THE EPIDERMOLYTIC TOXINS ARE SERINE PROTEASES

被引:70
作者
DANCER, SJ
GARRATT, R
SALDANHA, J
JHOTI, H
EVANS, R
机构
[1] LAB MOLEC BIOPHYS, OXFORD OX1 3QU, ENGLAND
[2] UNIV SAO PAULO, INST FIS & QUIM SAO CARLOS, DEPT FIS CIENCIAS MAT, BR-13560 SAO CARLOS, SP, BRAZIL
[3] IMPERIAL CANC RES FUND, BIOMED COMP UNIT, LONDON WC2A 3PX, ENGLAND
来源
FEBS LETTERS | 1990年 / 268卷 / 01期
关键词
Epidermolytic toxin; Serine protease; Staphylococcus aureus;
D O I
10.1016/0014-5793(90)80990-Z
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Certain strains of Staphylococcus aureus usually belonging to phage group II produce epidermolytic toxins (ETA and ETB) which cause intraepidermal splitting in mice, neonates and occasionally adults. Amino acid sequences of ETA and ETB have been reported but the mechanism of epidermolysis remains unknown. A search of the NBRF-PIR computer database showed the toxins to have significant sequence similarity with staphylococcal V8 protease and that the catalytic triad of V8 protease is present in ETA and ETB. Comparison of ETA, ETB and V8 protease with other members of the trypsin-like serine protease family revealed little homology save for the immediate vicinity of the residues constituting the catalytic triad. The toxins, therefore, exhibit a distant relationship to mammalian serine proteases. A potential Ca2+-binding loop was identified in ETA (but not ETB) on the basis of sequence similarity with the second calcium-binding loop of rat intestinal calcium-binding protein. Epidermolysis produced by ETA in the mouse bioassay was shown to be inhibited by the presence of EDTA consistent with a Ca2+-dependent mechanism. © 1990.
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收藏
页码:129 / 132
页数:4
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