| Autor: |
Reichhardt MP; Infection Biology Research Program, Department of Bacteriology and Immunology, Haartman Institute, University of Helsinki, Helsinki, Finland., Loimaranta V, Thiel S, Finne J, Meri S, Jarva H |
| Jazyk: |
angličtina |
| Zdroj: |
Frontiers in immunology [Front Immunol] 2012 Jul 16; Vol. 3, pp. 205. Date of Electronic Publication: 2012 Jul 16 (Print Publication: 2012). |
| DOI: |
10.3389/fimmu.2012.00205 |
| Abstrakt: |
The salivary scavenger and agglutinin (SALSA), also known as gp340, salivary agglutinin and deleted in malignant brain tumor 1, is a 340-kDa glycoprotein expressed on mucosal surfaces and secreted into several body fluids. SALSA binds to a broad variety of microbes and endogenous ligands, such as complement factor C1q, surfactant proteins D and A, and IgA. Our search for novel ligands of SALSA by direct protein-interaction studies led to the identification of mannan-binding lectin (MBL) as a new binding partner. We observed that surface-associated SALSA activates complement via binding of MBL. On the other hand, soluble SALSA was found to inhibit Candida albicans-induced complement activation. Thus, SALSA has a dual complement activation modifying function. It activates the lectin pathway when bound to a surface and inhibits it when free in the fluid phase. These activities are mediated via a direct interaction with MBL. This suggests that SALSA could target the innate immune responses to certain microorganisms and simultaneously limit complement activation in the fluid phase. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
