Abstract
Long pentraxin 3 (PTX3) is a non-redundant component of the humoral arm of innate immunity. The present study was designed to investigate the interaction of PTX3 with Neisseria meningitidis. PTX3 bound acapsular meningococcus, Neisseria-derived outer membrane vesicles (OMV) and 3 selected meningococcal antigens (GNA0667, GNA1030 and GNA2091). PTX3-recognized microbial moieties are conserved structures which fulfil essential microbial functions. Ptx3-deficient mice had a lower antibody response in vaccination protocols with OMV and co-administration of PTX3 increased the antibody response, particularly in Ptx3-deficient mice. Administration of PTX3 reduced the bacterial load in infant rats challenged with Neisseria meningitidis. These results suggest that PTX3 recognizes a set of conserved structures from Neisseria meningitidis and acts as an amplifier/endogenous adjuvant of responses to this bacterium.
Highlights
Neisseria meningitidis (Nm) is a leading cause of bacterial meningitis and severe sepsis [1, 2]
While no binding was observed to wild type MC58, by flow cytometry we found a dose dependent binding of Biotinylated PTX3 (bPTX3) to the mutant MC58 cap, lacking the polysaccharidic capsule (Fig. 1)
The long pentraxin pentraxin 3 (PTX3) is an essential component of the humoral arm of innate immunity highly conserved in evolution
Summary
Neisseria meningitidis (Nm) is a leading cause of bacterial meningitis and severe sepsis [1, 2]. PTX3 is a multifunctional molecule capable of interacting with several proteins, including complement components, microbial moieties and adhesion molecules [19,20,21,22,23,24,25,26] It facilitates recognition and phagocytosis of fungal conidia mainly by PMN via Fcγ receptors Given the role of PTX3 in the orchestration of innate immunity including complement activation, essential for resistance against Nm, and its high levels in patients with meningococcal sepsis [40], we decided to investigate PTX3 interaction with Nm. Here we report that PTX3 binds MenB, recognizes selected recombinant surface proteins from MenB, and has protective activity against infection in vivo
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