Zinc regulates the function of two superantigens. Fraser JD, Urban RG, Strominger JL, Robinson H.Monoclonal antibody-superantigen fusion proteins: tumor-specific agents for T-cell-based tumor therapy.

Dohlsten M, Abrahmsén L, Björk P, Lando PA, Hedlund G, Forsberg G, Brodin T, Gascoigne NR, Förberg C, Lind P, et al.Monoclonal antibody-targeted superantigens: a different class of anti-tumor agents. Dohlsten M, Hedlund G, Akerblom E, Lando PA, Kalland T.Functionalized membrane supports for covalent protein microsequence analysis. Coull JM, Pappin DJ, Mark J, Aebersold R, Köster H.Nucleotide sequence of the type A staphylococcal enterotoxin gene. Genetic and molecular analyses of the gene encoding staphylococcal enterotoxin D. Structural basis of superantigen action inferred from crystal structure of toxic-shock syndrome toxin-1. Acharya KR, Passalacqua EF, Jones EY, Harlos K, Stuart DI, Brehm RD, Tranter HS.Characterization of two distinct MHC class II binding sites in the superantigen staphylococcal enterotoxin A. Abrahmsén L, Dohlsten M, Segrén S, Björk P, Jonsson E, Kalland T.Links to PubMed are also available for Selected References. Get a printable copy (PDF file) of the complete article (2.6M), or click on a page image below to browse page by page. Full textįull text is available as a scanned copy of the original print version. The unique feature of SED in forming a Zn2+-dependent homodimer seems to facilitate novel and biologically relevant multimeric interactions with MHC class II molecules, as shown by the induction of cytokine mRNA in human monocytes when exposed to SED and SED mutants. A second Zn2+ site is located on the surface close to the domain interface of the molecule. Two bound metal ions are coordinated by residues from both molecules in the dimer interface and thus contribute directly to formation of the dimer. The high affinity Zn2+ site used in dimer formation is located on the surface of the beta-sheet in the C-terminal domain. The three-dimensional structure of SED is similar to structures of other bacterial superantigens, although this study has revealed that SED has the unique capability of forming dimers in the presence of Zn2+. The crystal structure of SED has been determined in two different space groups, at 2.3 and 3.0 A resolution respectively. Staphylococcal enterotoxin D (SED) is dependent upon Zn2+ for high affinity interactions with MHC class II molecules and thus SED was co-crystallized with Zn2+. Bacterial superantigens, including the staphylococcal enterotoxins, are the most potent activators of T cells known and have been suggested as a causative factor in Gram-positive shock in humans.

Tranter graphics