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Lectin-carbohydrate interactions: fine specificity difference between two mannose-binding proteins.

R T Lee¹, Y Shinohara, Y Hasegawa

¹Department of Biology, The Johns Hopkins University, Baltimore, MD 21218, USA. reiko.lee@jhu.edu

Bioscience Reports

|December 10, 1999

Summary

Rat mannose-binding proteins (MBPs) MBP-A and MBP-C bind mannose differently. MBP-C exhibits higher affinity for oligosaccharides due to an extended binding area and secondary site, unlike MBP-A which recognizes a single mannose residue.

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Area of Science:

Biochemistry
Structural Biology
Immunology

Background:

Two rat mannose-binding proteins (MBPs), serum type (MBP-A) and liver type (MBP-C), share similar binding specificity and structural features.
Despite similarities, MBP-A and MBP-C display distinct affinities for natural oligosaccharides and glycoproteins.

Purpose of the Study:

To elucidate the molecular basis for differential binding affinities between MBP-A and MBP-C.
To understand how structural variations influence the interaction with mannose-containing ligands.

Main Methods:

Utilized cloned fragments of the carbohydrate-recognition domain and connecting piece of MBP-A and MBP-C.
Conducted binding studies using various mannose-containing di- and tri-saccharides, and high-mannose type oligosaccharides.

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Analyzed binding interactions through structural and affinity assessments.

Main Results:

MBP-C demonstrated an extended binding area interacting with multiple mannose residues, unlike MBP-A which binds a single residue.
MBP-C possesses a secondary weak binding site located approximately 25 Å from the primary site.
MBP-C showed significantly higher affinity for natural high-mannose type oligosaccharides compared to MBP-A.

Conclusions:

The distinct binding modes, including extended interactions and secondary sites in MBP-C, explain its higher affinity for complex mannose structures.
Differences in subunit arrangement within MBP trimers may contribute to the observed affinity variations, particularly in steric-sensitive assays involving natural glycoproteins.