The Spectral and Thermodynamic Properties of Staphylococcal Enterotoxin A, E, and Variants Suggest That Structural Modifications Are Important to Control Their Function

The superantigens staphylococcal enterotoxin A and E (SEA and SEE) can activate a large number of T-cells. SEA and SEE have approximately 80% sequence identity but show some differences in their biological function. Here, the two superantigens and analogues were characterized biophysically. SEE was...

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Bibliographic Details
Published in:	The Journal of biological chemistry Vol. 275; no. 3; pp. 1665 - 1672
Main Authors:	Cavallin, Anders, Arozenius, Helena, Kristensson, Karin, Antonsson, Per, Otzen, Daniel E., Björk, Per, Forsberg, Göran
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 21-01-2000 American Society for Biochemistry and Molecular Biology
Subjects:	Amino Acid Sequence Animals Cells, Cultured Circular Dichroism Dose-Response Relationship, Drug Enterotoxins - chemistry Guanidine - pharmacology Histocompatibility Antigens Class II - metabolism Hydrogen-Ion Concentration Mice Mice, Inbred C57BL Molecular Sequence Data Protein Binding Protein Denaturation Protein Structure, Tertiary Recombinant Fusion Proteins - chemistry Sequence Homology, Amino Acid Spleen - metabolism staphylococcal enterotoxin A staphylococcal enterotoxin E Staphylococcus Structure-Activity Relationship Superantigens - metabolism T-Lymphocytes - metabolism Temperature Thermodynamics Zinc - metabolism
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