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Helicobacter pylori surface proteins and lipopolysaccharides (LPS) are essential components of the bacterial outer membrane that facilitate survival and persistence in the human gastric environment [3, 10]. Surface proteins, including outer membrane proteins (OMPs) such as BabA and SabA, function as adhesins that bind to host receptors like Lewis blood group antigens, ensuring stable colonization of the gastric mucosa [7, 15]. The lipopolysaccharide layer provides structural integrity and acts as a selective permeability barrier against antimicrobial agents [13, 14]. A distinctive feature of H. pylori LPS is the expression of Lewis-like carbohydrate structures that mimic host antigens, a strategy known as molecular mimicry that helps the pathogen evade immune detection [1, 6]. These surface molecules are primary targets for the development of vaccines and novel antimicrobial therapies aimed at preventing adhesion or neutralizing virulence factors [9, 12]. In clinical practice, they serve as the basis for diagnostic tests, such as the stool antigen test, which detects these molecules to confirm active infection [16]. However, the similarity between bacterial LPS and host antigens poses a therapeutic challenge, as it can potentially trigger autoimmune responses, such as the production of anti-parietal cell antibodies associated with chronic gastritis [2, 5].
Inhibition of bacterial adhesion to the gastric mucosa, disruption of the bacterial outer membrane integrity, and induction of protective humoral and cellular immune responses through antigen recognition.
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