Presence of vitronectin and activated complement factor C9 on ventriculoperitoneal shunts and temporary ventricular drainage catheters

Citation
F. Lundberg et al., Presence of vitronectin and activated complement factor C9 on ventriculoperitoneal shunts and temporary ventricular drainage catheters, J NEUROSURG, 90(1), 1999, pp. 101-108
Citations number
39
Categorie Soggetti
Neurology,"Neurosciences & Behavoir
Journal title
JOURNAL OF NEUROSURGERY
ISSN journal
00223085 → ACNP
Volume
90
Issue
1
Year of publication
1999
Pages
101 - 108
Database
ISI
SICI code
0022-3085(199901)90:1<101:POVAAC>2.0.ZU;2-E
Abstract
Object. The pathogenesis of cerebrospinal fluid (CSF) shunt infection is ch aracterized by staphylococcal adhesion to the polymeric surface of the shun t catheter. Proteins from the CSF-fibronectin, vitronectin, and fibrinogen- are adsorbed to the surface of the catheter immediately after insertion. Th ese proteins can interfere with the biological systems of the host and medi ate staphylococcal adhesion to the surface of the catheter. In the present study, the presence of fibronectin, vitronectin, and fibrinogen on CSF shun ts and temporary ventricular drainage catheters is shown. The presence of f ragments of fibrinogen is also examined. Methods. The authors used the following methods: binding radiolabeled antib odies to the catheter surface, immunoblotting of catheter eluates, and scan ning force microscopy of immunogold bound to the catheter surface. The immu noblot showed that vitronectin was adsorbed in its native form and that fib ronectin was degraded into small fragments. Furthermore, the study demonstr ated that the level of vitronectin in CSF increased in patients with an imp aired CSF-blood barrier. To study complement activation, an antibody that r ecognizes the neoepitope of activated complement factor C9 was used. The pr esence of activated complement factor C9 was shown on both temporary cathet ers and shunts. Conclusions. Activation of complement close to the surface of an inserted c atheter could contribute to the pathogenesis of CSP shunt infection.