Document Detail


Recombinant chimeric lectins consisting of mannose-binding lectin and L-ficolin are potent inhibitors of influenza A virus compared with mannose-binding lectin.
MedLine Citation:
PMID:  21035429     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
MBL structurally contains a type II-like collagenous domain and a carbohydrate recognition domain (CRD). We have recently generated three novel recombinant chimeric lectins (RCL), in which varying length of collagenous domain of mannose-binding lectin (MBL) is replaced with that of L-ficolin (L-FCN). CRD of MBL is used for target recognition because it has a broad spectrum in pathogen recognition compared with L-FCN. Results of our study demonstrate that these RCLs are potent inhibitors of influenza A virus (IAV). RCLs, against IAV, show dose-dependent activation of the lectin complement pathway, which is significantly higher than that of recombinant human MBL (rMBL). This activity is observed even without MBL-associated serine proteases (MASPs, provided by MBL deficient mouse sera), which have been thought to mediate complement activation. These observations suggest that RCLs are more efficient in associating with MASP-2, which predominantly mediates the activity. Yet, additional serum further increases the activity while RCL-mediated coagulation-like enzyme activities are diminished compared with rMBL, suggesting reduced association with MASP-1, which has been shown to mediate coagulation-like activity. These data suggest that RCLs may interfere less with host coagulation, which is advantageous to be a therapeutic drug. Importantly, these RCLs have surpassed rMBL for anti-viral activities, such as viral aggregation, reduction of viral hemagglutination (HA) and inhibition of virus-mediated HA and neuraminidase (NA) activities. These results are encouraging that novel RCLs could be used as anti-IAV agents with less side effect and that RCLs would be suitable candidates in developing a new anti-IAV therapy.
Authors:
Wei-Chuan Chang; Kevan L Hartshorn; Mitchell R White; Patience Moyo; Ian C Michelow; Henry Koziel; Bernard T Kinane; Emmett V Schmidt; Teizo Fujita; Kazue Takahashi
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.     Date:  2010-10-28
Journal Detail:
Title:  Biochemical pharmacology     Volume:  81     ISSN:  1873-2968     ISO Abbreviation:  Biochem. Pharmacol.     Publication Date:  2011 Feb 
Date Detail:
Created Date:  2010-12-27     Completed Date:  2011-01-21     Revised Date:  2013-01-16    
Medline Journal Info:
Nlm Unique ID:  0101032     Medline TA:  Biochem Pharmacol     Country:  England    
Other Details:
Languages:  eng     Pagination:  388-95     Citation Subset:  IM    
Copyright Information:
Copyright © 2010 Elsevier Inc. All rights reserved.
Affiliation:
Program of Developmental Immunology, Department of Pediatrics, Massachusetts General Hospital, Harvard Medical School, 55 Fruit Street, Boston, MA 02114, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Antiviral Agents / chemistry,  pharmacology*
Complement Activation
Complement Pathway, Mannose-Binding Lectin / drug effects
Dose-Response Relationship, Drug
Hemagglutination, Viral / drug effects
Influenza A virus / chemistry,  drug effects*
Lectins / chemistry,  pharmacology*
Mannose-Binding Lectin / chemistry,  pharmacology*
Mice
Mice, Inbred C57BL
Neuraminidase / antagonists & inhibitors
Recombinant Fusion Proteins / chemistry,  pharmacology*
Grant Support
ID/Acronym/Agency:
R21 AI077081-01/AI/NIAID NIH HHS; R21 AI077081-01A1/AI/NIAID NIH HHS; U01 AI070330/AI/NIAID NIH HHS; U01 AI070330-01/AI/NIAID NIH HHS; U01 AI074503-01/AI/NIAID NIH HHS; U01 AI074503-01/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Antiviral Agents; 0/Lectins; 0/Mannose-Binding Lectin; 0/Recombinant Fusion Proteins; 0/ficolin; EC 3.2.1.18/Neuraminidase

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