Helicobacter pylori membrane protein (or, more specifically, Helicobacter pylori outer membrane protein, for OMPs) (No universal abbreviation; individual families use abbreviations such as Hop (Helicobacter outer membrane porin), Hor (Hop-related), Hof (Helicobacter outer membrane family), Hom (Helicobacter outer membrane))

Helicobacter pylori membrane proteins comprise a heterogeneous group including lipoproteins, porins, adhesins, and efflux pumps that localize to the bacterial inner and outer membrane[10]. These proteins play critical roles in the bacterium’s ability to adhere to and invade gastric epithelial cells, mediate nutrient transport, interact with host immune defenses, and contribute to bacterial virulence[2][10][5]. Several families are well-defined: the Hop family (porin/adhesin, e.g., HopA–HopE), BabA/BabB (Lewis b antigen-binding adhesins), CagA (Type IV secretion system effector), and Hom/Hof/Hor groups, each with structure-function relationships tied to pathogenesis[3][4][7][8]. H. pylori membrane proteins underpin the organism’s role in chronic gastric inflammation, ulceration, and cancer, and they are the focus of targeted drug discovery and vaccine research[5][10].

Other names

Helicobacter pylori outer membrane proteinH. pylori OMPHop protein (HopA–HopE, BabA/BabB, HomA/HomB, HofA–HofH, etc.)

Inhibition of membrane protein function (e.g., porin/adhesin blockade reduces bacterial colonization) Disruption of outer membrane structure (leads to bacterial death) Blockade of efflux pumps (potentially increases antibiotic efficacy)