TY - JOUR
T1 - BPI-ANCA is found in reactive arthritis caused by Yersinia and Salmonella infection and recognise exclusively the C-terminal part of the BPI molecule
AU - Schultz, H.
AU - Csernok, E.
AU - Nikkari, S.
AU - Toivanen, P.
AU - Toivanen, A.
AU - Gross, W. L.
N1 - Funding Information:
This work was supported by DFG Grant Schu 1308/1-1 and by the Academy of Finland and EVO of Turku University Central Hospital.
Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2000
Y1 - 2000
N2 - Objective: To examine the prevalence, binding sites and functional interactions of antineutrophil cytoplasmic autoantibodies (ANCA) against the bactericidal/permeability increasing protein (BPI) in reactive arthritis (ReA). Methods: Sera were analysed for the occurrence of ANCA by indirect immunofluorescence microscopy (IIF) and ELISA. Binding sites were determined using BPI, lipopolysaccharid binding protein (LBP), and fusion proteins of both proteins in ELISA. In addition, the effect of antibodies on the antibiotic activity of BPI was examined. Results: BPI-ANCA was found in patients with Yersinia- and Salmonella-triggered ReA and directed against the C-terminal portion of BPI. Goat anti BPI antibodies recognising this part inhibited the antibiotic activity of BPI in vitro. Conclusion: BPI-ANCA was associated with ReA triggered by Salmonella and Yersinia infection. Directed against the C-terminal part of BPI, it can potentially inhibit its antibiotic activity and might be useful to identify patients with infectious bowel disease prone to extraintestinal sequelae.
AB - Objective: To examine the prevalence, binding sites and functional interactions of antineutrophil cytoplasmic autoantibodies (ANCA) against the bactericidal/permeability increasing protein (BPI) in reactive arthritis (ReA). Methods: Sera were analysed for the occurrence of ANCA by indirect immunofluorescence microscopy (IIF) and ELISA. Binding sites were determined using BPI, lipopolysaccharid binding protein (LBP), and fusion proteins of both proteins in ELISA. In addition, the effect of antibodies on the antibiotic activity of BPI was examined. Results: BPI-ANCA was found in patients with Yersinia- and Salmonella-triggered ReA and directed against the C-terminal portion of BPI. Goat anti BPI antibodies recognising this part inhibited the antibiotic activity of BPI in vitro. Conclusion: BPI-ANCA was associated with ReA triggered by Salmonella and Yersinia infection. Directed against the C-terminal part of BPI, it can potentially inhibit its antibiotic activity and might be useful to identify patients with infectious bowel disease prone to extraintestinal sequelae.
UR - http://www.scopus.com/inward/record.url?scp=0034538880&partnerID=8YFLogxK
U2 - 10.1080/030097400750041361
DO - 10.1080/030097400750041361
M3 - Journal articles
C2 - 11028843
AN - SCOPUS:0034538880
SN - 0300-9742
VL - 29
SP - 226
EP - 231
JO - Scandinavian Journal of Rheumatology
JF - Scandinavian Journal of Rheumatology
IS - 4
ER -