Methyl-accepting chemotaxis protein 4 (MCP-4)

Methyl-accepting chemotaxis protein 4 (MCP-4) is a specialized transmembrane receptor found in bacteria, including Escherichia coli (where it is known as Tap) and Borrelia burgdorferi (BB0680). It functions as a sensory transducer that detects environmental chemical signals—such as dipeptides in E. coli—and relays this information to the flagellar motor to direct bacterial movement, a process essential for nutrient acquisition and host colonization [1, 2, 28]. In pathogenic species like Borrelia burgdorferi, the causative agent of Lyme disease, MCP-4 has been identified as a major immunogenic protein that triggers CD4+ T cell responses and contributes to the inflammatory pathology of the disease [7, 14, 20]. While no therapeutic drugs currently target MCP-4, it is an active area of research for the development of anti-virulence therapies and vaccines aimed at preventing bacterial infections by disrupting their ability to navigate and persist within the host [2, 3, 31]. Its role as a specific bacterial antigen also makes it a potential candidate for diagnostic biomarkers in infectious diseases [14, 19].

Other names

TapMethyl-accepting chemotaxis protein IVBB0680Peptide sensor receptorMcp4

Inhibition of bacterial chemotaxis and host colonization