Mannan-binding lectin

Mannan-binding lectin 59 Mannose-binding lectin, MBL, MBP, rarf(p28)... 

Yamaguchi, M., Ogawa, T., Muramoto, K., Ka-mio, Y, Jimbo, M., Kamiya, H. Isolation and characterization of a mannan-binding lectin from the freshwater cyanobacterium (blue-green algae) Microcystis viridis. Biochem. Bio-phys. Res. Commun. 1999, 265, 703-708... 

Thiel S, Vorup-Jensen T, Stover CM, Schwaeble W, Laursen SB, Paulsen K, Willis AC, Eggleton P, Hamsen S, Holmskov U et al (1997) A second serine protease associated with mannan-binding lectin that activates complement. Nature 386 506-510... 

Evolutionary conservation of mannan-binding lectin (MBL) in bony fish identification, characterization and expression analysis of three bona fide coUectin homologues of MBL in the rainbow trout (Onchorhynchus mykiss) ,Fish Shellfish... 

D. Page, D. Zanini, and R. Roy, Macromolecular recognition Effect of multivalency in the inhibition of binding of yeast mannan to concanavalin A and pea lectins by mannosylated dendrimers, Bioorg. Med. Chem., 4 (1996) 1949-1961. 

A fluorescent tag (fluorescein isothiocyanate) attached to the lectin Concanavalin A is useful in staining yeast cell wall fragments (Siebert et al., 1981). Concanavalin A specifically binds to mannan, which is prominent in yeast cell walls. 

Christensen et al. [93] successfully obtained a divalent cluster having -600-1500 enhanced binding properties. We have also demonstrated that dendritic mannosides such as 66 (Scheme 11) can provide up to 100-fold higher affinity (on a per-mannoside basis) when used to inhibit the binding of plant lectins (Concanavalin A and pea lectins) to yeast mannan [85]. As these interactions are at the origin of host infections by fimbriated bacteria, mannoside dendrimers can form the basis of novel antiadhesin molecules. 

Metal analysis revealed one atom of Mn2+ and six atoms of Ca2+ associated with each 66.5 kg of protein.142 Addition of 5 mM Ca2+ and mM Mn2+ to the native lectins enhanced both hemagglutination and mannan precipitation. This indicates that either some metal loss occurred during purification, or that the metal binding-sites are never completely occupied442 (compare Refs. 300 and 301). Mn2+ stimulated the hemagglutinating activity of all lentil-lectin preparations more than did Ca2+, whereas Ca2+ promoted mannan precipitation more effectively.442 Demetallization, by dialysis against 0.1 M EDTA followed by M acetic... 

The mechanism of lectin-like cell-cell interactions has been established to explain yeast flocculation (Speers et al., 1998). Lectins are a structurally diverse group of proteins that are capable of binding carbohydrates while zymolectin is an anchored yeast cell wall protein that contains one or more mannose binding sites (Boulton Quain, 2001). This mechanism proposes that specific surface proteins known as zymolectins, which are present on flocculent yeast cells, bind to mannose residues of mannan molecules on neighbouring cell surfaces (Speers et al., 1998). The involvement of this protein-carbohydrate interaction was suggested by Taylor and Orton (Taylor Orton, 1978), as flocculation can be inhibited specifically by mannose. 

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