LECTINS FROM THE COLONIAL TUNICATE CLAVELINA PICTA ARE STRUCTURALLY RELATED TO ACUTE-PHASE REACTANTS FROM VERTEBRATES

ELOLA, M. T.; VASTA, G. R.

ANNALS OF THE NEW YORK ACADEMY OF SCIENCES.

BLACKWELL PUBLISHING

Lugar: Oxford; Año: 1994 vol. 712 p. 321 - 323

0077-8923

The presence of carbohydrate-binding molecules in invertebrates is well documented.’ Nevertheless, few agglutinins have been purified and fully characterized in their biochemical properties and molecular structure. From those taxa for which structural information is available, namely molluscs, arthropods, and sponges, most lectins are multivalent, oligomeric proteins or glycoproteins with binding sites for relatively small carbohydrate moieties.2 Considerably less is known about the protochordates and echinoderms, despite their close affinity to the vertebrates. We have concentrated our efforts on examining the structural and functional features and evolutionary relationships between lectins from selected protochordate and echinoderm species and “nonspecific” recognition molecules from vertebrates such as acute-phase reactants, in particular C-type lectins; members of the pentraxin family such as C-reactive protein (CRP); serum amyloid P (SAP) and serum amyloid A; and coagulation factor VIIIc. In this paper we describe the purification and biochemical characterization of four distinct fucosyl-binding lectins from the colonial tunicate Clavelina picta, and their structural and serological relationships with acute-phase proteins.