Protein IpaC (Invasin plasmid antigen C) (IpaC)

Protein IpaC, also known as Invasin plasmid antigen C, is a critical virulence factor produced by Shigella species, the causative agents of bacillary dysentery (UniProt P0A223). It is a key component of the Type III Secretion System (T3SS), specifically acting as a translocator protein that forms a translocon pore in the host cell membrane alongside IpaB (PubMed: 11443086). This pore allows the injection of bacterial effector proteins directly into the host cytoplasm, which is essential for the infection process. Additionally, IpaC plays a direct role in inducing host cell actin polymerization and membrane ruffling by activating Src-family kinases and Rho GTPases, which facilitates the internalization of the bacteria (PubMed: 15280483). Because it is essential for virulence and highly conserved among Shigella strains, IpaC is a primary target for the development of subunit vaccines, such as Invaplex, and anti-virulence drugs designed to block bacterial entry into intestinal epithelial cells (PubMed: 25691591). Experimental small molecules and antibodies targeting IpaC aim to disrupt the T3SS machinery or neutralize the protein's ability to manipulate host cell signaling.

Other names

Invasin plasmid antigen CIpaC proteinShigella invasin CTranslocator protein IpaC

Inhibition of the Type III secretion system (T3SS) translocon formation or neutralization of the protein's ability to induce host cell membrane remodeling.