Biological analysis of the deletion mutants of Staphylococcal enterotoxin C2.
To investigate the functional domains involved in the biological activity of staphylococcal enterotoxin (SEC2), a series of SEC2 mutants were constructed. Deletion of the last 77 amino acids at the C-terminus of SEC2 did not affect its native superantigen and fever activities, and further removal of the C-terminal residues reduced SEC2 activities significantly. On the other hand, the mutants lacking 18 or more N-terminal residues severely impaired superantigen activity. These data indicated that the functional regions for the biological activities of SEC2 were confined to N-terminal domain, further implied that the proper three-dimensional structure of SEC2 is not needed for its biological activities. Our results deliver valuable information that it is possible to design new SEC2 immunotherapeutic agents which have the superantigen activity and low molecular weight for permeability.
Wang
Xiaogang
X
Institute of Applied Ecology, Shenyang, People's Republic of China.
Zhang
Huiwen
H
Xu
Mingkai
M
Liu
Changxiao
C
Zhang
Chenggang
C
D001426:Bacterial Proteins / Q000235:genetics* / Q000276:immunology / Q000633:toxicity*; D004252:DNA Mutational Analysis; D004768:Enterotoxins / Q000235:genetics* / Q000276:immunology / Q000633:toxicity*; D050505:Mutant Proteins / Q000235:genetics / Q000276:immunology / Q000633:toxicity; D017384:Sequence Deletion; D013211:Staphylococcus aureus / Q000235:genetics*; D018089:Superantigens / Q000235:genetics / Q000276:immunology / Q000633:toxicity
D001426:Bacterial Proteins; D004768:Enterotoxins; D050505:Mutant Proteins; D018089:Superantigens; C034959:enterotoxin C, staphylococcal