The crystal structure of exfoliative toxin B: A superantigen with enzymatic activity

Gregory M. Vath, Cathleen A. Earhart, Dileep D. Monie, John J. Iandolo, Patrick M. Schlievert, Douglas H Ohlendorf

Research output: Contribution to journalArticlepeer-review

56 Scopus citations

Abstract

The exfoliative toxins (ETs) cause staphylococcal scalded skin syndrome, a disease characterized by specific separation of layers of the skin. Evidence suggests that the toxins act as serine proteases, though the Specific substrate and mode of action are not known for certain. The crystal structure of exfoliative toxin A (ETA) was reported earlier and shown to be similar to that of the chymotrypsin-like serine proteases. Here, we report the 2.4 Å resolution crystal structure of the other exfoliative toxin, ETB, which is 40% identical to ETA. The overall structures of ETA and ETB are similar including the positions of key residues within the active site. The structure of ETB supports the previous findings that the ETs are serine proteases that cleave substrates after glutamic acid residues. In this study we also discuss a number of structural differences including a large 14 residue loop insertion which may be a key feature involved in the differing biological properties of the ETs, particularly the pyrogenic and lethal activities of ETB not shared by ETA.

Original languageEnglish (US)
Pages (from-to)10239-10246
Number of pages8
JournalBiochemistry
Volume38
Issue number32
DOIs
StatePublished - Aug 10 1999

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