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The 30S ribosomal subunit of Helicobacter pylori is a vital ribonucleoprotein complex responsible for the initiation and accuracy of bacterial protein synthesis [5, 9]. It consists of the 16S ribosomal RNA (rRNA) and approximately 21 ribosomal proteins, which together facilitate the decoding of genetic information by ensuring correct codon-anticodon pairing between mRNA and tRNA [4, 5]. This subunit is a major therapeutic target for several classes of antibiotics, including tetracyclines and aminoglycosides, which are used to treat H. pylori infections [1, 13]. Tetracyclines inhibit translation by binding to the 30S subunit and blocking the entry of aminoacyl-tRNA into the ribosomal A-site, while aminoglycosides can induce mRNA misreading or inhibit translocation [8, 13, 16]. Resistance to these treatments is a significant clinical challenge, often arising from specific point mutations in the 16S rRNA gene that alter the antibiotic binding site [1, 8, 16]. Eradication of H. pylori is essential for preventing and treating associated diseases such as chronic gastritis, peptic ulcers, and gastric adenocarcinoma [7, 10, 19]. The subunit's structural conservation across bacteria makes it a broad-spectrum target, yet specific variations in H. pylori influence its susceptibility and resistance profiles [13, 16].
Inhibition of bacterial protein synthesis by binding to the 30S subunit, which blocks the attachment of aminoacyl-tRNA to the A-site (tetracyclines) or induces mRNA misreading and inhibits translocation (aminoglycosides) [8, 13, 16].
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