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TitleAltering the carbohydrate-binding specificity of the legume lectin FRIL through structure-guided engineering.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Year 2026
Publish dateMar 5, 2026
AuthorsYo-Min Liu / Hong Thuy Vy Nguyen / Xiaorui Chen / Md Shahed-Al-Mahmud / Ting-Hua Chen / Kuo-Shiang Liao / Jennifer M Lo / Tzu-Chun Kan / Chien-Tai Ren / Che Ma /
PubMed AbstractFRIL is a legume lectin from the hyacinth bean that has broad-spectrum antiviral activity. A distinctive trait of FRIL among similar mannose/glucose-specific legume lectins is that FRIL shows ...FRIL is a legume lectin from the hyacinth bean that has broad-spectrum antiviral activity. A distinctive trait of FRIL among similar mannose/glucose-specific legume lectins is that FRIL shows specificity for complex type N-glycans. We postulate that an extended binding site on FRIL facilitates this ligand selectivity. Here, we show legume lectin carbohydrate recognition domain (CRD) loop B is the main determinant of complex versus high-mannose N-glycan specificity in FRIL and Concanavalin A (ConA), respectively. First, we find that the inactive precursors of recombinant FRIL (rFRIL) and proConA (rproConA) can be activated via deglycosylation. Secondly, the cryo-EM structures of inactive apo rFRIL, active FRIL in complex with Galβ1,4-(Fucα1,3-)GlcNAcβ1,2-Man tetrasaccharide, and active rFRIL in complex with MannoseGlcNAc (Man9) N-glycan are determined, and residues H102 and Y101 on loop B are identified as crucial for complex glycan recognition. Finally, we swapped loop B residues 101 and 102 alongside loop C residue 145 on FRIL to their structural equivalent on ConA, resulting in a FRIL mutant that binds exclusively to high mannose N-glycans. Taken together, we have established a process of activating recombinant FRIL and related lectins through deglycosylation, and demonstrated the crucial role that loop B residues play in establishing oligosaccharide specificity.
External linksNat Commun / PubMed:41786775 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.4 - 2.67 Å
Structure data

64935

9vbx

EMDB-64935, PDB-9vbx:
Lectin FRIL from Lablab purpureus complexed to Lewis X tetrasaccharide
Method: EM (single particle) / Resolution: 2.4 Å

64936

9vby

EMDB-64936, PDB-9vby:
Lectin FRIL from Lablab purpureus with self glycan
Method: EM (single particle) / Resolution: 2.67 Å

64937

9vbz

EMDB-64937, PDB-9vbz:
Lectin FRIL from Lablab purpureus complexed to oligomannose
Method: EM (single particle) / Resolution: 2.56 Å

64938

9vc0

EMDB-64938, PDB-9vc0:
Lectin FRIL from Lablab purpureus complexed to oligomannose
Method: EM (single particle) / Resolution: 2.48 Å

PDB-9vbw:
Lectin FRIL from Lablab purpureus complexed to Lewis X tetrasaccharide
Method: X-RAY DIFFRACTION / Resolution: 2.49 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-MN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • lablab purpureus (hyacinth bean)
KeywordsPLANT PROTEIN / Flt3 receptor-interacting lectin / carbohydrate binding protein / lectin / glycoprotein / complex type glycan / FRIL / self glycan / high-mannose type glycan. OMS-FRIL

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