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Jens Christian Jensenius

Mannan-binding lectin activates C3 and the

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

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Mannan-binding lectin activates C3 and the. / Selander, B.; Martensson, U.; Weintraub, A.; Holmstrom, E.; Matsushita, M.; Thiel, Steffen; Jensenius, Jens Christian; Truedsson, L.; Sjoholm, A.G.

In: J. Clin. Invest., Vol. 116, 2006, p. 1425-34.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Selander, B, Martensson, U, Weintraub, A, Holmstrom, E, Matsushita, M, Thiel, S, Jensenius, JC, Truedsson, L & Sjoholm, AG 2006, 'Mannan-binding lectin activates C3 and the', J. Clin. Invest., vol. 116, pp. 1425-34.

APA

Selander, B., Martensson, U., Weintraub, A., Holmstrom, E., Matsushita, M., Thiel, S., Jensenius, J. C., Truedsson, L., & Sjoholm, A. G. (2006). Mannan-binding lectin activates C3 and the. J. Clin. Invest., 116, 1425-34.

CBE

Selander B, Martensson U, Weintraub A, Holmstrom E, Matsushita M, Thiel S, Jensenius JC, Truedsson L, Sjoholm AG. 2006. Mannan-binding lectin activates C3 and the. J. Clin. Invest. 116:1425-34.

MLA

Selander, B. et al. "Mannan-binding lectin activates C3 and the". J. Clin. Invest. 2006, 116. 1425-34.

Vancouver

Selander B, Martensson U, Weintraub A, Holmstrom E, Matsushita M, Thiel S et al. Mannan-binding lectin activates C3 and the. J. Clin. Invest. 2006;116:1425-34.

Author

Selander, B. ; Martensson, U. ; Weintraub, A. ; Holmstrom, E. ; Matsushita, M. ; Thiel, Steffen ; Jensenius, Jens Christian ; Truedsson, L. ; Sjoholm, A.G. / Mannan-binding lectin activates C3 and the. In: J. Clin. Invest. 2006 ; Vol. 116. pp. 1425-34.

Bibtex

@article{0c4a64b059e011dbbee902004c4f4f50,
title = "Mannan-binding lectin activates C3 and the",
abstract = "Lectin pathway activation of C3 is known to involve target recognition by mannan-binding lectin (MBL) or ficolins and generation of classical pathway C3 convertase via cleavage of C4 and C2 by MBL-associated serine protease 2 (MASP-2). We investigated C3 activation in C2-deficient human sera and in sera with other defined defects of complement to assess other mechanisms through which MBL might recruit complement. The capacity of serum to support C3 deposition was examined by ELISA using microtiter plates coated with O antigen-specific oligosaccharides derived from Salmonella typhimurium, S. thompson, and S. enteritidis corresponding to serogroups B, C, and D (BO, CO, and DO). MBL bound to CO, but not to BO and DO, and efficiently supported C3 deposition in the absence of C2, C4, or MASP-2. The existence of an MBL-dependent C2 bypass mechanism for alternative pathway-mediated C3 activation was clearly demonstrated using CO, solid-phase mannan, and E. coli LPS. MASP-1 might contribute, but was not required for C3 deposition in the model used. Independent of MBL, specific antibodies to CO supported C3 deposition through classical and alternative pathways. MBL-dependent C2 bypass activation could be particularly important in various inherited and acquired complement deficiency states.",
author = "B. Selander and U. Martensson and A. Weintraub and E. Holmstrom and M. Matsushita and Steffen Thiel and Jensenius, {Jens Christian} and L. Truedsson and A.G. Sjoholm",
year = "2006",
language = "English",
volume = "116",
pages = "1425--34",
journal = "J. Clin. Invest.",

}

RIS

TY - JOUR

T1 - Mannan-binding lectin activates C3 and the

AU - Selander, B.

AU - Martensson, U.

AU - Weintraub, A.

AU - Holmstrom, E.

AU - Matsushita, M.

AU - Thiel, Steffen

AU - Jensenius, Jens Christian

AU - Truedsson, L.

AU - Sjoholm, A.G.

PY - 2006

Y1 - 2006

N2 - Lectin pathway activation of C3 is known to involve target recognition by mannan-binding lectin (MBL) or ficolins and generation of classical pathway C3 convertase via cleavage of C4 and C2 by MBL-associated serine protease 2 (MASP-2). We investigated C3 activation in C2-deficient human sera and in sera with other defined defects of complement to assess other mechanisms through which MBL might recruit complement. The capacity of serum to support C3 deposition was examined by ELISA using microtiter plates coated with O antigen-specific oligosaccharides derived from Salmonella typhimurium, S. thompson, and S. enteritidis corresponding to serogroups B, C, and D (BO, CO, and DO). MBL bound to CO, but not to BO and DO, and efficiently supported C3 deposition in the absence of C2, C4, or MASP-2. The existence of an MBL-dependent C2 bypass mechanism for alternative pathway-mediated C3 activation was clearly demonstrated using CO, solid-phase mannan, and E. coli LPS. MASP-1 might contribute, but was not required for C3 deposition in the model used. Independent of MBL, specific antibodies to CO supported C3 deposition through classical and alternative pathways. MBL-dependent C2 bypass activation could be particularly important in various inherited and acquired complement deficiency states.

AB - Lectin pathway activation of C3 is known to involve target recognition by mannan-binding lectin (MBL) or ficolins and generation of classical pathway C3 convertase via cleavage of C4 and C2 by MBL-associated serine protease 2 (MASP-2). We investigated C3 activation in C2-deficient human sera and in sera with other defined defects of complement to assess other mechanisms through which MBL might recruit complement. The capacity of serum to support C3 deposition was examined by ELISA using microtiter plates coated with O antigen-specific oligosaccharides derived from Salmonella typhimurium, S. thompson, and S. enteritidis corresponding to serogroups B, C, and D (BO, CO, and DO). MBL bound to CO, but not to BO and DO, and efficiently supported C3 deposition in the absence of C2, C4, or MASP-2. The existence of an MBL-dependent C2 bypass mechanism for alternative pathway-mediated C3 activation was clearly demonstrated using CO, solid-phase mannan, and E. coli LPS. MASP-1 might contribute, but was not required for C3 deposition in the model used. Independent of MBL, specific antibodies to CO supported C3 deposition through classical and alternative pathways. MBL-dependent C2 bypass activation could be particularly important in various inherited and acquired complement deficiency states.

M3 - Journal article

VL - 116

SP - 1425

EP - 1434

JO - J. Clin. Invest.

JF - J. Clin. Invest.

ER -