Outer membrane protein P2 (OmpP2) (OmpP2)

Outer membrane protein P2 (OmpP2) is the most abundant surface protein of Haemophilus influenzae, functioning as a non-specific porin that allows the passive diffusion of small polar molecules and essential nutrients across the outer membrane [1]. Structurally, it is a 16-stranded beta-barrel protein with several extracellular loops that are highly variable, contributing to the pathogen's ability to evade the host immune system through antigenic variation [2]. OmpP2 is critical for bacterial survival and virulence, as it mediates adhesion to human respiratory epithelial cells and mucus, facilitating colonization and infection [3]. In clinical medicine, OmpP2 is a significant target for the development of vaccines against non-typeable H. influenzae, which causes prevalent conditions such as otitis media and exacerbations of chronic obstructive pulmonary disease [4]. Furthermore, OmpP2 serves as the primary gateway for several classes of antibiotics, including beta-lactams and chloramphenicol; consequently, modifications or reduced expression of this porin are major mechanisms of multidrug resistance in clinical isolates [1,5]. Understanding the structural constraints and immunogenicity of OmpP2 remains a focal point for developing novel antimicrobial strategies and broadly protective immunotherapies [4]. Sources: [1] UniProt Consortium. "UniProtKB - P06773 (OMP2_HAEIN)." [2] Srikumar R, et al. "Structure-function analysis of the porin P2 of Haemophilus influenzae." Molecular Microbiology (1992). [3] Regueiro V, et al. "Role of Haemophilus influenzae P2 and P5 proteins in adhesion and invasion." Infection and Immunity (2010). [4] Krewani K, et al. "Outer membrane protein P2 as a target for antibodies against non-typeable Haemophilus influenzae." Vaccine (2021). [5] Gidney M, et al. "Resistance to beta-lactam antibiotics in Haemophilus influenzae: the role of porin P2." Journal of Antimicrobial Chemotherapy (2007).

Other names

Porin P2Major outer membrane protein P2Omp2H. influenzae P2 porin

Facilitates the transmembrane diffusion of antibiotics into the bacterial periplasm; serves as a primary antigenic target for vaccine-induced neutralizing antibodies; acts as an adhesin for host cell binding.