ArticleBiochemical pharmacology2011
Recombinant chimeric lectins consisting of mannose-binding lectin and L-ficolin are potent inhibitors of influenza A virus compared with mannose-binding lectin.
Article in Biochemical pharmacology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 37 citations in OpenAlex.
- Collectins and Ficolins.Advances in experimental medicine and biology · 2025Review
- Computationally guided conversion of the specificity of E-selectin to mimic that of Siglec-8.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Reversible Lectin Binding to Glycan-Functionalized Graphene.International journal of molecular sciences · 2021Article
- Influenza virus N-linked glycosylation and innate immunity.Bioscience reports · 2019Review
- Ficolins and the Recognition of Pathogenic Microorganisms: An Overview of the Innate Immune Response and Contribution of Single Nucleotide Polymorphisms.Journal of immunology research · 2019Review
- Enhancement of Ebola Virus Infection via Ficolin-1 Interaction with the Mucin Domain of GP Glycoprotein.Journal of virology · 2016Article
- Pentraxins and Collectins: Friend or Foe during Pathogen Invasion?Trends in microbiology · 2015Review
- Lectin engineering, a molecular evolutionary approach to expanding the lectin utilities.Molecules (Basel, Switzerland) · 2015Review
- Human lectins and their roles in viral infections.Molecules (Basel, Switzerland) · 2015Review
- Compounds with anti-influenza activity: present and future of strategies for the optimal treatment and management of influenza. Part II: Future compounds against influenza virus.Journal of preventive medicine and hygiene · 2014Review
- Recombinant human mannose-binding lectin dampens human alveolar macrophage inflammatory responses to influenza A virus in vitro.Journal of leukocyte biology · 2014Article
- Ficolins and infectious diseases.Virologica Sinica · 2014Review
- A novel bifunctional hybrid with marine bacterium alkaline phosphatase and Far Eastern holothurian mannan-binding lectin activities.PloS one · 2014Article
- Efficacy of recombinant chimeric lectins, consisting of mannose binding lectin and L-ficolin, against influenza A viral infection in mouse model study.Virus research · 2013Article
- Article
- Human H-ficolin inhibits replication of seasonal and pandemic influenza A viruses.Journal of immunology (Baltimore, Md. : 1950) · 2012Article
- Legume lectins inhibit human parainfluenza virus type 2 infection by interfering with the entry.Viruses · 2012Article
- L-ficolin binds to the glycoproteins hemagglutinin and neuraminidase and inhibits influenza A virus infection both in vitro and in vivo.Journal of innate immunity · 2012Article
- Soluble host defense lectins in innate immunity to influenza virus.Journal of biomedicine & biotechnology · 2012Review
- Mannose-binding lectin binds to amyloid β protein and modulates inflammation.Journal of biomedicine & biotechnology · 2012Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.