Streptococcal pyrogenic exotoxin type A (scarlet fever toxin) is related to Staphylococcus aureus enterotoxin B

Johnson, L. P. V.; L’Italien, James; Schlievert, Patrick M.

doi:10.1007/bf00333979

Cited by 80 publications

(32 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Of the two slightly different peptide sequences reported for SEB, we elected to use the one of Jones and Kahn (18) because it was derived from the nucleotide sequence rather than the protein sequence (14). For our comparisons we used the SPEA sequence reported by Weeks and Ferritti (54), because in the region corresponding to SEA amino acid residues 145 to 156 this SPEA sequence had 10 of 12 residues in common with three enterotoxins, whereas the SPEA sequence in this region reported by Johnson et al (16) (16).…”

Section: Resultsmentioning

confidence: 99%

“…The deduced amino acid sequence of SEA was shown to contain regions of homology to the amino acid sequences of SEB (14,18), SEC1 (43), type A streptococcal exotoxin (SPEA) (16,54), and toxic shock syndrome toxin 1 (TSST-1) (8). DNA probes derived from the cloned entA gene as well as a synthetic oligonucleotide probe (representing the coding sequences for a highly conserved peptide present in three of the enterotoxins) were shown to hybridize to DNA isolated from other types of staphylococcal enterotoxin producers.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Nucleotide sequence of the type A staphylococcal enterotoxin gene

1988

View full text Add to dashboard Cite

We determined the nucleotide sequence of the gene encoding staphylococcal enterotoxin A (entA). The gene, composed of 771 base pairs, encodes an enterotoxin A precursor of 257 amino acid residues. A 24-residue N-terminal hydrophobic leader sequence is apparently processed, yielding the mature form of staphylococcal enterotoxin A (Mr, 27,100). Mature enterotoxin A has 82, 72, 74, and 34 amino acid residues in common with staphylococcal enterotoxins B and Cl, type A streptococcal exotoxin, and toxic shock syndrome toxin 1, respectively. This level of homology was determined to be significant based on the results of computer analysis and biological considerations. DNA sequence homology between the entA gene and genes encoding other types of staphylococcal enterotoxins was examined by DNA-DNA hybridization analysis with probes derived from the entA gene. A 624-base-pair DNA probe that represented an internal fragment of the entA gene hybridized well to DNA isolated from EntE+ strains and some EntA+ strains. In contrast, a 17-base oligonucleotide probe that encoded a peptide conserved among staphylococcal enterotoxins A, B, and Cl hybridized well to DNA isolated from EntA', EntB+, EntC1+, and EntD+ strains. These hybridization results indicate that considerable sequence divergence has occurred within this family of exotoxins.

show abstract

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Nucleotide sequence of the type A staphylococcal enterotoxin gene

1988

View full text Add to dashboard Cite

show abstract

“…The extensive homology among streptococcal and staphylococcal superantigens suggests that they share a common ancestor, either before the evolutionary divergence of the two organisms or as a result of horizontal gene transfer. The two prototypic streptococcal superantigens, SPE A and SPE C, are both encoded on functional phage (11, 20-23, 26, 39, 41), and lateral movement by converting bacteriophage has been demonstrated for both speA (19,63,65) and speC (11). Comparison of the phylogenetic tree constructed from all known streptococcal and staphylococcal bacterial superantigens reveals three main evolutionary branches, not including SPE H (Fig.…”

Section: Discussionmentioning

confidence: 99%

Functional Characterization of Streptococcal Pyrogenic Exotoxin J, a Novel Superantigen

et al. 2001

Self Cite

View full text Add to dashboard Cite

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 V␤2, -3, -12, -14, and -17 on their T-cell receptors, and was active at concentrations as low as 5 ؋ 10 ؊6 g/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.

show abstract

“…Sequences specific for speA (32), speB (34), speC (24), speF (28), speG (56), speH (56), speJ (56), smeZ (21), ssa (59), cpa (55), cpa-1 (T. Miyoshi-Akiyama, N. Wakisaka, J. Zhao, and T. Uchiyama, unpublished data), fba (75), fbp-54 (Miyoshi-Akiyama et al, unpublished), pfbp (61), prtf-1 (66), prtf-2 (29), prtf-15 (35), sciA (58), sciB (78), sfb (72), and sfb-II (40) were detected by PCR on a model 9600 thermocycler (Perkin-Elmer, Gouda, The Netherlands) with the primers listed in Table 1. Amplification of all genes was carried out under the following conditions: an initial 5-min denaturation step at 96°C, followed by 30 cycles of denaturation at Table 1, and 70 s of extension at 72°C, with a final extension step at 72°C for 5 min.…”

Section: Methodsmentioning

confidence: 99%

Site-Specific Manifestations of Invasive Group A Streptococcal Disease: Type Distribution and Corresponding Patterns of Virulence Determinants

Vlaminckx¹,

Mascini²,

Schellekens

et al. 2003

J Clin Microbiol

View full text Add to dashboard Cite

As part of a national surveillance program on invasive group A streptococci (GAS), isolates that caused specific manifestations of invasive GAS disease in The Netherlands were collected between 1992 and 1996. These site-specific GAS infections involved meningitis, arthritis, necrotizing fasciitis, and puerperal sepsis. An evaluation was performed to determine whether GAS virulence factors correlate with these different disease manifestations. PCRs were developed to detect 9 genes encoding exotoxins and 12 genes encoding fibronectin binding proteins. The genetic backgrounds of all isolates were determined by M genotyping and pulsed-field gel electrophoresis (PFGE) analysis. The predominant M types included M1, M2, M3, M4, M6, M9, M12, and M28. Most M types were associated with all manifestations of GAS disease. However, M2 was found exclusively in patients with puerperal sepsis, M6 predominated in patients with meningitis, and M12 predominated in patients with GAS arthritis. While characteristic gene profiles were detected in most M types, the resolution of detection of different gene profiles within M genotypes was enhanced by PFGE analysis, which clearly demonstrated the existence of some clonal lineages among invasive GAS isolates in The Netherlands. M1 isolates comprised a single clone carrying highly mitogenic toxin genes (speA, smeZ) and were associated with toxic shock-like syndrome. Toxin profiles were highly conserved among the most virulent strains, such as M1 and M3.

show abstract

Streptococcal pyrogenic exotoxin type A (scarlet fever toxin) is related to Staphylococcus aureus enterotoxin B

Cited by 80 publications

References 18 publications

Nucleotide sequence of the type A staphylococcal enterotoxin gene

Nucleotide sequence of the type A staphylococcal enterotoxin gene

Functional Characterization of Streptococcal Pyrogenic Exotoxin J, a Novel Superantigen

Site-Specific Manifestations of Invasive Group A Streptococcal Disease: Type Distribution and Corresponding Patterns of Virulence Determinants

Contact Info

Product

Resources

About