Lynch, Nicholas J. and Roscher, Silke and Hartung, Thomas and Morath, Siegfried and Matsushita, Misao and Maennel, Daniela N. and Kuraya, Mikio and Fujita, Teizo and Schwaeble, Wilhelm J. (2004) L-ficolin specifically binds to lipoteichoic acid, a cell wall constituent of gram-positive bacteria, and activates the lectin pathway of complement. JOURNAL OF IMMUNOLOGY, 172 (2). pp. 1198-1202. ISSN 0022-1767, 1550-6606
Full text not available from this repository. (Request a copy)Abstract
The lectin pathway of complement is activated when a carbohydrate recognition complex and associated serine proteases binds to the surface of a pathogen. Three recognition subcomponents have been shown to form active initiation complexes: mannan-binding lectin (MBL), L-ficolin, and H-ficolin. The importance of MBL in antimicrobial host defense is well recognized, but the role of the ficolins remains largely undefined. This report shows that L-ficolin specifically binds to lipoteichoic acid (LTA), a cell wall component found in all Gram-positive bacteria. Immobilized LTA from Staphylococcus aureus binds L-ficolin complexes from sera, and these complexes initiate lectin pathway-dependent C4 turnover. C4 activation correlates with serum L-ficolin concentration, but not with serum MBL levels. L-ficolin binding and corresponding levels of C4 turnover were observed on LTA purified from other clinically important bacteria, including Streptococcus pyogenes and Streptococcus agalactiae. None of the LTA. preparations bound MBL, H-ficolin, or the classical pathway recognition molecule, C1q. The Journal of Immunology, 2004, 172: 1198-1202.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SERINE-PROTEASE; STAPHYLOCOCCUS-AUREUS; HAKATA ANTIGEN; SERUM LECTIN; OPSONOPHAGOCYTOSIS; ASSOCIATION; COMPONENTS; COMPLEXES; FAMILY; MEMBER; |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Immunologie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 02 Aug 2021 11:24 |
| Last Modified: | 02 Aug 2021 11:24 |
| URI: | https://pred.uni-regensburg.de/id/eprint/38078 |
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