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RESEARCH PRODUCT
Major histocompatibility complex class II binding site for streptococcal pyrogenic (erythrogenic) toxin A.
Udo F. HartwigBernhard FleischerBernhard FleischerDieter Gerlachsubject
Microbiology (medical)Recombinant Fusion ProteinsT-LymphocytesImmunologyAntigen presentationErythrogenic toxinBacterial ToxinsMolecular Sequence DataExotoxinsEnterotoxinmedicine.disease_causeMajor histocompatibility complexLymphocyte ActivationMicrobiologyCell LineMajor Histocompatibility ComplexEnterotoxinsMicestomatognathic systemBacterial ProteinsmedicineEscherichia coliImmunology and AllergyAnimalsHumansCells CulturedMice Inbred BALB CBinding SitesSuperantigensbiologyBase SequencePyrogensToxic shock syndromeMembrane ProteinsStreptococcusGeneral MedicineGene Expression Regulation BacterialHLA-DR Antigensmedicine.diseasebiology.organism_classificationSpeaStreptococcus pyogenesbiology.proteinExotoxindescription
Streptococcal pyrogenic exotoxin A (SPEA) is an important pathogenicity factor of group A streptococci. It is a member of the family of „superantigens” produced by Staphylococcus aureus and Streptococcus pyogenes and its T lymphocyte stimulating activity is involved into the pathogenesis of certain diseases caused by pyogenic streptococci. In this study we have produced and characterized recombinant SPEA molecules in Escherichia coli. These molecules are indistinguishable from natural SPEA in both T cell stimulatory and HLA class II binding activities. Human class II molecules are more efficient than mouse class II molecules in presenting SPEA to T cells. In binding tests to major histocompatibility complex class II-positive cells SPEA competes with staphylococcal enterotoxin B and A but not with toxic shock syndrome toxin-1.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1994-11-01 | Medical microbiology and immunology |