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Bee Venom and Its Two Main Components—Melittin and Phospholipase A2—As Promising Antiviral Drug Candidates
Carole Yaacoub, Rim Wehbe, Rabih Roufayel, Ziad Fajloun, Bruno Coutard

Bee Venom and Its Two Main Components—Melittin and Phospholipase A2—As Promising Antiviral Drug Candidates

Science & Mathematics Published 2023 Verification Pending

Overview & Synopsis

Viruses are known to infect most types of organisms. In humans, they can cause several diseases that range from mild to severe. Although many antiviral therapies have been developed, viral infections continue to be a leading cause of morbidity and mortality worldwide. Therefore, the discovery of new and effective antiviral agents is desperately needed. Animal venoms are a rich source of bioactive molecules found in natural goods that have been used since ancient times in alternative medicine to treat a variety of human diseases. Recently, and with the onset of the COVID-19 pandemic, scientists have regained their interest in the possible use of natural products, such as bee venom (BV), as a potential antiviral agent to treat viral infections. BV is known to exert many therapeutic activities such as anti-proliferative, anti-bacterial, and anti-inflammatory effects. However, there is limited discussion of the antiviral activity of BV in the literature. Therefore, this review aims to highlight the antiviral properties of BV and its two primary constituents, melittin (MEL) and phospholipase A2 (PLA2), against a variety of enveloped and non-enveloped viruses. Finally, the innovative strategies used to reduce the toxicity of BV and its two compounds for the development of new antiviral treatments are also considered.

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Document Information

Document Title Bee Venom and Its Two Main Components—Melittin and Phospholipase A2—As Promising Antiviral Drug Candidates
Author / Organization Carole Yaacoub, Rim Wehbe, Rabih Roufayel, Ziad Fajloun, Bruno Coutard
Subject & Discipline Multidisciplinary Academic Open Research
Categories Science & Mathematics
Publication Year 2023
License / Rights Open Access / Creative Commons
Resource Verification Listed PDF (Verification Pending)
Original Host Website HAL Open Science (hal.science)
File Format application/pdf (Portable Document Format)
Language EN
Catalog ID DOC-182731
Original Source Link Visit Source Page on hal.science »