Evidence for an Increase in Positive Surface Charge and an Increase in Susceptibility to Trypsin of Sarcophaga Lectin (from the Flesh Fly, Sarcophaga Peregrina) on Its Interaction with Galactose, a Hapten Sugar of the Lectin

Overview

Journal Biochem J

Specialty Biochemistry

Date 1992 May 15

PMID 1599400

Citations 2

Authors

H Komano

T Kurama

Y Nagasawa

S Natori

Affiliations

Soon will be listed here.

Abstract

When Sarcophaga lectin (from the flesh fly, Sarcophaga peregrina), an insect humoral lectin, was eluted from a column of DEAE-cellulose in the presence of galactose (a hapten sugar of this lectin), it emerged at a lower salt concentration than when galactose was absent. In the presence of galactose the lectin was, in addition, more susceptible to trypsin digestion. The lectin was found to have an affinity for basic proteins such as histone H3 and sarcotoxin IA, but this property was lost in the presence of galactose. These results suggested that the lectin changes its conformation on interaction with galactose. This change is suggested to result in the exposure of some hidden lysine and/or arginine residues.

Citing Articles

Detection of ligand- and solvent-induced shape alterations of cell-growth-regulatory human lectin galectin-1 in solution by small angle neutron and x-ray scattering.

He L, Andre S, Siebert H, Helmholz H, Niemeyer B, Gabius H Biophys J. 2003; 85(1):511-24.

PMID: 12829506 PMC: 1303107. DOI: 10.1016/S0006-3495(03)74496-8.

The how and why of protein-carbohydrate interaction: a primer to the theoretical concept and a guide to application in drug design.

Gabius H Pharm Res. 1998; 15(1):23-30.

PMID: 9487542 DOI: 10.1023/a:1011936300845.

References

Abbott W, Feizi T . Soluble 14-kDa beta-galactoside-specific bovine lectin. Evidence from mutagenesis and proteolysis that almost the complete polypeptide chain is necessary for integrity of the carbohydrate recognition domain. J Biol Chem. 1991; 266(9):5552-7. View

Komano H, Mizuno D, Natori S . Purification of lectin induced in the hemolymph of Sarcophaga peregrina larvae on injury. J Biol Chem. 1980; 255(7):2919-24. View

Natori S . Dual functions of insect immunity proteins in defence and development. Res Immunol. 1990; 141(9):938-9. DOI: 10.1016/0923-2494(90)90198-8. View

Loeb J, Drickamer K . Conformational changes in the chicken receptor for endocytosis of glycoproteins. Modulation of ligand-binding activity by Ca2+ and pH. J Biol Chem. 1988; 263(20):9752-60. View

Drickamer K . Two distinct classes of carbohydrate-recognition domains in animal lectins. J Biol Chem. 1988; 263(20):9557-60. View

Takahashi H, Komano H, Kawaguchi N, Kitamura N, Nakanishi S, Natori S . Cloning and sequencing of cDNA of Sarcophaga peregrina humoral lectin induced on injury of the body wall. J Biol Chem. 1985; 260(22):12228-33. View

Komano H, Kasama E, Nagasawa Y, Nakanishi Y, Matsuyama K, Ando K . Purification of Sarcophaga (fleshfly) lectin and detection of sarcotoxins in the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina. Biochem J. 1987; 248(1):217-22. PMC: 1148521. DOI: 10.1042/bj2480217. View

Okada M, Natori S . Primary structure of sarcotoxin I, an antibacterial protein induced in the hemolymph of Sarcophaga peregrina (flesh fly) larvae. J Biol Chem. 1985; 260(12):7174-7. View

Komano H, Natori S . Participation of Sarcophaga peregrina humoral lectin in the lysis of sheep red blood cells injected into the abdominal cavity of larvae. Dev Comp Immunol. 1985; 9(1):31-40. DOI: 10.1016/0145-305x(85)90057-6. View

10.

Dipaola M, Maxfield F . Conformational changes in the receptors for epidermal growth factor and asialoglycoproteins induced by the mildly acidic pH found in endocytic vesicles. J Biol Chem. 1984; 259(14):9163-71. View

11.

Komano H, Nozawa R, Mizuno D, Natori S . Measurement of Sarcophaga peregrina lectin under various physiological conditions by radioimmunoassay. J Biol Chem. 1983; 258(4):2143-7. View

12.

Komano H, Mizuno D, Natori S . A possible mechanism of induction of insect lectin. J Biol Chem. 1981; 256(14):7087-9. View

13.

Hunter W, GREENWOOD F . Preparation of iodine-131 labelled human growth hormone of high specific activity. Nature. 1962; 194:495-6. DOI: 10.1038/194495a0. View

14.

LOWRY O, ROSEBROUGH N, FARR A, RANDALL R . Protein measurement with the Folin phenol reagent. J Biol Chem. 1951; 193(1):265-75. View

15.

LaFramboise W, Daood M, Guthrie R, Schiaffino S, Moretti P, Brozanski B . Emergence of the mature myosin phenotype in the rat diaphragm muscle. Dev Biol. 1991; 144(1):1-15. DOI: 10.1016/0012-1606(91)90473-g. View