Lectins, proteins that are able to bind carbohydrate structures, are typically involved in cell recognition mechanisms. We demonstrate here that TBF-1, the main soluble protein in the Tuber borchii Vittad. fruiting body, is a phase-specific lectin that is able selectively to bind the exopolysaccharides produced by ascoma associated Rhizobium spp. Characterization of TBF-1 was performed using both the protein purified from the truffles and the recombinant protein overexpressed in Escherichia coli. The two proteins exhibit the same hemagglutination activity toward rabbit red blood cells and the same sugar binding specificity. The discovery of lectin activity for TBF-1 led us to propose revising the protein name to ‘T. borchii fruiting body lectin 1’ with the acronym TBFL-1.
The Tuber borchii fruiting body-specific protein TBF-1, is a novel lectin which interacts with associated Rhizobium species
PALMA, FRANCESCO;BARBIERI, ELENA;BUFFALINI, MICHELE;STOCCHI, VILBERTO
2008
Abstract
Lectins, proteins that are able to bind carbohydrate structures, are typically involved in cell recognition mechanisms. We demonstrate here that TBF-1, the main soluble protein in the Tuber borchii Vittad. fruiting body, is a phase-specific lectin that is able selectively to bind the exopolysaccharides produced by ascoma associated Rhizobium spp. Characterization of TBF-1 was performed using both the protein purified from the truffles and the recombinant protein overexpressed in Escherichia coli. The two proteins exhibit the same hemagglutination activity toward rabbit red blood cells and the same sugar binding specificity. The discovery of lectin activity for TBF-1 led us to propose revising the protein name to ‘T. borchii fruiting body lectin 1’ with the acronym TBFL-1.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
