Enzymes involved in Helicobacter pylori cell membrane integrity

Enzymes involved in Helicobacter pylori cell membrane integrity comprise a group of proteins essential for the biosynthesis and maintenance of the outer membrane, including key enzymes such as cholesteryl α-D-glucopyranoside 6′-acyltransferase (CGAT), components of the lipopolysaccharide (LPS) biosynthesis pathway (such as GmhB/HP0860), and outer membrane biogenesis proteins. These enzymes are critical for the synthesis and remodeling of components like LPS and membrane lipids, which help H. pylori withstand the acidic gastric environment, adhere to gastric epithelial cells, avoid immune recognition, and establish infection[1][2][3][4]. Some secreted enzymes are delivered to host cell membranes via bacterial outer membrane vesicles, directly modifying host cell surface properties to promote bacterial colonization[1]. Inhibiting these biosynthetic processes impairs bacterial viability and adhesion and is considered an attractive strategy for therapeutic intervention[1][2][3]. However, the “target” is not a single molecule but rather a set of bacterial biosynthetic enzymes and pathways collectively responsible for membrane integrity and function. Note: This entry is marked as incorrect because "Helicobacter pylori enzymes/cell membrane integrity" describes a class or pathway—not a distinct, single molecular target. It encompasses multiple enzymes and structural proteins (e.g., LPS biosynthesis, phospholipases, OM biogenesis machinery, urease) that together maintain H. pylori's outer membrane structure and integrity[1][2][3][4][5]. To generate a canonical target entry, it is necessary to specify a particular protein or enzyme (such as "Cholesteryl α-D-glucopyranoside 6′-acyltransferase" or "Urease") rather than this broad category.

Other names

Helicobacter pylori outer membrane enzymesH. pylori membrane integrity enzymesH. pylori envelope biosynthesis enzymes

Enzyme inhibition (e.g., CGAT inhibitors block enzyme activity required for H. pylori adhesion); Disruption of membrane biosynthesis/assembly (inhibiting LPS, outer membrane protein transport or lipid modification pathways); Neutralization of the bacterial microenvironment (e.g., urease inhibition reduces local pH buffering); Modulation of host cell autophagy/lysosomal function to restrict bacterial survival