Chapter 18 : Bacterial Toxins—Staphylococcal Enterotoxin B

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is a nonmotile, ubiquitous, gram-positive coccus which is a major human pathogen responsible for a wide range of infections, including skin and soft tissue infections, bacteremia, pneumonia, and several toxin-mediated diseases. Among many extracellular proteins, strains also secrete a variety of potent toxins which include alpha hemolysin, enterotoxins, leukocidins, and exfoliative toxins, all of which are directly associated with particular disease manifestations. To date, more than 33 enterotoxin sequences have been described in various genomes. Enterotoxins are heat stable and exert their effect on the epithelium of the intestinal tract when ingested, and thus, they are a common cause of food poisoning. Several enterotoxins are potent superantigens (SAgs) that, in a non-antigen (Ag)-dependent way, predominantly activate CD4 T cells ( ) but also activate other immune cells. The SAgs of include toxic shock syndrome toxin 1 (TSST-1), enterotoxin serotypes A to E and I (, , , , , and ), and enterotoxin-like serotypes G (), H (), and J to U ( to ). Of these SAgs, to have the ability to induce emesis in monkeys and are thus referred to as classic enterotoxins. The remaining SAgs either have not been tested for emetic activity or lack emetic activity and are therefore referred to as enterotoxin-like proteins (, , and to ). For the most part, staphylococcal SAgs are encoded by mobile genetic elements, which include extrachromosomal plasmids as well as chromosomal prophages, transposons, and pathogenicity islands. It is noteworthy that a chromosomally carried enterotoxin-like gene () was recently identified ( ). The gene is carried on the pathogenicity island SaPI3. The genes of SAgs , , , , and are located in the enterotoxin gene cluster (egc) and are among the most prevalent SAgs in clinical isolates. They are expressed by during logarithmic growth and shut off expression once a certain bacterial density is reached. Consequently, they do not induce a humoral response in the human host. In contrast, non-egc-associated SAgs (e.g., , , , and -) are expressed in late-logarithmic and stationary growth, induce a specific antibody (Ab) response in the human host, and are a prominent cause of cause toxic shock ( ).

Citation: Fries B, Varshney A. 2015. Bacterial Toxins—Staphylococcal Enterotoxin B, p 303-318. In Crowe J, Boraschi D, Rappuoli R (ed), Antibodies for Infectious Diseases. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.AID-0002-2012
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Figure 1

Alignment of amino acid sequences of SEB derived from clinical isolates. Amino acid mutations are highlighted in green. MHC- and TcR-interacting residues are shown in blue and magenta, respectively.

Citation: Fries B, Varshney A. 2015. Bacterial Toxins—Staphylococcal Enterotoxin B, p 303-318. In Crowe J, Boraschi D, Rappuoli R (ed), Antibodies for Infectious Diseases. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.AID-0002-2012
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Image of Figure 2
Figure 2

(A) Ribbon structure of SEB protein showing amino acid mutations in isolates. Residues which interact with MHC and TcR are shown in blue and magenta, respectively. (B) View after rotating 180 degrees around vertical axis.

Citation: Fries B, Varshney A. 2015. Bacterial Toxins—Staphylococcal Enterotoxin B, p 303-318. In Crowe J, Boraschi D, Rappuoli R (ed), Antibodies for Infectious Diseases. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.AID-0002-2012
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Major biological and pathological activities of SEB

Citation: Fries B, Varshney A. 2015. Bacterial Toxins—Staphylococcal Enterotoxin B, p 303-318. In Crowe J, Boraschi D, Rappuoli R (ed), Antibodies for Infectious Diseases. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.AID-0002-2012
Generic image for table

List of MAbs generated against SEB toxins

Citation: Fries B, Varshney A. 2015. Bacterial Toxins—Staphylococcal Enterotoxin B, p 303-318. In Crowe J, Boraschi D, Rappuoli R (ed), Antibodies for Infectious Diseases. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.AID-0002-2012

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