Toward a structure-based comprehension of the lectin pathway of complement

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

To initiate the lectin pathway of complement pattern recognition molecules bind to surface-linked carbohydrates or acetyl groups on pathogens or damaged self-tissue. This leads to activation of the serine proteases MASP-1 and MASP-2 resulting in deposition of C4 on the activator and assembly of the C3 convertase. In addition MASP-3 and the non-catalytic MAp19 and MAp44 presumably play regulatory functions, but the exact function of the MASP-3 protease remains to be established. Recent functional studies have significantly advanced our understanding of the molecular events occurring as activation progresses from pattern recognition to convertase assembly. Furthermore, atomic structures derived by crystallography or solution scattering of most proteins acting in the lectin pathway and two key complexes have become available. Here we integrate the current functional and structural knowledge concerning the lectin pathway proteins and derive overall models for their glycan bound complexes. These models are used to discuss cis- versus trans-activation of MASP proteases and the geometry of C4 deposition occurring on glycans in the lectin pathway.
Original languageEnglish
JournalMolecular Immunology
Volume56
Issue3
Pages (from-to)222-231
Number of pages10
ISSN0161-5890
DOIs
Publication statusPublished - 15 Dec 2013
Event14th European Meeting on Complement in Human Disease - , Germany
Duration: 17 Aug 201321 Aug 2013

Conference

Conference14th European Meeting on Complement in Human Disease
CountryGermany
Period17/08/201321/08/2013

    Research areas

  • Animals, Complement Activation, Complement C4, Complement Pathway, Mannose-Binding Lectin, Complement System Proteins, Humans, Mannose-Binding Protein-Associated Serine Proteases

See relations at Aarhus University Citationformats

Download statistics

No data available

ID: 68706890