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1.
Biochem Biophys Res Commun ; 491(3): 708-713, 2017 09 23.
Artigo em Inglês | MEDLINE | ID: mdl-28751211

RESUMO

F-type lectins are fucose binding lectins with characteristic fucose binding and calcium binding motifs. Although they occur with a selective distribution in viruses, prokaryotes and eukaryotes, most biochemical studies have focused on vertebrate F-type lectins. Recently, using sensitive bioinformatics search techniques on the non-redundant database, we had identified many microbial F-type lectin domains with diverse domain organizations. We report here the biochemical characterization of F-type lectin domains from Cyanobium sp. PCC 7001, Myxococcus hansupus and Leucothrix mucor. We demonstrate that while all these three microbial F-type lectin domains bind to the blood group H antigen epitope on fucosylated glycans, there are fine differences in their glycan binding specificity. Cyanobium sp. PCC 7001 F-type lectin domain binds exclusively to extended H type-2 motif, Myxococcus hansupus F-type lectin domain binds to B, H type-1 and Lewisb motifs, and Leucothrix mucor F-type lectin domain binds to a wide range of fucosylated glycans, including A, B, H and Lewis antigens. We believe that these microbial lectins will be useful additions to the glycobiologist's toolbox for labeling, isolating and visualizing glycans.


Assuntos
Proteínas de Bactérias/química , Proteínas de Bactérias/ultraestrutura , Antígenos de Grupos Sanguíneos/química , Antígenos de Grupos Sanguíneos/ultraestrutura , Lectinas/química , Lectinas/ultraestrutura , Sítios de Ligação , Modelos Químicos , Simulação de Acoplamento Molecular , Ligação Proteica , Domínios Proteicos
2.
Glycobiology ; 27(1): 80-86, 2017 01.
Artigo em Inglês | MEDLINE | ID: mdl-27496762

RESUMO

Recently, combined nuclear magnetic resonance (NMR), native mass spectrometry (MS) and X-ray crystallographic studies have demonstrated that binding of histo-blood group antigens (HBGAs) to norovirus capsid protein (P-dimers) is a cooperative process involving four binding pockets. Here, we show that binding to norovirus virus-like particles (VLPs) is even more complex. We performed saturation transfer difference (STD) NMR titration experiments with two representative genotypes of norovirus VLPs using l-fucose as a minimal HBGA. Compared to titrations with P-dimers, the corresponding binding isotherms reflect at least six distinct binding events.


Assuntos
Antígenos de Grupos Sanguíneos/química , Proteínas do Capsídeo/química , Norovirus/química , Antígenos de Grupos Sanguíneos/metabolismo , Antígenos de Grupos Sanguíneos/ultraestrutura , Proteínas do Capsídeo/ultraestrutura , Cristalografia por Raios X , Fucose/química , Humanos , Espectroscopia de Ressonância Magnética , Norovirus/ultraestrutura , Ligação Proteica , Vírion/química , Vírion/ultraestrutura
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