2 glycoproteins was attributed to the N-glycans of E1 and E2. These findings provide new insights into the biological functions of L-ficolin in clinically important hepatic viral diseases.

关 键 词：L-FICOLIN hepatitis C virus envelope glycoproteins COMPLEMENT viral hepatitis 

分 类 号：S852.65[农业科学—基础兽医学] Q78[农业科学—兽医学]