Mannose binding lectin is required for alphavirus-induced arthritis/myositis.
Authors: Gunn BM, Morrison TE, Whitmore AC
PLoS Pathog., 2012;8(3):e1002586.
Species: Mouse
Sample Type: Tissue Homogenates
Application: WB
Transglutaminase is essential for IgA nephropathy development acting through IgA receptors.
Authors: Berthelot L, Papista C, Maciel TT, Biarnes-Pelicot M, Tissandie E, Wang PH, Tamouza H, Jamin A, Bex-Coudrat J, Gestin A, Boumediene A, Arcos-Fajardo M, England P, Pillebout E, Walker F, Daugas E, Vrtosvnik F, Flamant M, Benhamou M, Cogne M, Moura IC, Monteiro RC
J. Exp. Med., 2012;209(4):793-806.
Species: Mouse
Sample Type: Whole Tissue
Application: IHC Frozen

Mannan binding lectin (MBL) belongs to the collectin family of innate immune defense proteins, which binds to an array of carbohydrate patterns on pathogen surfaces (1, 2). Collectin family members share common structural features: a cysteine rich amino-terminal domain, a collagen-like region, an alpha -helical coiled-coil neck domain and a carboxy terminal C-type (Ca⁺⁺-dependent) lectin or carbohydrate recognition domain (CRD). MBL homotrimerizes to form a structural unit joined by N-terminal disulfide bridges. These homotrimers further associate into oligomeric structures of up to 6 units. Whereas two forms of MBL proteins (MBL-1, also known as S-MBP or MBL-A and MBL-2, also known as L-MBP or MBL-C) exist in rodents and other animals, only one functional MBL protein is present in humans. Mouse MBL-1 shares about 52% and 60% amino acid sequence identity with mouse MBL-2 and human MBL, respectively.

In mouse, MBL-1 and MBL-2 are the only collectins that can activate complement via the lectin complement pathway (1, 2). Serum oligomeric MBL associates with MBL-associated serine protease (MASP) proenzymes. The MBL-MASP proenzyme complex preferentially interacts with sugar patterns containing mannose, glucose,
L‑fucose, or N-acetyl-glucosamine present at a terminal nonreducing postion on the cell surface of various pathogens and certain tumor cells. This interaction induces pro-enzyme activation and the triggering of the complement cascade, resulting in opsonization and pathogen removal via humoral and cellular immune responses. MBL does not recognize self-components or glycoproteins from other higher animals due to the presence of terminal sialic acid or galactose that interrupts the repeating carbohydrate structures (3). A number of membrane receptors for MBL, including C1q phagocytic receptor (C1qRp), calreticulin (also known as C1qR), and CR1 (CD35), have been described. Interactions with these receptors may also be important in stimulating phagocytosis (1, 2).

Mouse MBL-1 and MBL-2 are produced primarily in the liver and are secreted into the blood stream. In addition, mouse MBL-1 is also expressed in lung, kidney and testis while MBL-2 is expressed in kidney, thymus, and small intestine (1, 4, 5).

1. Holmskov, U. et al. (2003) Annu. Rev. Immunol. 21:547. 
2. Fujita, R. et al. (2004) Immunol. Rev. 198:185.
3. Saevarsdottir, S. et al. (2004) Scand. J. Immnunol. 60:23.
4. Uemura, K. et al. (2002) J. Immunol. 169:6945.
5. Wagner, S. et al. (2003) J. Immunol. 170:1462.