Bacterial P-fimbriae adhesin (PapG) (PapG)

Bacterial P-fimbriae adhesins, primarily the PapG protein located at the distal tip of the P-pilus, are critical virulence factors for uropathogenic Escherichia coli (UPEC). These adhesins function as lectins that specifically recognize and bind to galabiose-containing glycosphingolipids, such as the P-blood group antigens, on the surface of human kidney epithelial cells (UniProt: P07110; PubMed: 11021936). This specific adhesion is a prerequisite for the colonization of the upper urinary tract and the subsequent development of acute pyelonephritis. Because PapG is essential for infection but not for bacterial survival, it is considered a high-priority target for anti-adhesion therapies that aim to prevent infection without inducing the selective pressure that leads to antibiotic resistance (PubMed: 15505115). Current therapeutic strategies include the development of galabiose-mimetic small molecules to block the binding site and pilicides that inhibit the assembly of the fimbriae structure (PubMed: 21830858).

Other names

PapG adhesinP-pilus adhesinPyelonephritis-associated pilus adhesinGal-Gal adhesinP-fimbrial tip adhesin

Competitive inhibition of bacterial attachment to host cell glycolipid receptors (specifically galabiose) and disruption of the chaperone-usher pathway required for pilus biogenesis (PubMed: 21830858, 11021936).