Outer membrane protein A (OmpA)

Outer membrane protein A (OmpA) is a predominant and highly conserved protein located in the outer membrane of Gram-negative bacteria, such as Escherichia coli, Acinetobacter baumannii, and Klebsiella pneumoniae (UniProt P0A910). It serves a critical structural role by anchoring the outer membrane to the underlying peptidoglycan layer through its C-terminal domain, thereby maintaining the mechanical integrity of the bacterial cell envelope (PubMed: 12730179). OmpA also functions as a multifaceted virulence factor, facilitating bacterial adhesion to host epithelial and endothelial cells, promoting biofilm formation, and contributing to resistance against host immune defenses like the complement system (PubMed: 25691586). In clinical contexts, OmpA is implicated in the pathogenesis of neonatal meningitis, pneumonia, and sepsis, making it a high-priority target for the development of next-generation antibacterial agents. Current therapeutic research focuses on utilizing OmpA as a vaccine antigen to elicit protective immunity or developing small molecules and monoclonal antibodies that inhibit its adhesive and structural functions (PubMed: 30254114). Additionally, OmpA acts as a receptor for various bacteriophages and colicins, highlighting its importance in bacterial ecology and competition (PubMed: 10411745).

Other names

OmpA-like proteinPeptidoglycan-associated proteinOmpA family proteinOuter membrane protein A (OmpA)

Disruption of outer membrane integrity, inhibition of bacterial adhesion to host cells, and induction of protective immune responses through antigenic recognition.