Outer membrane protein P2 (OMP P2) (OMP P2)

Outer membrane protein P2 (OMP P2) is the most abundant surface protein in Haemophilus influenzae, functioning as a non-specific porin that facilitates the passive diffusion of nutrients and small molecules across the bacterial outer membrane [1, 2]. It plays a critical role in the pathogen's interaction with the host, acting as an adhesin that binds to the laminin receptor (LamR) on human brain microvascular endothelial cells, which is a key step in crossing the blood-brain barrier during meningitis [19]. OMP P2 is a primary target for the human bactericidal antibody response and has been extensively investigated as a vaccine candidate for both encapsulated (type b) and nontypeable H. influenzae (NTHi) [12, 17]. However, the protein exhibits significant antigenic heterogeneity, particularly in its surface-exposed loops, which allows the bacteria to evade the host immune system and complicates vaccine design [4, 5]. Additionally, OMP P2 is clinically important in the context of antibiotic resistance, as mutations that alter porin permeability can reduce the entry of beta-lactam antibiotics, such as imipenem, into the cell [3, 15]. Understanding the structural and functional variations of OMP P2 is therefore essential for developing effective therapeutics and preventative measures against H. influenzae infections [18].

Other names

OmpP2Porin P2Major outer membrane protein P2ompP2

Acts as a porin channel for the passive diffusion of antibiotics into the bacterium and serves as an antigenic target for the induction of bactericidal antibodies.