التفاصيل البيبلوغرافية
العنوان: |
Concomitant loss of conformation and superantigenic activity of staphylococcal enterotoxin B deletion mutant proteins |
المؤلفون: |
Metzroth, B, Marx, T, Linnig, M, Fleischer, B |
المصدر: |
Infection and Immunity ; volume 61, issue 6, page 2445-2452 ; ISSN 0019-9567 1098-5522 |
بيانات النشر: |
American Society for Microbiology |
سنة النشر: |
1993 |
الوصف: |
The T-cell-stimulating activity of staphylococcal enterotoxin B (SEB) is an important factor in the pathogenesis of certain staphylococcal diseases. To investigate the immunologically active domains of the SEB molecule, we have produced truncated fragments of recombinant SEB by C-terminal and N-terminal deletions. The fragments were expressed as fusion proteins with protein A, including a cleavage site to remove the protein A part. Mutant proteins were tested for the ability to stimulate human resting T cells and SEB-reactive T-cell clones. Deletion of only 9 amino acids from the C terminus leads to complete loss of T-cell-stimulating activity. Removing further amino acids from the SEB molecule did not lead to a reexpression of T-cell-mitogenic activity. A mutant protein, however, in which the 9 C-terminal amino acids were replaced with a tail of 68 amino acids encoded by the vector was fully active. Two mutant proteins with N-terminal deletions of 60 and 81 amino acids were inactive as well. A neutralizing monoclonal antibody against a conformational epitope lost binding with all the inactive mutant proteins only, whereas a monoclonal antibody recognizing an epitope involved in emetic activity reacted with all mutant proteins. These results suggest that even small deletions at the C terminus affect the three-dimensional conformation of the SEB molecule. |
نوع الوثيقة: |
article in journal/newspaper |
اللغة: |
English |
DOI: |
10.1128/iai.61.6.2445-2452.1993 |
الإتاحة: |
https://doi.org/10.1128/iai.61.6.2445-2452.1993Test |
حقوق: |
https://journals.asm.org/non-commercial-tdm-licenseTest |
رقم الانضمام: |
edsbas.62E7F92 |
قاعدة البيانات: |
BASE |