التفاصيل البيبلوغرافية
| العنوان: |
Specific cleavage sites of Nef proteins from human immunodeficiency virus types 1 and 2 for the viral proteases |
| المؤلفون: |
Schorr, J, Kellner, R, Fackler, O, Freund, J, Konvalinka, J, Kienzle, N, Kräusslich, H G, Mueller-Lantzsch, N, Kalbitzer, H R |
| المصدر: |
Journal of Virology ; volume 70, issue 12, page 9051-9054 ; ISSN 0022-538X 1098-5514 |
| بيانات النشر: |
American Society for Microbiology |
| سنة النشر: |
1996 |
| الوصف: |
Human immunodeficiency virus type 2 (HIV-2) Nef is proteolytically cleaved by the HIV-2-encoded protease. The proteolysis is not influenced by the absence or presence of the N-terminal myristoylation. The main cleavage site is located between residues 39 and 40, suggesting a protease recognition sequence, GGEY-SQFQ. As observed previously for Nef protein from HIV-1, a large, stable core domain with an apparent molecular mass of 30 kDa is produced by the proteolytic activity. Cleavage of Nef from HIV-1 in two domains by its own protease or the protease from HIV-2 is also independent of Nef myristoylation. However, processing of HIV-1 Nef by the HIV-2 protease is less selective than that by the HIV-1 protease: the obtained core fragment is heterogeneous at its N terminus and has an additional cleavage site between amino acids 99 and 100. Preliminary experiments suggest that the full-length Nef of HIV-2 and the core domain are part of the HIV-2 particles, analogous to the situation reported recently for HIV-1. |
| نوع الوثيقة: |
article in journal/newspaper |
| اللغة: |
English |
| DOI: |
10.1128/jvi.70.12.9051-9054.1996 |
| الإتاحة: |
https://doi.org/10.1128/jvi.70.12.9051-9054.1996Test |
| حقوق: |
https://journals.asm.org/non-commercial-tdm-licenseTest |
| رقم الانضمام: |
edsbas.F84BADB3 |
| قاعدة البيانات: |
BASE |
