CEACAM3 is a glycoprotein that is primarily expressed on the surface of granulocytes, a type of white blood cell. It plays a crucial role in the immune system by mediating the phagocytosis of bacteria. The protein consists of an extracellular domain, a single transmembrane region, and a cytoplasmic tail. The extracellular domain is responsible for binding to bacterial pathogens, while the cytoplasmic tail contains signaling motifs that activate the immune response.
CEACAM3 is particularly important in the body’s defense against Gram-negative bacteria. It acts as a receptor for various bacterial adhesins, which are molecules that facilitate the attachment of bacteria to host cells. Upon binding to these adhesins, CEACAM3 triggers a series of intracellular signaling events that lead to the engulfment and destruction of the bacteria by granulocytes .
The recombinant form of CEACAM3 has been studied for its potential therapeutic applications. By blocking the interactions between bacterial pathogens and human epithelial cells, recombinant CEACAM3 can inhibit bacterial infections. This has significant implications for the treatment of diseases caused by mucosal pathogens, such as Moraxella catarrhalis .
Recent studies have focused on the development of recombinant polypeptides derived from CEACAM3. These polypeptides have shown promise in blocking bacterial interactions and enhancing the immune response. Additionally, antibodies against CEACAM3 have been developed to further inhibit bacterial infections .