Lectin Arrays for Profiling Cell Surface Carbohydrate Expression

2005 ◽  
Vol 127 (28) ◽  
pp. 9982-9983 ◽  
Author(s):  
Ting Zheng ◽  
Dora Peelen ◽  
Lloyd M. Smith
Keyword(s):  
Cell Surface ◽  
Cell Surface Carbohydrate

Enhanced Iridium Complex Electrochemiluminescence Cytosensing and Dynamic Evaluation of Cell-Surface Carbohydrate Expression

2014 ◽  
Vol 20 (45) ◽  
pp. 14736-14743 ◽  
Author(s):  
Hong Zhou ◽  
Yiying Yang ◽  
Chunxiang Li ◽  
Bing Yu ◽  
Shusheng Zhang
Keyword(s):  
Cell Surface ◽  
Iridium Complex ◽  
Dynamic Evaluation ◽  
Cell Surface Carbohydrate

scholarly journals Structural analysis of Pore-Forming CEL-III

2014 ◽  
Vol 70 (a1) ◽  
pp. C1679-C1679
Author(s):  
Hideaki Unno ◽  
Shuichiro Goda ◽  
Tomomitsu Hatakeyama
Keyword(s):  
Cell Surface ◽  
Structural Transition ◽  
Carbohydrate Binding ◽  
Binding Domains ◽  
Cell Surface Carbohydrate ◽  
Transmembrane Pores ◽  
Flat Ring ◽  
Domain 3 ◽  
Monomeric Structure ◽  
Carbohydrate Chains

CEL-III is a hemolytic lectin isolated from the sea cucumber Cucumaria echinata. This lectin is composed of two carbohydrate-binding domains (domains 1-2) and one oligomerization domain (domain 3). After binding to the cell surface carbohydrate chains through domains 1-2, domain 3 self-associates to form transmembrane pores, leading to cell lysis or death, which resembles other pore-forming toxins of diverse organisms. To elucidate the pore-formation mechanism of CEL-III, the crystal structure of the CEL-III oligomer was determined. The CEL-III oligomer has a heptameric structure with a long β-barrel as a transmembrane pore. This β-barrel is composed of 14 β-strands resulting from a large structural transition of α-helices accommodated in the interface between domains 1-2 and domain 3 in the monomeric structure, suggesting that the dissociation of these α-helices triggered their structural transition into a β-barrel. After heptamerization, domains 1-2 form a flat ring, in which all carbohydrate- binding sites remain bound to cell surface carbohydrate chains, stabilizing the transmembrane β-barrel in a position perpendicular to the plane of the lipid bilayer.

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