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Shocking! The Effect of TSST‐1 in Toxic Shock Syndrome
Author(s) -
Arnholt Mark,
Munzenmaier Diane H,
Anderson Evelyn,
Benson Cassidy,
Brown Julia,
Colwell Margaret,
Colwell Theodore,
Flanagan Michael,
Hautala Lauren,
Hennes Delaney,
Hoffmann Gabriel,
Kennedy Cara,
Lisowski Leah,
Stoeckmann Tate,
Witt Emma,
Zuern Rachel
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.lb297
Subject(s) - superantigen , toxic shock syndrome , immune system , staphylococcus aureus , major histocompatibility complex , biology , mutant , immunology , microbiology and biotechnology , chemistry , t cell , genetics , gene , bacteria
Almost 20% of children who die of Sudden Infant Death Syndrome have a protein called Toxic Shock Syndrome Toxin‐1 (TSST‐1), produced by Staphylococcus aureus. This protein is also responsible for toxic shock and food poisoning. S. aureus produces this superantigen TSST‐1 to divert the immune system and multiply rapidly inside the body. TSST‐1 contains 194 amino acids and three domains. Identical domains A, B, and C consist of a larger alpha‐helix, residues 152‐168, along with two beta‐sheets, and three shorter alpha helices. The long alpha helix defines the protein as a superantigen. Antigen‐presenting cells, such as macrophages, contain Major Histocompatibility Complex class II. These domains are bound to T‐cell receptor beta sheets by TSST‐1, bypassing the normal interface, and activating up to 24% more than the average immune response. Despite TSST‐1 having no disulfide bridges, therefore lack of thermal denaturation resistance, TSST‐1 thrives in the human body due to an immune system distraction. TSST‐1 can move through mucous membranes, allowing S. aureus to disrupt the immune response without being inside the body. In the wild form of TSST‐1, His‐135 located adjacent to the long alpha‐helix is mutated to Alanine, creating mutant TSST‐1, making the superantigen inactive for reasons unknown. The HUHS SMART Team (Students Modeling A Research Topic) Team has designed a model of the wild form of TSST‐1 with 3D printing technology to investigate structure_function relationships. By studying how TSST‐1 interacts with the immune system, advances can be made to control the spread of these pyrogenic toxin superantigens. Support or Funding Information The MSOE Center for BioMolecular Modeling would like to acknowledge and thank the National Institutes of Health Clinical and Translational Science Award (NIH_CTSA UL1RR031973) and the Milwaukee School of Engineering for their support in funding the 2018_2019 SMART Team program. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .