Identification of the staphylococcal enterotoxin A superantigen binding site in the beta 1 domain of the human histocompatibility antigen HLA-DR.
A Herman, N Labrecque, J Thibodeau… - Proceedings of the …, 1991 - National Acad Sciences
The staphylococcal enterotoxin A (SEA) is a superantigen that must bind to class II
molecules of the major histocompatibility complex to be recognized by T cells. In humans …
molecules of the major histocompatibility complex to be recognized by T cells. In humans …
Staphylococcal enterotoxins A and B share a common structural motif for binding class II major histocompatibility complex molecules
RG Ulrich, S Bavari, MA Olson - Nature structural biology, 1995 - nature.com
A comparative site-directed mutagenesis study of staphylococcal enterotoxins A and B was
undertaken to identify key amino-acid residues which govern interactions with major …
undertaken to identify key amino-acid residues which govern interactions with major …
The crystal structure of staphylococcal enterotoxin type D reveals Zn2+‐mediated homodimerization.
M Sundström, L Abrahmsen, P Antonsson… - The EMBO …, 1996 - embopress.org
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 …
activators of T cells known and have been suggested as a causative factor in Gram‐positive …
Staphylococcal enterotoxin A has two cooperative binding sites on major histocompatibility complex class II.
KR Hudson, RE Tiedemann, RG Urban… - The Journal of …, 1995 - rupress.org
The superantigen staphylococcal enterotoxin A (SEA) binds to major histocompatibility
complex (MHC) class II molecules at two sites on either side of the peptide groove. Two …
complex (MHC) class II molecules at two sites on either side of the peptide groove. Two …
Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides.
TS Jardetzky, JH Brown, JC Gorga… - Proceedings of the …, 1996 - National Acad Sciences
The structure of the human major histocompatibility complex (MHC) class II molecule HLA-
DR1 derived from the human lymphoblastoid cell line LG-2 has been determined in a …
DR1 derived from the human lymphoblastoid cell line LG-2 has been determined in a …
Crystal structure of the superantigen enterotoxin C2 from Staphylococcus aureus reveals a zinc-binding site
AC Papageorgiou, KR Acharya, R Shapiro… - Structure, 1995 - cell.com
Background: Staphylococcus aureus enterotoxin C2 (SEC2) belongs to a family of proteins,
termed 'superantigens', that form complexes with class II MHC molecules enabling them to …
termed 'superantigens', that form complexes with class II MHC molecules enabling them to …
Cross-linking of MHC class II molecules by staphylococcal enterotoxin A is essential for antigen-presenting cell and T cell activation.
RE Tiedemann, JD Fraser - Journal of immunology (Baltimore, Md …, 1996 - journals.aai.org
Two binding sites for MHC class II have previously been identified on opposite sides of the
superantigen, staphylococcal enterotoxin A (SEA). The sites mediate separate binding …
superantigen, staphylococcal enterotoxin A (SEA). The sites mediate separate binding …
Major histocompatibility complex class II‐associated peptides determine the binding of the superantigen toxic shock syndrome toxin‐1
A von Bonin, S Ehrlich, G Malcherek… - European journal of …, 1995 - Wiley Online Library
Superantigens bind to major histocompatibility complex (MHC) class II proteins and interact
with variable parts of the T cell antigen receptor (TCR) β‐chain. Cross‐linking the TCR with …
with variable parts of the T cell antigen receptor (TCR) β‐chain. Cross‐linking the TCR with …
Crystal structure of the superantigen staphylococcal enterotoxin type A.
EM Schad, I Zaitseva, VN Zaitsev, M Dohlsten… - The EMBO …, 1995 - embopress.org
Staphylococcal enterotoxins are prototype superantigens characterized by their ability to
bind to major histocompatibility complex (MHC) class II molecules and subsequently activate …
bind to major histocompatibility complex (MHC) class II molecules and subsequently activate …
Isolation of HLA-DR1.(staphylococcal enterotoxin A) 2 trimers in solution.
RE Tiedemann, RJ Urban… - Proceedings of the …, 1995 - National Acad Sciences
Mutational studies indicate that the superantigen staphylococcal enterotoxin A (SEA) has
two separate binding sites for major histocompatibility complex (MHC) class II molecules …
two separate binding sites for major histocompatibility complex (MHC) class II molecules …