TY - JOUR
T1 - Multivalent binding of ricin to bovine serum albumin-based neoglycoconjugates
AU - Blome, Matthew C.
AU - Schengrund, Cara Lynne
N1 - Funding Information:
We thank Dr. Bruce Stanley for his assistance with the MALDI-TOF MS analyses of our ligands. This work was supported, in part, under a grant with the Pennsylvania Department of Health's Health Research Formula Funding Program (State of Pennsylvania, Act 2001-77-PA Tobacco Settlement Legislation). The Department specifically disclaims responsibility for any analyses, interpretations, or conclusions.
PY - 2008/6/1
Y1 - 2008/6/1
N2 - Ricin, a ribosome-inactivating protein from the plant Ricinus communis, is a heterodimeric protein. The A chain is a N-glycosidase and the B chain (RTB) is a lectin with two carbohydrate binding sites. RTB has been shown to bind asialofetuin with much greater affinity than it does galactose, supporting the hypothesis that it may exhibit multivalency. To test this, neoglycoconjugates were prepared and tested for their ability to function as ligands for ricin binding. Because the two carbohydrate binding sites on RTB are ∼70 Å apart, bovine serum albumin (BSA) was used as the carbohydrate carrier. It was derivatized with either the oligosaccharide portion of asialo-GM1 or with lactose. These sugars were used because ricin was found to adhere more effectively to asialo-GM1 and LacCer immobilized on plastic than to the other glycosphingolipids tested. Results of binding studies done using surface plasmon resonance indicated that the RTB subunit of ricin exhibited a multivalent effect when it bound to the neoglycoconjugates.
AB - Ricin, a ribosome-inactivating protein from the plant Ricinus communis, is a heterodimeric protein. The A chain is a N-glycosidase and the B chain (RTB) is a lectin with two carbohydrate binding sites. RTB has been shown to bind asialofetuin with much greater affinity than it does galactose, supporting the hypothesis that it may exhibit multivalency. To test this, neoglycoconjugates were prepared and tested for their ability to function as ligands for ricin binding. Because the two carbohydrate binding sites on RTB are ∼70 Å apart, bovine serum albumin (BSA) was used as the carbohydrate carrier. It was derivatized with either the oligosaccharide portion of asialo-GM1 or with lactose. These sugars were used because ricin was found to adhere more effectively to asialo-GM1 and LacCer immobilized on plastic than to the other glycosphingolipids tested. Results of binding studies done using surface plasmon resonance indicated that the RTB subunit of ricin exhibited a multivalent effect when it bound to the neoglycoconjugates.
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U2 - 10.1016/j.toxicon.2008.02.005
DO - 10.1016/j.toxicon.2008.02.005
M3 - Article
C2 - 18384830
AN - SCOPUS:43849089490
SN - 0041-0101
VL - 51
SP - 1214
EP - 1224
JO - Toxicon
JF - Toxicon
IS - 7
ER -