Pathogenesis and pathophysiology of pneumococcal meningitis - PubMed (original) (raw)
Review
Pathogenesis and pathophysiology of pneumococcal meningitis
Barry B Mook-Kanamori et al. Clin Microbiol Rev. 2011 Jul.
Abstract
Pneumococcal meningitis continues to be associated with high rates of mortality and long-term neurological sequelae. The most common route of infection starts by nasopharyngeal colonization by Streptococcus pneumoniae, which must avoid mucosal entrapment and evade the host immune system after local activation. During invasive disease, pneumococcal epithelial adhesion is followed by bloodstream invasion and activation of the complement and coagulation systems. The release of inflammatory mediators facilitates pneumococcal crossing of the blood-brain barrier into the brain, where the bacteria multiply freely and trigger activation of circulating antigen-presenting cells and resident microglial cells. The resulting massive inflammation leads to further neutrophil recruitment and inflammation, resulting in the well-known features of bacterial meningitis, including cerebrospinal fluid pleocytosis, cochlear damage, cerebral edema, hydrocephalus, and cerebrovascular complications. Experimental animal models continue to further our understanding of the pathophysiology of pneumococcal meningitis and provide the platform for the development of new adjuvant treatments and antimicrobial therapy. This review discusses the most recent views on the pathophysiology of pneumococcal meningitis, as well as potential targets for (adjunctive) therapy.
Figures
Fig. 1.
(A) Mucus breakdown. S. pneumoniae colonization of the nasopharynx is facilitated by mucus degradation by the enzymes NanA, BgaA, StrH, and NanB. Ply decreases epithelial cell ciliary beating, enhancing bacterial adherence. (B) Evasion of proteolytic enzymes. Pneumococcal cell wall peptidoglycans may be destroyed by lysozyme. PdgA and Adr deacetylate pneumococcal cell surface petidoglycan molecules, rendering them resistant to lysozyme. (C) Epithelial cell binding. S. pneumoniae binds host GalNac by using SpxB, Smi, MsrA, and PlpA. (D) Intracellular translocation. By binding the pIgR with PspC (or PAF receptor [PAFr] with ChoP), pneumococci can use the pIgR or PAF receptor recycling pathway to be transported through the epithelial cell layer. (E) Inter- and pericellular translocation. Plasminogen bound by Gly3Ph, CbpE, and enolase enhances epithelial cell binding and degrades interepithelial adherens junctions, allowing pericellular migration.
Fig. 2.
S. pneumoniae adheres to endothelial cells by using PspC, which binds laminin and pIgR, enabling transcytosis across the endothelium. Once in the CSF, pneumococci multiply freely and release bacterial products such as LTA and Ply, which are recognized by TLR2 and TLR4 on circulating APCs. The subsequent release of proinflammatory cytokines and chemokines from macrophages and microglial cells results in upregulation of endothelial cell P- and E-selectin and ICAM (which binds MAC-1 on leukocytes), leading to increased neutrophil recruitment into the CSF.
Fig. 3.
Host pattern recognition receptors involved in sensing S. pneumoniae. TLR2 is activated by pneumococcal cell wall peptidoglycan and LTA. Nod2 is activated by cell wall peptidoglycans and TLR4, which in turn is activated by Ply. TLR2 and -4 activate the transcription factor NF-κB via MyD88 and IRAK-4. Nod2 also activates NF-κB, inducing transcription of several proinflammatory cytokines.
Fig. 4.
Neuronal damage and histopathology in humans with pneumococcal meningitis. The images show the histopathology of patients with bacterial meningitis, including parenchymal and meningeal hemorrhages (A), neutrophilic infiltration and arteritis obliterans (B), abscess formation and venous thrombosis (C), recent infarctions (D and E), and meningitis without cortical infiltration (F).
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