Purification and characterization of a natural lectin from the plasma of the shrimp Fenneropenaeus chinensis.
A natural lectin from the plasma of the shrimp Fenneropenaeus chinensis was purified by singlestep affinity chromatography using fetuin-coupled agarose. The purified plasma lectin showed a strong affinity for human A/B/O erythrocytes (RBC), mouse RBC and chicken RBC. The hemagglutinating (HA) activity of the lectin was dependent on Ca(2+) and reversibly sensitive to EDTA. This lectin was named FC-L and its inactive form had a molecular mass estimate of 168 kDa. Fifteen N-terminal amino acid sequences of this protein were determined. We performed HA-inhibition assays with several carbohydrates and glycoproteins. FC-L showed a distinct and unique specificity to N-acetylated sugars, particularly sialic acid and sialoproteins. The FC-L also has binding activity to some Gram-negative bacteria which caused disease in shrimp and fish. The activity of FC-L was inhibited at temperatures greater than 75 degrees C and at a pH less than 7 or greater than 11. These results suggest that FC-L may play a role as pattern recognition proteins in the reorganization and clearance of invaders in shrimp F. chinensis.
Sun
Jie
J
Institute of Oceanology, The Chinese Academy of Sciences, Qingdao, China.
Wang
Lei
L
Wang
Baojie
B
Guo
Zhenyu
Z
Liu
Mei
M
Jiang
Keyong
K
Tao
Ran
R
Zhang
Guofan
G
D000818:Animals; D001419:Bacteria / Q000378:metabolism; D002118:Calcium / Q000378:metabolism; D050260:Carbohydrate Metabolism; D004912:Erythrocytes / Q000378:metabolism; D006385:Hemagglutination Inhibition Tests; D006386:Hemagglutination Tests; D006458:Hemolymph / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D037102:Lectins / Q000302:isolation & purification* / Q000378:metabolism*; D033561:Penaeidae / Q000378:metabolism*; D013696:Temperature
D037102:Lectins; D002118:Calcium