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Gene Review

Mbl1  -  mannose-binding lectin (protein A) 1

Rattus norvegicus

Synonyms: MBP-A, Mannan-binding protein, Mannose-binding protein A, Mbpa, Mlb1
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Disease relevance of Mbl1


High impact information on Mbl1

  • The activity of MBP-A in a hemolytic complement fixation assay using mannan-coated sheep erythrocytes was approximately 20-fold greater than the activity of MBP-C [2].
  • Rat serum mannose-binding protein (MBP-A) functions as part of the innate immune system by targetting complement toward potentially pathogenic microorganisms [2].
  • In order to examine the molecular basis for complement activation, rat MBP-A has been overproduced in Chinese hamster ovary cells [2].
  • Analysis of wild-type MBP-A and MBP-A containing the substitution Cys6 --> Ser suggests that polypeptides within each trimeric structural unit are mostly linked by disulfide bonds between cysteine residues at positions 13 and 18 arranged in an asymmetrical configuration [2].
  • Ligand-binding characteristics of rat serum-type mannose-binding protein (MBP-A). Homology of binding site architecture with mammalian and chicken hepatic lectins [3].

Biological context of Mbl1

  • The carbohydrate-binding portion of MBP-A is encoded by the remaining two exons [4].
  • This gene, which encodes the minor form of binding protein (designated MBP-A), has been characterized by sequence analysis [4].
  • The protein-coding portion of the mRNA for the MBP-A is encoded by four exons separated by three introns [4].
  • From these and other data, we postulate that the binding site of MBP-C has an extended area of interaction, probably the size of a mannotriose, while MBP-A interacts essentially with one mannose residue [5].
  • This study demonstrates that the amino acid residues 174-194 of SP-A and the corresponding region of MBP-A are critical for SP-A-type II cell interaction and Ca2+-dependent lipid binding of collectins [6].

Associations of Mbl1 with chemical compounds

  • The structure was solved by molecular replacement using rat serum mannose-binding protein (MBP-A) as a search model and was refined to maximum Bragg spacings of 1.7 A [7].
  • In contrast, the serum-type MBP CRD of rat (MBP-A) bound all the methyl glycosides of manno-oligosaccharide and methyl alpha-mannopyranoside with similar affinities [5].
  • It has previously been shown that MBP-A binds to a range of monosaccharide-bovine serum albumin conjugates, and that, among oligosaccharide ligands tested, preferential binding is to terminal nonreducing N-acetylglucosamine residues of complex type N-linked oligosaccharides [8].
  • Since LPS was also a ligand for the collectins, we compared the characteristics of binding of MBP-A to LPS with those of binding to CD14 [1].
  • SP-A binds to dipalmitoyl phosphatidylcholine (DPPC) and galactosylceramide (GalCer) and MBP-A binds to phosphatidylinositol (PI) [6].

Other interactions of Mbl1

  • It appears that the three COOH-terminal exons of the asialoglycoprotein receptor gene have been fused into a single exon in the MBP-A gene [4].
  • These structures explain how MBPs recognize a wide range of monosaccharides and suggest how fine specificity differences between MBP-A and MBP-C may be achieved [7].

Analytical, diagnostic and therapeutic context of Mbl1

  • Gel filtration, chemical cross-linking, and crystallographic self-rotation function analyses indicate that the subtilisin fragment is a dimer, although the complete bacterially expressed fragment, containing the neck and CRD of MBP-A, is a trimer [9].


  1. Rat mannose-binding protein a binds CD14. Chiba, H., Sano, H., Iwaki, D., Murakami, S., Mitsuzawa, H., Takahashi, T., Konishi, M., Takahashi, H., Kuroki, Y. Infect. Immun. (2001) [Pubmed]
  2. Molecular determinants of oligomer formation and complement fixation in mannose-binding proteins. Wallis, R., Drickamer, K. J. Biol. Chem. (1999) [Pubmed]
  3. Ligand-binding characteristics of rat serum-type mannose-binding protein (MBP-A). Homology of binding site architecture with mammalian and chicken hepatic lectins. Lee, R.T., Ichikawa, Y., Fay, M., Drickamer, K., Shao, M.C., Lee, Y.C. J. Biol. Chem. (1991) [Pubmed]
  4. Exon structure of a mannose-binding protein gene reflects its evolutionary relationship to the asialoglycoprotein receptor and nonfibrillar collagens. Drickamer, K., McCreary, V. J. Biol. Chem. (1987) [Pubmed]
  5. Difference in binding-site architecture of the serum-type and liver-type mannose-binding proteins. Lee, R.T., Lee, Y.C. Glycoconj. J. (1997) [Pubmed]
  6. Introduction of mannose binding protein-type phosphatidylinositol recognition into pulmonary surfactant protein A. Chiba, H., Sano, H., Saitoh, M., Sohma, H., Voelker, D.R., Akino, T., Kuroki, Y. Biochemistry (1999) [Pubmed]
  7. Structural analysis of monosaccharide recognition by rat liver mannose-binding protein. Ng, K.K., Drickamer, K., Weis, W.I. J. Biol. Chem. (1996) [Pubmed]
  8. Differential recognition of core and terminal portions of oligosaccharide ligands by carbohydrate-recognition domains of two mannose-binding proteins. Childs, R.A., Feizi, T., Yuen, C.T., Drickamer, K., Quesenberry, M.S. J. Biol. Chem. (1990) [Pubmed]
  9. Physical characterization and crystallization of the carbohydrate-recognition domain of a mannose-binding protein from rat. Weis, W.I., Crichlow, G.V., Murthy, H.M., Hendrickson, W.A., Drickamer, K. J. Biol. Chem. (1991) [Pubmed]
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