Distinct Pathways of Mannan-Binding Lectin (MBL)- and C1-Complex Autoactivation Revealed by Reconstitution of MBL with Recombinant MBL-Associated Serine Protease-2 | Zendy

Thomas VorupJensen | Zendy; Steen V. Petersen | Zendy; Annette G. Hansen | Zendy; Knud Poulsen | Zendy; Wilhelm Schwaeble | Zendy; Robert B. Sim | Zendy; Kenneth B. M. Reid | Zendy; Simon J. Davis | Zendy; Steffen Thiel | Zendy; Jens C. Jensenius | Zendy

Open Access

Distinct Pathways of Mannan-Binding Lectin (MBL)- and C1-Complex Autoactivation Revealed by Reconstitution of MBL with Recombinant MBL-Associated Serine Protease-2

Author(s) -

Thomas VorupJensen,

Steen V. Petersen,

Annette G. Hansen,

Knud Poulsen,

Wilhelm Schwaeble,

Robert B. Sim,

Kenneth B. M. Reid,

Simon J. Davis,

Steffen Thiel,

Jens C. Jensenius

Publication year - 2000

Publication title -

the journal of immunology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.737

H-Index - 372

eISSN - 1550-6606

pISSN - 0022-1767

DOI - 10.4049/jimmunol.165.4.2093

Subject(s) - mannan binding lectin , lectin pathway , proteases , complement system , serine protease , serine , complement component 2 , masp1 , collectin , lectin , ficolin , biology , classical complement pathway , alternative complement pathway , innate immune system , protease , c type lectin , biochemistry , enzyme , immunology , immune system , receptor

Mannan-binding lectin (MBL) plays a pivotal role in innate immunity by activating complement after binding carbohydrate moieties on pathogenic bacteria and viruses. Structural similarities shared by MBL and C1 complexes and by the MBL- and C1q-associated serine proteases, MBL-associated serine protease (MASP)-1 and MASP-2, and C1r and C1s, respectively, have led to the expectation that the pathways of complement activation by MBL and C1 complexes are likely to be very similar. We have expressed rMASP-2 and show that, whereas C1 complex autoactivation proceeds via a two-step mechanism requiring proteolytic activation of both C1r and C1s, reconstitution with MASP-2 alone is sufficient for complement activation by MBL. The results suggest that the catalytic activities of MASP-2 split between the two proteases of the C1 complex during the course of vertebrate complement evolution.

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