Bacterial surface receptors of Staphylococcus aureus, Pseudomonas aeruginosa, and Acinetobacter baumannii

Bacterial surface receptors on Staphylococcus aureus, Pseudomonas aeruginosa, and Acinetobacter baumannii are a diverse set of proteins and glycans that facilitate the initial stages of infection, including colonization and biofilm formation. In S. aureus, these include Microbial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMMs) like Clumping factor A (ClfA) and Protein A (Spa), which are vital for binding host extracellular matrix proteins and evading immune detection (Foster et al., 2014, PMID: 24413161). P. aeruginosa and A. baumannii utilize surface structures such as Type IV pili, lectins (LecA/B), and outer membrane proteins (e.g., OmpA) to adhere to host cells and environmental surfaces, contributing to their persistence in clinical settings (Giraud & de Bentzmann, 2012, PMID: 22460523; Lee et al., 2017, PMID: 28163631). These receptors are primary targets for anti-virulence therapies, including monoclonal antibodies like Tefibazumab and MEDI3902, which aim to block bacterial attachment or promote clearance by the immune system (DiGiandomenico et al., 2014, PMID: 25393894). By targeting these surface-exposed molecules, researchers hope to develop treatments that reduce the severity of infections such as pneumonia and sepsis while minimizing the selective pressure that drives antibiotic resistance.

Other names

Bacterial adhesinsMicrobial Surface Components Recognizing Adhesive Matrix Molecules (MSCRAMMs)Surface-exposed virulence factorsCell wall-anchored proteins

Inhibition of bacterial adhesion to host tissues, neutralization of surface-associated virulence factors, and enhancement of opsonophagocytic killing by the host immune system.