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Chapter 21 : Staphylococcal and Streptococcal Superantigens

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Staphylococcal and Streptococcal Superantigens, Page 1 of 2

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Abstract:

This chapter discusses the superantigens (SAgs) of and . The classic SAgs form a large family of related proteins that lack detectable enzymatic function but rather function to cross-link major histocompatibility complex (MHC) class II molecules on antigen-presenting cells (APCs) with certain T-cell receptors (TCRs), primarily those of the CD4 lineage. Staphylococcal and streptococcal SAgs are single-polypeptide-chain, nonglycosylated proteins of 22 to 30 kDa. TSST-1 is encoded on SaPIs 1, 2, and bovine. SaPIs are approximately 15.2 kb in size and are present in a single, but not necessarily the same, site in the chromosome. Mutagenesis studies provided evidence that the cystine loop of SE C1 is required for emesis. SAgs interact with TCR outside the typical TCR region for contact with antigenic peptide and MHC class II. The massive release of these cytokines can cause hypotension through capillary leak mediated by the nitric oxide pathway, with consequent effects on the endothelium. SAgs are most often associated with TSS illnesses. Staphylococci and streptococci are common pathogens of humans, and as such have myriad cell surface virulence factors that contribute to colonization and immune avoidance. Most of the SAgs are made during the postexponential phase of growth (excluding SE A, K, and Q, which are exponential phase regulated), when cell numbers are highest and the organisms are most likely to spread to new hosts.

Citation: Schlievert P. 2003. Staphylococcal and Streptococcal Superantigens, p 293-308. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch21

Key Concept Ranking

MHC Class II
0.7172354
Bacterial Proteins
0.6257007
Immune Systems
0.49078423
Toxic Shock Syndrome
0.45963666
0.7172354
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Figures

Image of Figure 1
Figure 1

Ribbon diagram of TSST-1. The -carbon backbone of the toxin is shown, highlighting the A and B domains of the toxin in the standard view. The TCR-binding domain on TSST-1 is on the top back of the toxin. The site for binding MHC class II is the lowaffinity site to the right of the toxin in domain B. Some SAgs, but not TSST-1, have a zinc-dependent, high-affinity MHC class II binding site in the position shown to the left of TSST-1.

Citation: Schlievert P. 2003. Staphylococcal and Streptococcal Superantigens, p 293-308. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch21
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Image of Figure 2
Figure 2

Genetic structure of SaPI 3. The PI is 15.7 kb. The attachment sites left and right (attand att) for integration into the bacterial chromosome are indicated. Putative genes (identified only as open reading frames greater than 5,000 base pairs) are numbered, including 19 (which has similarity to cI repressor from phage lambda), 20 (which has similarity to a phage protein from ), and 21 (which has similarity to an ABC transporter). Direction of transcription of genes is indicated by arrows. encodes a protein of unknown function that is secreted in very high concentrations. , , and encode staphylococcal enterotoxins; encodes a putative integrase.

Citation: Schlievert P. 2003. Staphylococcal and Streptococcal Superantigens, p 293-308. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch21
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Image of Figure 3
Figure 3

Ribbon diagrams of the SAgs (darker gray) SE B (A), SPE C (B), and SE A (C) complexed with MHC class II molecules (lighter gray). The and indicate the chains of the MHC class II molecules. Small ribbon structures in the groove of the MHC class II molecules are the antigenic peptides. Sphere in SPE C and SE A structures is the zinc atom in the high-affinity MHC class II interaction site.

Citation: Schlievert P. 2003. Staphylococcal and Streptococcal Superantigens, p 293-308. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch21
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Image of Figure 4
Figure 4

Schematic (top) and ribbon (bottom) diagrams of the interaction of antigenic peptide (Ag, small ribbon in bottom structures) and SAg, (SE B) with the TCR - and -chains and the - and -chains of MHC class II molecules.

Citation: Schlievert P. 2003. Staphylococcal and Streptococcal Superantigens, p 293-308. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch21
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References

/content/book/10.1128/9781555817893.chap21
1. Dinges, M. M.,, P. M. Orwin,, and P. M. Schlievert. 2000. Exotoxins of Staphylococcus aureus. Clin. Microbiol. Rev. 13:1634.
2. Kotzin, B. L.,, D. Y. Leung,, J. Kappler,, and P. Marrack. 1993. Superantigens and their potential role in human disease. Adv. Immunol. 54:99166.
3. Li, H.,, A. Llera,, E. L. Malchiodi,, and R. A. Mariuzza. 1999. The structural basis of T cell activation by superantigens. Annu. Rev. Immunol. 17:435466.
4. Li, H.,, A. Llera,, D. Tsuchiya,, L. Leder,, X. Ysern,, P. M. Schlievert,, K. Karjalainen,, and R. A. Mariuzza. 1998. Three-dimensional structure of the complex between a T cell receptor beta chain and the superantigen staphylococcal enterotoxin B. Immunity 9:807816.
5. Li, Y.,, H. Li,, N. Dimasi,, J. K. McCormick,, R. Martin,, P. Schuck,, P. M. Schlievert,, and R. A. Mariuzza. 2001. Crystal structure of a superantigen bound to the highaffinity, zinc-dependent site on MHC class II. Immunity 14:93104.
6. Marrack, P.,, and J. Kappler. 1990. The staphylococcal enterotoxins and their relatives. Science 248:705711.
7. McCormick, J. K.,, J. M. Yarwood,, and P. M. Schlievert. 2001. Toxic shock syndrome and bacterial superantigens: an update. Annu. Rev. Microbiol. 55:77104.
8. Parsonnet, J.,, Z. A. Gillis,, A. G. Richter,, and G. B. Pier. 1987. A rabbit model of toxic shock syndrome that uses a constant, subcutaneous infusion of toxic shock syndrome toxin 1. Infect. Immun. 55:10701076.
9. Schlievert, P. M.,, M. Y. Kotb,, and D. L. Stevens,. 2000. Streptococcal superantigens: streptococcal toxic shock syndrome. In M. W. Cunningham, and R. S. Fujinami (ed.), Effects of Microbes on the Immune System. Lippincott Williams & Wilkins, Philadelphia, Pa.
1. Leung, D. Y. M.,, B. T. Huber,, and P. M. Schlievert. 1997. Superantigens: Relevence to Human Disease and Basic Biology. Marcel Dekker, Inc., New York, N.Y.

Tables

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Table 1

Known and proposed bacterial and viral T-cell SAgs

Citation: Schlievert P. 2003. Staphylococcal and Streptococcal Superantigens, p 293-308. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch21
Generic image for table
Table 2

Properties of staphylococcal and streptococcal SAgs

Citation: Schlievert P. 2003. Staphylococcal and Streptococcal Superantigens, p 293-308. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch21
Generic image for table
Table 3

Biological activities of staphylococcal and streptococcal SAgs

Citation: Schlievert P. 2003. Staphylococcal and Streptococcal Superantigens, p 293-308. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch21
Generic image for table
Table 4

Skin test reactivity of staphylococcal and streptococcal SAgs

Citation: Schlievert P. 2003. Staphylococcal and Streptococcal Superantigens, p 293-308. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch21
Generic image for table
Table 5

Diagnostic criteria for staphylococcal and streptococcal TSS

Citation: Schlievert P. 2003. Staphylococcal and Streptococcal Superantigens, p 293-308. In Burns D, Barbieri J, Iglewski B, Rappuoli R (ed), Bacterial Protein Toxins. ASM Press, Washington, DC. doi: 10.1128/9781555817893.ch21

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