In a full-length cDNA library from the compound ascidian Botryllus schlosseri, we identified, by BLAST search against UniProt database, five transcripts, each with complete coding sequence, homologous to known rhamnose-binding lectins (RBLs). Comparisons of the predicted amino acid sequences suggest that they represent different isoforms of a novel RBL, called BsRBL-1–5. Four of these isolectins were found in Botryllus homogenate after purification by affinity chromatography on acid-treated Sepharose, analysis by reverse-phase HPLC and mass spectrometry. Analysis of both molecular masses and tryptic digests of BsRBLs indicated that the N-terminal sequence of the purified proteins starts from residue 22 of the putative amino acid sequence, and residues 1–21 represent a signal peptide. Analysis by mass spectrometry of V8-protease digests confirmed the presence and alignments of the eight cysteines involved in the disulphide bridges that characterise RBLs. Functional studies proved the enhancing effect on phagocytosis of the affinity-purified material. Results are discussed in terms of phylogenetic relationships of BsRBLs with orthologous molecules from protostomes and deuterostomes.

Novel rhamnose-binding lectins from the colonial ascidian Botryllus schlosseri / Gasparini, Fabio; Franchi, Nicola; Spolaore, Barbara; Ballarin, Loriano. - In: DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY. - ISSN 0145-305X. - 32:(2008), pp. 1177-1191. ((Intervento presentato al convegno IX Convegno della Società Italiana di Immunologia Comparata e dello Sviluppo (SIICS) tenutosi a Varese nel 27-29 febbraio [10.1016/j.dci.2008.03.006].

Novel rhamnose-binding lectins from the colonial ascidian Botryllus schlosseri

FRANCHI, NICOLA;
2008

Abstract

In a full-length cDNA library from the compound ascidian Botryllus schlosseri, we identified, by BLAST search against UniProt database, five transcripts, each with complete coding sequence, homologous to known rhamnose-binding lectins (RBLs). Comparisons of the predicted amino acid sequences suggest that they represent different isoforms of a novel RBL, called BsRBL-1–5. Four of these isolectins were found in Botryllus homogenate after purification by affinity chromatography on acid-treated Sepharose, analysis by reverse-phase HPLC and mass spectrometry. Analysis of both molecular masses and tryptic digests of BsRBLs indicated that the N-terminal sequence of the purified proteins starts from residue 22 of the putative amino acid sequence, and residues 1–21 represent a signal peptide. Analysis by mass spectrometry of V8-protease digests confirmed the presence and alignments of the eight cysteines involved in the disulphide bridges that characterise RBLs. Functional studies proved the enhancing effect on phagocytosis of the affinity-purified material. Results are discussed in terms of phylogenetic relationships of BsRBLs with orthologous molecules from protostomes and deuterostomes.
32
1177
1191
Novel rhamnose-binding lectins from the colonial ascidian Botryllus schlosseri / Gasparini, Fabio; Franchi, Nicola; Spolaore, Barbara; Ballarin, Loriano. - In: DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY. - ISSN 0145-305X. - 32:(2008), pp. 1177-1191. ((Intervento presentato al convegno IX Convegno della Società Italiana di Immunologia Comparata e dello Sviluppo (SIICS) tenutosi a Varese nel 27-29 febbraio [10.1016/j.dci.2008.03.006].
Gasparini, Fabio; Franchi, Nicola; Spolaore, Barbara; Ballarin, Loriano
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11380/1252908
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