Anti-FliD (Pseudomonas aeruginosa), mAb (rec.) (SH1579-B7)

Pathogenic bacteria cause a multitude of deadly human diseases. Pseudomonas aeruginosa is a predominant organism within the hospital environment, an increasingly multidrug-resistant microbe, and the most common gram-negative pathogen causing nosocomial pneumonia in the United States. Nearly all P. aeruginosa infections are associated with compromised host defenses, which may include patients with severe burns, diabetes, cancer, organ transplants or additional immunodeficiencies. Many of these pathogenic bacteria possess flagella, molecular machines responsible for cell motility, adherence to host cells, and pathogenicity. Flagella are helix-shaped hollow attachments formed predominantly by thousands of copies of the protein flagellin (also called FliC), anchored in the bacterial membrane by a hook (or joint) that is attached to the basal body and that is composed of rotary motor proteins. A FliD (also called HAP2) oligomer forms the cap protein complex that is located at the tip of the flagellar filament. This complex controls the distal growth of the filament by regulating the assembly of FliC molecules, which are transported through the hollow filament from the cytoplasm to the tip of the flagellum. In the absence of FliD, flagella are not formed, resulting in impaired motility and infectivity. Protein function: Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end. Essential for motility. Responsible for adhesion to mucin, which is the initial event in colonization by this organism of the airways of cystic fibrosis patients. [The UniProt Consortium]