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The etiological agents of Staphylococcal food poisoning (SFP) are members of the genus , predominantly . This form of food poisoning is considered intoxication; it does not involve infection by, and growth of, the bacteria in the host. This chapter primarily addresses SFP; however, in regard to the staphylococcal enterotoxins (SEs), there is significant overlap in the natural histories of both diseases. Humans are the main reservoir for staphylococci involved in human disease, including . is known for acquiring genetic resistance to heavy metals and antimicrobial agents used in clinical medicine. SFP occurs as either isolated cases or outbreaks affecting a large number of people. Biochemical and structural studies of SEs have revealed that some SEs are dependent on zinc ions to be functional and to be able to properly bind major histocompatibility complex class II (MHCII). SEs and other superantigens (SAgs) interact with a characteristic repertoire of T-cell receptors (TCR) sequences. The TCR specificity of each SE is determined by toxin residues in the shallow cavity at the top of the molecule. The structural aspects of SEs that enable them to survive degradation by pepsin and other enzymes in the gastrointestinal tract are required for the toxins to induce SFP. Progress has been made toward understanding the molecular aspects relevant to SFP. has some unique properties that promote its ability to produce foodborne illness.

Citation: Seo K, Bohach G. 2013. , p 547-573. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch21
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Image of Figure 21.1
Figure 21.1

Alignment of primary sequences of mature SEs and SEls in the current literature. Also shown are the consensus sequence (at the bottom) and dashes (–) to indicate gaps in the sequences made by alignment. Sequence alignment and output were conducted using the CLUSTAL W Program ( ). doi:10.1128/9781555818463.ch21f1

Citation: Seo K, Bohach G. 2013. , p 547-573. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch21
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Image of Figure 21.2
Figure 21.2

Interactions between APC and T cells facilitated by conventional antigens (Ags) and superantigens (SAgs). Following processing by the APC, conventional Ags are presented to highly specific T-cell receptors (TCR) in association with the Ag-binding groove of the MHCII molecule. SAgs interact with MHCII molecules (without processing) outside the Ag binding groove. The SAg/MHCII bimolecular complex binds to the TCR through specificity determined only by the V region of the receptor α or β chain.doi:10.1128/9781555818463.ch21f2

Citation: Seo K, Bohach G. 2013. , p 547-573. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch21
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Figure 21.3

Tree representation demonstrating molecular relatedness of the currently known SE family and compared to TSST-1. This tree was created with the clustering feature of the PHYLIP program ( ). doi:10.1128/9781555818463.ch21f3

Citation: Seo K, Bohach G. 2013. , p 547-573. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch21
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Image of Figure 21.4
Figure 21.4

General characteristics of the locus in . This physical map shows the relative location of genes within the locus and other interacting regulatory genes and gene products (not drawn to scale). doi:10.1128/9781555818463.ch21f4

Citation: Seo K, Bohach G. 2013. , p 547-573. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch21
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Image of Figure 21.5
Figure 21.5

Schematic diagrams of the SEC3 crystal structure illustrating major structural features. Numerical designations defining the location of select residues and each α-helix and β-strand are shown within the two major domains. Also indicated are the N and C termini. The intramolecular disulfide linkage between Cys residues 93 and 110 (stick) connects the disulfide loop to the β5 strand containing the conserved residues ( Fig. 21.7 ) potentially important for emesis. The zinc atom bound by SEC3 faces the back of the SEC3 molecule between domains 1 and 2 and is coordinated by D83, H118, and H122. In contrast, the high-affinity zinc-binding site in SEA is positioned on the opposite edge of domain 2. The conformational topology of domain 1 is the same as the OB binding domains of several other proteins described in the text. doi:10.1128/9781555818463.ch21f5

Citation: Seo K, Bohach G. 2013. , p 547-573. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch21
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Image of Figure 21.6
Figure 21.6

(A) Schematic diagram of the SEA crystal structure. SEA has two MHCII binding sites. A relatively low-affinity MHCII binding occurs at a generic binding site that is conserved in most of SEs. A high-affinity MHCII binding site is located on the external surface of domain 2. This includes the high-affinity zinc-binding site, formed by His187, His225, and Asp227. The zinc ion mediates cross-linking of SEA with MHCII molecules and is crucial for maximal B- and T-cell activation. (B) A hypothetical model of MHCII-SEC-TCR complex based on the modeling predicted from the crystal structures of the SEC3-HLA-DR1 (low-affinity binding site) and SEB-Vβ complexes. doi:10.1128/9781555818463.ch21f6

Citation: Seo K, Bohach G. 2013. , p 547-573. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch21
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Figure 21.7

Comparison of cysteine loop and adjacent sequences for SEs and the analogous regions of the SEls. Evidence suggests that proper positioning of the critical downstream residues by a stable disulfide bond is required for emesis. Toxins designated as emetic are those reported as inducing emesis in the monkey feeding assay ( ). SEI was reported to be weakly emetic ( ). doi:10.1128/9781555818463.ch21f7

Citation: Seo K, Bohach G. 2013. , p 547-573. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch21
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Generic image for table
Table 21.1

General characteristics of selected species

Citation: Seo K, Bohach G. 2013. , p 547-573. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch21
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Table 21.2

Biochemical and functional properties of SEs

Citation: Seo K, Bohach G. 2013. , p 547-573. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch21
Generic image for table
Table 21.3

Prevalence of in several foods

Citation: Seo K, Bohach G. 2013. , p 547-573. In Doyle M, Buchanan R (ed), Food Microbiology. ASM Press, Washington, DC. doi: 10.1128/9781555818463.ch21

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