PMID- 9079821
OWN - NLM
STAT- MEDLINE
DCOM- 19970429
LR  - 20071114
IS  - 0014-2980 (Print)
IS  - 0014-2980 (Linking)
VI  - 27
IP  - 3
DP  - 1997 Mar
TI  - Carboxy-terminal residues of major histocompatibility complex class II-associated 
      peptides control the presentation of the bacterial superantigen toxic shock 
      syndrome toxin-1 to T cells.
PG  - 772-81
AB  - Previous studies have shown that the presentation of some bacterial superantigens 
      by major histocompatibility complex (MHC) class II molecules is strongly 
      influenced by class II-associated peptides. For example, presentation of the 
      toxic shock syndrome toxin-1 (TSST-1) superantigen by 
      antigen-processing-defective T2-I-Ab cells (which expresses I-Ab that is either 
      empty or associated with invariant chain-derived peptides) can be strongly 
      enhanced by some, but not other, I-Ab-binding peptides. Here we investigate the 
      contribution of I-Ab-associated peptides in the presentation of TSST-1 to T 
      cells. The data show that overlapping peptides expressing the same core 
      I-Ab-restricted epitope, but with various N and C termini, can differ profoundly 
      in their ability to promote TSST-1 presentation to T cells. Analysis of altered 
      and truncated peptides indicates that residues at the C-terminal end of the 
      peptide have a dramatic effect on TSST-1 presentation. This effect does not 
      involve a cognate interaction between the peptide and the TSST-1 molecule, but 
      appears to depend on the length of the C-terminal region. These data are 
      consistent with crystallographic studies suggesting that TSST-1 may interact with 
      the C-terminal residues of MHC class II-associated peptides. We also examined the 
      capacity of naturally processed peptides to promote TSST-1 binding using a 
      superantigen blocking assay. The data demonstrated that a naturally processed 
      epitope is dominated by peptides that do not promote strong TSST-1 binding to 
      I-Ab. Taken together, these data suggest that TSST-1 binding to MHC class II 
      molecules is controlled by the C-terminal residues of the associated peptide, and 
      that many naturally processed peptide/class II complexes do not present TSST-1 to 
      T cells. Thus, the peptide dependence of TSST-1 binding to class II molecules may 
      significantly reduce the capacity of TSST-1 to stimulate T cells.
FAU - Wen, R
AU  - Wen R
AD  - Department of Immunology, St. Jude Children's Research Hospital, Memphis, TN 
      38105, USA.
FAU - Broussard, D R
AU  - Broussard DR
FAU - Surman, S
AU  - Surman S
FAU - Hogg, T L
AU  - Hogg TL
FAU - Blackman, M A
AU  - Blackman MA
FAU - Woodland, D L
AU  - Woodland DL
LA  - eng
GR  - AI-09585/AI/NIAID NIH HHS/United States
GR  - AI-31596/AI/NIAID NIH HHS/United States
GR  - CA-56570/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - Germany
TA  - Eur J Immunol
JT  - European journal of immunology
JID - 1273201
RN  - 0 (Bacterial Toxins)
RN  - 0 (Enterotoxins)
RN  - 0 (Histocompatibility Antigens Class II)
RN  - 0 (Peptides)
RN  - 0 (Superantigens)
RN  - 0 (enterotoxin F, Staphylococcal)
RN  - 39424-53-8 (enterotoxin B, staphylococcal)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antigen-Presenting Cells/*physiology
MH  - *Bacterial Toxins
MH  - Enterotoxins/*immunology
MH  - Epitope Mapping
MH  - Histocompatibility Antigens Class II/*immunology
MH  - Hybridomas
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Molecular Sequence Data
MH  - Peptides/chemistry/*immunology
MH  - Protein Binding
MH  - Structure-Activity Relationship
MH  - Superantigens/*immunology
EDAT- 1997/03/01 00:00
MHDA- 1997/03/01 00:01
CRDT- 1997/03/01 00:00
PHST- 1997/03/01 00:00 [pubmed]
PHST- 1997/03/01 00:01 [medline]
PHST- 1997/03/01 00:00 [entrez]
AID - 10.1002/eji.1830270328 [doi]
PST - ppublish
SO  - Eur J Immunol. 1997 Mar;27(3):772-81. doi: 10.1002/eji.1830270328.