ArticleProtein & cell2010
Specific interaction of hepatitis C virus glycoproteins with mannan binding lectin inhibits virus entry.
Article in Protein & cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
37 citing papers in PubMed, 1 synthesis or guideline pooled it, 63 citations in OpenAlex.
- Relationship of serum mannose-binding lectin levels with the development of sepsis: a meta-analysis.Inflammation · 2015Pooled it
- Interplay of host and viral genetic variations in modulating antibody responses to genotype 3a hepatitis C virus: Implications for vaccine design.Cell reports · 2025Article
- Biochemical characterization of a novel purified lectin extracted from Pleurotus ostreatus mushroom for its antiviral activity.Scientific reports · 2025Article
- Article
- A B cell screen against endogenous retroviruses identifies glycan-reactive IgM that recognizes a broad array of enveloped viruses.Science immunology · 2024Article
- Effects ofBiochemistry and biophysics reports · 2023Article
- Tinker, tailor, soldier, cell: the role of C-type lectins in the defense and promotion of disease.Protein & cell · 2023Review
- Hepatitis C Virus Glycan-Dependent Interactions and the Potential for Novel Preventative Strategies.Pathogens (Basel, Switzerland) · 2021Review
- Review
- Mannose binding lectin gene 2 (rs1800450) missense variant may contribute to development and severity of COVID-19 infection.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2021Article
- Hepatitis C Virus Vaccine: Challenges and Prospects.Vaccines · 2020Review
- In the Crosshairs: RNA Viruses OR Complement?Frontiers in immunology · 2020Review
- Collectins: Innate Immune Pattern Recognition Molecules.Advances in experimental medicine and biology · 2020Review
- Microarray analysis of infectious bronchitis virus infection of chicken primary dendritic cells.BMC genomics · 2019Article
- Association of C-type lectin 18 levels with extrahepatic manifestations in chronic HCV infection.Scientific reports · 2018Article
- Global aspects of viral glycosylation.Glycobiology · 2018Article
- The Complement System and C1q in Chronic Hepatitis C Virus Infection and Mixed Cryoglobulinemia.Frontiers in immunology · 2018Review
- Chicken mannose binding lectin has antiviral activity towards infectious bronchitis virus.Virology · 2017Article
- Preferential association of hepatitis C virus with CD19Hepatology (Baltimore, Md.) · 2016Article
- Secreted NS1 Protects Dengue Virus from Mannose-Binding Lectin-Mediated Neutralization.Journal of immunology (Baltimore, Md. : 1950) · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 4 institutions in 1 country.
Funding
Abstract
Mannan-binding lectin (MBL) is a soluble innate immune protein that binds to glycosylated targets. MBL acts as an opsonin and activates complement, contributing to the destruction and clearance of infecting microorganisms. Hepatitis C virus (HCV) encodes two envelope glycoproteins E1 and E2, expressed as non-covalent E1/E2 heterodimers in the viral envelope. E1 and E2 are potential ligands for MBL. Here we describe an analysis of the interaction between HCV and MBL using recombinant soluble E2 ectodomain fragment, the full-length E1/E2 heterodimer, expressed in vitro, and assess the effect of this interaction on virus entry. A binding assay using antibody capture of full length E1/E2 heterodimers was used to demonstrate calcium dependent, saturating binding of MBL to HCV glycoproteins. Competition with various saccharides further confirmed that the interaction was via the lectin domain of MBL. MBL binds to E1/E2 representing a broad range of virus genotypes. MBL was shown to neutralize the entry into Huh-7 cells of HCV pseudoparticles (HCVpp) bearing E1/E2 from a wide range of genotypes. HCVpp were neutralized to varying degrees. MBL was also shown to neutralize an authentic cell culture infectious virus, strain JFH-1 (HCVcc). Furthermore, binding of MBL to E1/E2 was able to activate the complement system via MBL-associated serine protease 2. In conclusion, MBL interacts directly with HCV glycoproteins, which are present on the surface of the virion, resulting in neutralization of HCV particles.
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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.