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Outer membrane protein of Neisseria meningitidis

Molecular classification
Porin, β-barrel outer membrane protein, Adhesin, Metallopeptidase (for specific proteins, e.g., NMB0315), Lipoprotein transporter (Slam), Protein complex (β-barrel assembly machinery), Other
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Overview

The term "outer membrane proteins and polysaccharides of Neisseria meningitidis" refers to a heterogeneous group of structurally and functionally distinct molecules located on the surface of the Gram-negative bacterial pathogen Neisseria meningitidis. These surface molecules include integral membrane proteins such as OpcA, which mediates adhesion to human host cells via interaction with proteoglycans and vitronectin[1]; PilQ, a pore-forming complex essential for type IV pilus assembly and translocation[2]; and members of the β-barrel assembly machinery (for example, Omp85/BamA), which are responsible for the correct insertion and assembly of other outer membrane proteins[4]. The outer membrane also contains lipoprotein-specific transporters such as Slam, which allow surface display of lipidated virulence factors important for immune evasion and nutrient acquisition[5]. Polysaccharide molecules, such as those constituting the bacterial capsule, are translocated to the surface via dedicated protein complexes (e.g., CtrA)[6]. These surface-exposed molecules play critical roles in pathogenesis, forming the primary interface with the host immune system and being central to both vaccine development (as immunogens) and diagnostic purposes[3][5]. Major challenges to therapeutic targeting include high antigenic variability and mechanisms of immune evasion. The current entry is non-ideal: it refers to a large, functionally diverse set of proteins and polysaccharides, not to a single canonical molecule/receptor, and therefore should be divided into entries for individual proteins or polysaccharides for structured data extraction. **Note:** - This target is incorrectly specified for purposes of target-based drug or biomarker databases, as it groups numerous distinct entities (see is_incorrect: true). Each prominent outer membrane protein (e.g., OpcA, PilQ) or polysaccharide (e.g., type B capsule polysaccharide) should be listed separately for structured data. - The entry covers various classifications depending on the specific OMP or polysaccharide referenced. For canonical forms, see e.g., "OpcA", "PilQ", or "capsular polysaccharide biosynthesis protein CtrA".

Other names
Outer membrane proteins (OMPs)OpcAPilQNMB0315Omp85CtrASlam proteins
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Mechanism of action

Induction of immune response (vaccines targeting OMPs and polysaccharides); Inhibition of bacterial adhesion (theoretical); Antibody-mediated complement activation

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Biological functions

Adhesion to host cellsImmune evasionPolysaccharide capsule expression and exportAssembly of outer membrane proteinsNutrient acquisitionEnzymatic activity (e.g., peptidase)
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Disease associations

InfectionMeningitisSepticemia
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Safety considerations

Immune evasion by antigenic variation of surface proteins and polysaccharidesPoor cross-protection due to OMP sequence variabilityAutoimmunity risk from molecular mimicry (capsule polysaccharides may resemble host molecules)Reactogenicity of OMV-based vaccines
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Interacting drugs

Meningococcal polysaccharide-based vaccines

1 more in the full profile.

07

Biomarkers

OpcA surface expression (potential for diagnostics)Capsular polysaccharide (serogroup identification)Outer membrane protein signatures (strain typing)

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