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Infection and Immunity, March 2001, p. 1381-1388, Vol. 69, No. 3
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.3.1381-1388.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Functional Characterization of Streptococcal Pyrogenic Exotoxin J, a Novel Superantigen

John K. McCormick,1 Alexa A. Pragman,1 John C. Stolpa,2 Donald Y. M. Leung,2,3 and Patrick M. Schlievert1,*

Department of Microbiology, University of Minnesota Medical School, Minneapolis, Minnesota 55455,1 and Department of Pediatrics, Dermatology and Medicine, University of Colorado Health Sciences Center,2 and Division of Pediatric Allergy and Immunology, The National Jewish Medical and Research Center,3 Denver, Colorado 80262

Received 6 September 2000/Returned for modification 26 October 2000/Accepted 16 November 2000

Streptococcal toxic shock syndrome (STSS) is a highly lethal, acute-onset illness that is a subset of invasive streptococcal disease. The majority of clinical STSS cases have been associated with the pyrogenic toxin superantigens (PTSAgs) streptococcal pyrogenic exotoxin A or C (SPE A or C), although cases have been reported that are not associated with either of these exotoxins. Recent genome sequencing projects have revealed a number of open reading frames that potentially encode proteins with similarity to SPEs A and C and to other PTSAgs. Here, we describe the cloning, expression, purification, and functional characterization of a novel exotoxin termed streptococcal pyrogenic exotoxin J (SPE J). Purified recombinant SPE J (rSPE J) expressed from Escherichia coli stimulated the expansion of both rabbit splenocytes and human peripheral blood lymphocytes, preferentially expanded human T cells displaying Vbeta 2, -3, -12, -14, and -17 on their T-cell receptors, and was active at concentrations as low as 5 × 10-6 µg/ml. Furthermore, rSPE J induced fevers in rabbits and was lethal in two models of STSS. Biochemically, SPE J had a predicted molecular weight of 24,444 and an isoelectric point of 7.7 and lacked the ability to form the cystine loop structure characteristic of many PTSAgs. SPE J shared 19.6, 47.1, 38.8, 18.1, 19.6, and 24.4% identity with SPEs A, C, G, and H, streptococcal superantigen, and streptococcal mitogenic exotoxin Z-2, respectively, and was immunologically cross-reactive with SPE C. The characterization of a seventh functional streptococcal PTSAg raises important questions relating to the evolution of the streptococcal superantigens.

* Corresponding author. Mailing address: Department of Microbiology, University of Minnesota Medical School, 420 Delaware St., SE, Minneapolis, MN 55455. Phone: (612) 624-9471. Fax: (612) 626-0623. E-mail: pats{at}lenti.med.umn.edu.

Infection and Immunity, March 2001, p. 1381-1388, Vol. 69, No. 3
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.3.1381-1388.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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