Antibiotics, also known as antibacterials, are medications that destroy or slow down the growth of bacteria. Since ancient times, many civilizations used topical application of mouldy bread, with many references to its beneficial effects. Alexander Fleming discovered penicillin, the first natural antibiotic, in 1928. There are two types of antibiotics: bactericidal antibiotic which interfere with either the formation of the bacterial cell wall or its cell contents and bacteriostatic agent which can prevent bacteria from multiplying. Antibiotics cannot treat viral infections, such as cold, flu, and most coughs.
Brefeldin A (BFA) is a lactone antibiotic and a specific inhibitor of protein trafficking.
Brefeldin A is a macrolide antibiotic produced by diverse kinds of fungi. Meanwhile, Brefeldin A is also a potent, reversible inhibitor of intracellular vesicle formation. Therefore, it can inhibit protein trafficking between the endoplasmic reticulum (ER) and the Golgi apparatus. Brefeldin A was initially isolated with hopes to become an antiviral drug but is now primarily used in research to study protein transport. As a research tool, Brefeldin A has been characterized extensively and used to analyze the mechanisms of membrane transport. Its best-known effect is the induction of the formation of numerous long tubules from the Golgi complex, which then fuse to the endoplasmic reticulum, thereby mediating the redistribution of resident Golgi proteins into the ER and hence causing a rapid and reversible block of secretion.
Since its first isolation from Penicillium decumbens in 1958, Brefeldin A exhibits potent biological activity in the antitumor, antifungal, and antiviral fields. More importantly, it shows apoptosis-inducing properties in various cancer cell lines. Brefeldin A also effectively inhibits the secretion of cytokines by blocking the trafficking of upstream signaling proteins. Interestingly, despite effectively impairing NLRP3 inflammasome activation, Brefeldin A does not block the release of IL-1β.