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Complement System

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The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a membrane...

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Updated: May 26, 2026

Portable Paper-Based Immunoassay Combined with Smartphone Application for Colorimetric and Quantitative Detection of Dengue NS1 Antigen

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Complement-mediated neutralization of dengue virus requires mannose-binding lectin.

Panisadee Avirutnan¹, Richard E Hauhart, Mary A Marovich

¹Department of Medicine, Washington University School of Medicine, St. Louis, Missouri, USA.

|December 15, 2011

Summary

Mannose-binding lectin (MBL) neutralizes dengue virus (DENV) infection by activating complement and directly binding the virus. Higher MBL levels in human serum correlate with more effective DENV neutralization, suggesting a role for MBL genetics in disease.

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A Murine Model of Dengue Virus-induced Acute Viral Encephalitis-like Disease

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Published on: April 28, 2019

Area of Science:

Immunology
Virology
Genetics

Background:

Mannose-binding lectin (MBL) is a crucial innate immune protein recognizing microbial glycans and activating complement via the lectin pathway.
Previous research demonstrated MBL's role in neutralizing West Nile virus (WNV).
Dengue virus (DENV) poses a significant global health threat, with four serotypes causing varied disease severity.

Purpose of the Study:

To investigate the antiviral activity of MBL against DENV infection.
To determine the role of the lectin complement pathway in MBL-mediated DENV neutralization.
To assess the impact of MBL concentration and genetic variation on DENV control.

Main Methods:

Utilized mouse strains deficient in complement components to assess lectin pathway dependence.
Tested MBL's binding and neutralization activity against all four DENV serotypes.
Analyzed human serum samples with varying MBL levels to correlate MBL concentration with DENV neutralization efficacy.

Main Results:

MBL-mediated inhibition of DENV infection was primarily dependent on the lectin pathway.
Human MBL effectively bound and neutralized all four DENV serotypes via complement-dependent and -independent mechanisms.
A direct correlation was observed between MBL concentration in human serum and the degree of DENV neutralization.

Conclusions:

MBL plays a significant role in controlling DENV infection through multiple pathways.
Genetic variations influencing MBL levels and function in humans may impact DENV pathogenesis and disease severity.
MBL represents a potential target for therapeutic strategies against DENV infections.