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Isolectins from Solanum tuberosum with different detailed carbohydrate binding specificities: unexpected recognition of lactosylceramide by N-acetyllactosamine-binding lectins.

Artikel i vetenskaplig tidskrift
Författare J Ciopraga
Jonas Ångström
Jörgen Bergström
Thomas Larsson
Niclas G. Karlsson
C Motas
O Gozia
Susann Teneberg
Publicerad i Journal of biochemistry
Volym 128
Nummer/häfte 5
Sidor 855-67
ISSN 0021-924X
Publiceringsår 2000
Publicerad vid Institutionen för medicinsk och fysiologisk kemi
Sidor 855-67
Språk en
Länkar www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord Amino Sugars, metabolism, Antigens, CD, Antimicrobial Cationic Peptides, Carbohydrate Metabolism, Carbohydrate Sequence, Electrophoresis, Polyacrylamide Gel, Lactosylceramides, metabolism, Lectins, chemistry, isolation & purification, metabolism, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Plant Lectins, Plant Proteins, chemistry, Sequence Alignment, Solanum tuberosum, chemistry, Structure-Activity Relationship
Ämneskategorier Kemi

Sammanfattning

Glycosphingolipid recognition by two isolectins from Solanum tuberosum was compared by the chromatogram binding assay. One lectin (PL-I) was isolated from potato tubers by affinity chromatography, and identified by MALDI-TOF mass spectrometry as a homodimer with a subunit molecular mass of 63,000. The other (PL-II) was a commercial lectin, characterized as two homodimeric isolectins with subunit molecular masses of 52,000 and 55,000, respectively. Both lectins recognized N-acetyllactosamine-containing glycosphingolipids, but the fine details of their carbohydrate binding specificities differed. PL-II preferentially bound to glycosphingolipids with N-acetyllactosamine branches, as Galbeta4GlcNAcbeta6(Galbeta4GlcNAcbeta3)Galbeta4Glcbeta1C er. PL-I also recognized this glycosphingolipid, but bound equally well to the linear glycosphingolipid Galbeta4GlcNAcbeta3Galbeta4GlcNAcbeta3Galbeta4Glcbeta1Cer. Neolactotetraosylceramide and the B5 pentaglycosylceramide were also bound by PL-I, while other glycosphingolipids with only one N-acetyllactosamine unit were non-binding. Surprisingly, both lectins also bound to lactosylceramide, with an absolute requirement for sphingosine and non-hydroxy fatty acids. The inhibition of binding to both lactosylceramide and N-acetyllactosamine-containing glycosphingolipids by N-acetylchitotetraose suggests that lactosylceramide is also accomodated within the N-acetylchitotetraose/N-acetyllactosamine-binding sites of the lectins. Through docking of glycosphingolipids onto a three-dimensional model of the PL-I hevein binding domain, a Galbeta4GlcNAcbeta3Galbeta4 binding epitope was defined. Furthermore, direct involvement of the ceramide in the binding of lactosylceramide was suggested.

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