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The new discovery - pertussis pathogen

Recently, an article in the Nature Communications study by researchers wrote articles studied the structure and function of bacteria that cause pertussis important membrane proteins. Discovered the protein structure is different from previous pertussis assumed model, this discovery provides a basis for new treatments for the infection.

Many tiny protein pores are found in the outer membrane of the pertussis pathogen, the bacterium Bordetella pertussis. Through these pores, the pathogen secretes proteins, which are important for bacterial attachment in the human respiratory tract and for the formation of resistant biofilms. 

Cellular membranes are barriers, which protect the cell from the outside world. Certain molecules can however still move across these barriers at specifically designed sites. The membrane protein FhaC in the pertussis pathogen is such a border guard. It is located on the outer cell membrane and channels the adhesin FHA across the membrane to the outside. FHA allows the bacterium to attach to host surfaces and thus plays an important role in the pertussis infection.

investigations have shown that the FhaC protein has the same architecture as proteins that integrate new membrane proteins. The structural analysis also revealed how a helical protein domain acts like a plug, closing the pore in the absence of a cognate substrate. When the FHA adhesin binds to the membrane protein FhaC, this plug is released, the pore opens and the adhesion traverses the membrane.

Finally, it can be significantly impaired by inhibitors FhaC targeting function to prevent adhesion of pathogens to host cells, thereby treating pertussis.