PREPARATION FROM HUMAN RED CELLS OF A SUBSTANCE INHIBITING VIRUS HEMAGGLUTINATION

Area of Science:

• Virology
• Biochemistry
• Immunology

Background:

• Viral hemagglutination is a key process in viral infection, mediated by interactions between viral surface proteins and host cell receptors.
• Understanding these interactions is crucial for developing antiviral therapies.
• Human red blood cells and lung tissue are potential sources of biological inhibitors.

Purpose of the Study:

• To describe methods for extracting and purifying an agent that inhibits hemagglutination by influenza (PR8) and mumps viruses.
• To characterize the purified inhibitor and investigate its potential role as a virus receptor.
• To explore the inactivation mechanism of the inhibitor upon interaction with the virus.

Main Methods:

• Extraction and purification of the inhibitory agent from human red cells and lung.
• Chemical characterization of purified fractions (nitrogen, polysaccharide, phosphorus content).
• Ultracentrifugation analysis to determine macromolecular properties.
• Investigation of inhibitor solubility and conversion between ether/chloroform-soluble and insoluble forms.
• Incubation of the purified inhibitor with virus at 37°C to assess inactivation.

Main Results:

• A potent inhibitor of hemagglutination by influenza (PR8) and mumps viruses was successfully extracted and purified.
• Purified material (0.1 gamma) inhibited one hemagglutinating dose of virus, indicating high potency.
• Chemical analysis revealed the inhibitor contains polysaccharide and nitrogen, but no phosphorus, behaving as a polydisperse macromolecule.
• The inhibitor exists in different solubility forms, with the ether/chloroform-soluble form potentially representing the red cell virus receptor.
• The purified inhibitor is inactivated when incubated with the virus at 37°C.

Conclusions:

• A highly purified inhibitor of viral hemagglutination has been obtained from human sources.
• The inhibitor's properties suggest it may mimic the natural virus receptor on red blood cells.
• Further investigation into the inactivation mechanism by virus is warranted.