Helicobacter pylori urease and cell adhesion factors

The term "Helicobacter pylori urease and cell adhesion factors" collectively refers to two functionally distinct classes of molecules central to H. pylori pathogenesis: (1) **urease**, a nickel-dependent metalloenzyme required for survival in the acidic human stomach by catalyzing the hydrolysis of urea into ammonia and carbon dioxide, thereby locally neutralizing gastric acid; and (2) **bacterial cell adhesion factors**, a diverse group of outer membrane proteins (OMPs) such as BabA, SabA, and HpaA that mediate specific binding to host epithelial cell surface molecules (e.g., Lewis blood group antigens and sialylated glycans), facilitating colonization, persistence, and delivery of virulence factors by the bacterium. Both urease and adhesion factors are considered *bona fide* anti-infective drug targets in H. pylori, but the targets are structurally and mechanistically distinct, and interventions may address either or both components depending on therapeutic strategy[1][2][4][5][6][7][8].

Other names

Urease (for the enzyme)BabA (blood group antigen-binding adhesin)SabA (sialic acid-binding adhesin)HpaA (Helicobacter pylori adhesin A)OMPs (outer membrane proteins; family including many adhesins)

Urease inhibitors: compete with urea for binding to the active site, block nickel coordination, or disrupt maturation of the enzyme[1][3][5][7] Adhesin blockers (experimental): disrupt binding of bacterial adhesins (BabA/SabA/HpaA) to host cell surface glycans and receptors[6][4][8]