Carbohydrate binding specificity of four N-acetyl-D-galactosamine-"specific" lectins: Helix pomatia A hemagglutinin, soy bean agglutinin, lima bean lectin, and Dolichos biflorus lectin

Biochemistry ◽  
1977 ◽  
Vol 16 (12) ◽  
pp. 2750-2755 ◽  
Author(s):  
Sten Hammarstrom ◽  
Lee A. Murphy ◽  
Irwin J. Goldstein ◽  
Marilynn E. Etzler
Keyword(s):  
Helix Pomatia ◽  
Lima Bean ◽  
Binding Specificity ◽  
Carbohydrate Binding ◽  
Dolichos Biflorus

Effects of an Oxidative Agent and Lectins on the Binding Inhibition of Recombinant Hepatitis A Virus Proteins to Oyster Digestive Tissues

2011 ◽  
Vol 74 (1) ◽  
pp. 157-160 ◽  
Author(s):  
SANG-MU KO ◽  
JONG-OH KIM ◽  
MYUNG-JOO OH ◽  
DUWOON KIM
Keyword(s):  
Binding Sites ◽  
Hepatitis A ◽  
Hepatitis A Virus ◽  
Helix Pomatia ◽  
Control Group ◽  
Carbohydrate Binding ◽  
Dolichos Biflorus ◽  
Ulex Europaeus ◽  
Binding Inhibition ◽  
Viral Contaminants

While the exact mechanism of hepatitis A virus (HAV) accumulation remains unclear, it has been demonstrated that viruses related to shellfish-borne gastroenteritis can bind to carbohydrates of oyster tissues. We investigated carbohydrate-binding sites to determine if they were related to the binding of HAV to carbohydrate moieties on oyster digestive tissues (DTs) using recombinant HAV proteins (rHAVPs). In addition, we evaluated lectins to determine if they influenced the inhibition of binding of rHAVPs to carbohydrates present in DT. DT that was treated with 0.5% potassium periodate allowed only 23% ± 3.6% and 33% ± 7.8% binding of VP1-P2A and VP1 rHAVPs, respectively, when compared with a control group (100%) treated with distilled water, indicating that carbohydrate-binding sites are strongly related to the binding of HAV. Soybean agglutinin (SBA) led to the greatest decrease in the binding affinity among six lectins (Helix pomatia, Dolichos biflorus, Ulex europaeus, SBA, Triticum vulgaris, and Arachis hypogaea) tested for inhibition of the binding of rHAVPs to DT, indicating that exposing the virus-contaminated DT to SBA might have the potential to depurate viral contaminants found in shellfish food products by high-affinity binding between SBA and rHAVPs, thus improving food safety.

Carbohydrate binding, quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus 1 1Edited by R. Huber

1999 ◽  
Vol 286 (4) ◽  
pp. 1161-1177 ◽  
Author(s):  
Thomas W Hamelryck ◽  
Remy Loris ◽  
Julie Bouckaert ◽  
Minh-Hoa Dao-Thi ◽  
Gerard Strecker ◽  
...  
Keyword(s):  
Binding Site ◽  
Quaternary Structure ◽  
Carbohydrate Binding ◽  
Dolichos Biflorus ◽  
Legume Lectin ◽  
Hydrophobic Binding

scholarly journals Carbohydrate binding specificity of immobilized Psathyrella velutina lectin.

1992 ◽  
Vol 267 (2) ◽  
pp. 707-713
Author(s):  
T Endo ◽  
H Ohbayashi ◽  
K Kanazawa ◽  
N Kochibe ◽  
A Kobata
Keyword(s):  
Binding Specificity ◽  
Carbohydrate Binding

scholarly journals Redefinition of the Carbohydrate Binding Specificity ofHelicobacter pyloriBabA Adhesin

2012 ◽  
Vol 287 (38) ◽  
pp. 31712-31724 ◽  
Author(s):  
John Benktander ◽  
Jonas Ångström ◽  
Michael E. Breimer ◽  
Susann Teneberg
Keyword(s):  
Binding Specificity ◽  
Carbohydrate Binding
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