The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata
Abstract SeviL is a recently isolated lectin found to bind to the linear saccharides of the ganglioside GM1b (Neu5Ac $$\alpha$$ α (2-3)Gal $$\beta$$ β (1-3)GalNAc $$\beta$$ β (1-4)Gal $$\beta$$ β (1-4)Glc) and its precursor, asialo-GM1 (Gal $$\beta$$ β (1-3)GalNAc $$\beta$$ β (1-4)Gal $$\beta$$ β (1...
Guardado en:
| Autores principales: | , , , , , , , , , , , , |
|---|---|
| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
Nature Portfolio
2020
|
| Materias: | |
| Acceso en línea: | https://doaj.org/article/b60abb2e47eb4f1aadf04cd6577a2ac0 |
| Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
| id |
oai:doaj.org-article:b60abb2e47eb4f1aadf04cd6577a2ac0 |
|---|---|
| record_format |
dspace |
| spelling |
oai:doaj.org-article:b60abb2e47eb4f1aadf04cd6577a2ac02021-12-02T12:40:41ZThe structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata10.1038/s41598-020-78926-72045-2322https://doaj.org/article/b60abb2e47eb4f1aadf04cd6577a2ac02020-12-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-78926-7https://doaj.org/toc/2045-2322Abstract SeviL is a recently isolated lectin found to bind to the linear saccharides of the ganglioside GM1b (Neu5Ac $$\alpha$$ α (2-3)Gal $$\beta$$ β (1-3)GalNAc $$\beta$$ β (1-4)Gal $$\beta$$ β (1-4)Glc) and its precursor, asialo-GM1 (Gal $$\beta$$ β (1-3)GalNAc $$\beta$$ β (1-4)Gal $$\beta$$ β (1-4)Glc). The crystal structures of recombinant SeviL have been determined in the presence and absence of ligand. The protein belongs to the $$\beta$$ β -trefoil family, but shows only weak sequence similarity to known structures. SeviL forms a dimer in solution, with one binding site per subunit, close to the subunit interface. Molecular details of glycan recognition by SeviL in solution were analysed by ligand- and protein-based NMR techniques as well as ligand binding assays. SeviL shows no interaction with GM1 due to steric hindrance with the sialic acid branch that is absent from GM1b. This unusual specificity makes SeviL of great interest for the detection and control of certain cancer cells, and cells of the immune system, that display asialo-GM1.Kenichi KamataKenji MizutaniKatsuya TakahashiRoberta MarchettiAlba SilipoChristine AddySam-Yong ParkYuki FujiiHideaki FujitaTsuyoshi KonumaTakahisa IkegamiYasuhiro OzekiJeremy R. H. TameNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 10, Iss 1, Pp 1-13 (2020) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
Medicine R Science Q |
| spellingShingle |
Medicine R Science Q Kenichi Kamata Kenji Mizutani Katsuya Takahashi Roberta Marchetti Alba Silipo Christine Addy Sam-Yong Park Yuki Fujii Hideaki Fujita Tsuyoshi Konuma Takahisa Ikegami Yasuhiro Ozeki Jeremy R. H. Tame The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata |
| description |
Abstract SeviL is a recently isolated lectin found to bind to the linear saccharides of the ganglioside GM1b (Neu5Ac $$\alpha$$ α (2-3)Gal $$\beta$$ β (1-3)GalNAc $$\beta$$ β (1-4)Gal $$\beta$$ β (1-4)Glc) and its precursor, asialo-GM1 (Gal $$\beta$$ β (1-3)GalNAc $$\beta$$ β (1-4)Gal $$\beta$$ β (1-4)Glc). The crystal structures of recombinant SeviL have been determined in the presence and absence of ligand. The protein belongs to the $$\beta$$ β -trefoil family, but shows only weak sequence similarity to known structures. SeviL forms a dimer in solution, with one binding site per subunit, close to the subunit interface. Molecular details of glycan recognition by SeviL in solution were analysed by ligand- and protein-based NMR techniques as well as ligand binding assays. SeviL shows no interaction with GM1 due to steric hindrance with the sialic acid branch that is absent from GM1b. This unusual specificity makes SeviL of great interest for the detection and control of certain cancer cells, and cells of the immune system, that display asialo-GM1. |
| format |
article |
| author |
Kenichi Kamata Kenji Mizutani Katsuya Takahashi Roberta Marchetti Alba Silipo Christine Addy Sam-Yong Park Yuki Fujii Hideaki Fujita Tsuyoshi Konuma Takahisa Ikegami Yasuhiro Ozeki Jeremy R. H. Tame |
| author_facet |
Kenichi Kamata Kenji Mizutani Katsuya Takahashi Roberta Marchetti Alba Silipo Christine Addy Sam-Yong Park Yuki Fujii Hideaki Fujita Tsuyoshi Konuma Takahisa Ikegami Yasuhiro Ozeki Jeremy R. H. Tame |
| author_sort |
Kenichi Kamata |
| title |
The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata |
| title_short |
The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata |
| title_full |
The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata |
| title_fullStr |
The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata |
| title_full_unstemmed |
The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata |
| title_sort |
structure of sevil, a gm1b/asialo-gm1 binding r-type lectin from the mussel mytilisepta virgata |
| publisher |
Nature Portfolio |
| publishDate |
2020 |
| url |
https://doaj.org/article/b60abb2e47eb4f1aadf04cd6577a2ac0 |
| work_keys_str_mv |
AT kenichikamata thestructureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT kenjimizutani thestructureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT katsuyatakahashi thestructureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT robertamarchetti thestructureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT albasilipo thestructureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT christineaddy thestructureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT samyongpark thestructureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT yukifujii thestructureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT hideakifujita thestructureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT tsuyoshikonuma thestructureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT takahisaikegami thestructureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT yasuhiroozeki thestructureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT jeremyrhtame thestructureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT kenichikamata structureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT kenjimizutani structureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT katsuyatakahashi structureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT robertamarchetti structureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT albasilipo structureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT christineaddy structureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT samyongpark structureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT yukifujii structureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT hideakifujita structureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT tsuyoshikonuma structureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT takahisaikegami structureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT yasuhiroozeki structureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata AT jeremyrhtame structureofsevilagm1basialogm1bindingrtypelectinfromthemusselmytiliseptavirgata |
| _version_ |
1718393761429454848 |