Related Experiment Video
Updated: Mar 19, 2026

Affinity Purification of Influenza Virus Ribonucleoprotein Complexes from the Chromatin of Infected Cells
Published on: June 3, 2012
The Human Antimicrobial Protein Bactericidal/Permeability-Increasing Protein (BPI) Inhibits the Infectivity of
Olaf Pinkenburg1, Torben Meyer1, Norbert Bannert2
1Institute for Immunology, Philipps-University of Marburg, Marburg, Germany.
Abstract:
In addition to their well-known antibacterial activity some antimicrobial peptides and proteins (AMPs) display also antiviral effects. A 27 aa peptide from the N-terminal part of human bactericidal/permeability-increasing protein (BPI) previously shown to harbour antibacterial activity inhibits the infectivity of multiple Influenza A virus strains (H1N1, H3N2 and H5N1) the causing agent of the Influenza pneumonia. In contrast, the homologous murine BPI-peptide did not show activity against Influenza A virus. In addition human BPI-peptide inhibits the activation of immune cells mediated by Influenza A virus. By changing the human BPI-peptide to the sequence of the mouse homologous peptide the antiviral activity was completely abolished. Furthermore, the human BPI-peptide also inhibited the pathogenicity of the Vesicular Stomatitis Virus but failed to interfere with HIV and measles virus. Electron microscopy indicate that the human BPI-peptide interferes with the virus envelope and at high concentrations was able to destroy the particles completely.
Insights
A human antimicrobial peptide (AMP) derived from bactericidal/permeability-increasing protein (BPI) shows potent antiviral activity against Influenza A virus strains. This peptide also inhibits viral pathogenicity and immune cell activation, offering new therapeutic avenues.
Area of Science:
- Biochemistry
- Virology
- Immunology
Background:
- Antimicrobial peptides and proteins (AMPs) possess antibacterial and antiviral properties.
- Human bactericidal/permeability-increasing protein (BPI) N-terminal peptide exhibits antibacterial activity.
- Influenza A virus causes significant respiratory illness and pneumonia.
Purpose of the Study:
- To investigate the antiviral activity of a human BPI-derived peptide against Influenza A virus.
- To determine the specificity of the peptide's antiviral effects.
- To elucidate the mechanism of action of the human BPI-peptide on virus particles.
Main Methods:
- Peptide synthesis and characterization.
- In vitro antiviral assays using Influenza A virus strains (H1N1, H3N2, H5N1).
- Assays for immune cell activation.
- Electron microscopy to visualize virus-peptide interactions.
Main Results:
- The human BPI-peptide effectively inhibited infectivity of multiple Influenza A virus strains.
- Homologous murine BPI-peptide lacked antiviral activity, indicating sequence specificity.
- Human BPI-peptide also inhibited Vesicular Stomatitis Virus but not HIV or measles virus.
- Electron microscopy revealed interference with the virus envelope and particle destruction at high concentrations.
Conclusions:
- The human BPI-peptide is a potent inhibitor of Influenza A virus infectivity and pathogenicity.
- Sequence-specific interactions are crucial for the peptide's antiviral efficacy.
- The peptide's mechanism involves direct disruption of the viral envelope.
Related Concept Videos
Influenza
Leaky Scanning
Antimicrobial Proteins
Interferons
Interferons (IFNs) are proteins produced by lymphocytes, macrophages, and fibroblasts infected with viruses. While IFNs cannot prevent viruses from entering and...
Antimicrobial Effectiveness
Inhibitors of Gram-positive Cell Wall Synthesis
Inhibitors of Viral Protein Synthesis

