Streptococcus agalactiae molecular targets (GBS targets)

Streptococcus agalactiae, commonly referred to as Group B Streptococcus (GBS), is a Gram-positive bacterium that serves as a major cause of neonatal sepsis, meningitis, and pneumonia, as well as invasive infections in the elderly and immunocompromised [1, 17]. Its molecular targets encompass a wide range of essential bacterial components, most notably the penicillin-binding proteins (PBPs), such as PBP2X and PBP1A, which are the primary targets for first-line beta-lactam antibiotics like penicillin G and ampicillin [1, 5]. These enzymes are critical for the synthesis and cross-linking of the peptidoglycan cell wall, and mutations in PBP2X have been linked to reduced penicillin susceptibility [3, 13]. Additionally, the bacterial ribosome (50S and 30S subunits) serves as a target for macrolides (e.g., erythromycin) and lincosamides (e.g., clindamycin), which inhibit protein synthesis, although resistance mediated by erm genes is an increasing concern [16, 19]. Virulence-associated targets include Sortase A (SrtA), an enzyme responsible for anchoring surface proteins to the cell wall, and C5a peptidase (ScpB), a serine protease that facilitates immune evasion by degrading host complement factors [2, 10, 15]. These virulence factors are currently being investigated as potential targets for novel anti-infective therapies and vaccine development [6, 22]. Clinical management relies on identifying these targets through screening and susceptibility testing to ensure effective treatment and prophylaxis [20, 23].

Other names

Group B Streptococcus targetsGBS molecular targetsS. agalactiae drug targetsStreptococcus agalactiae virulence factors

Inhibition of cell wall peptidoglycan synthesis by binding to penicillin-binding proteins (PBPs); Inhibition of protein synthesis by binding to the 50S or 30S ribosomal subunits; Inhibition of DNA gyrase and topoisomerase IV; Disruption of cell wall synthesis by binding to D-alanyl-D-alanine precursors.