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  Specific cleavage sites of Nef proteins from human immunodeficiency virus types 1 and 2 for the viral proteases

Schorr, J., Kellner, R., Fackler, O., Freund, J., Konvalinka, J., Kienzle, N., et al. (1996). Specific cleavage sites of Nef proteins from human immunodeficiency virus types 1 and 2 for the viral proteases. Journal of Virology, 70(12), 9051-9054. Retrieved from http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid%3D191010.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-3D89-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-3D8A-8
Genre: Journal Article
Alternative Title : Specific cleavage sites of Nef proteins from human immunodeficiency virus types 1 and 2 for the viral proteases

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JVirol_70_1996_9051.pdf (Any fulltext), 235KB
 
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 Creators:
Schorr, Jacqueline1, Author              
Kellner, Roland, Author
Fackler, O., Author
Freund, Jens1, Author              
Konvalinka, Jan, Author
Kienzle, N., Author
Kräusslich, Hans-Georg, Author
Mueller-Lantzsch, Nikolaus, Author
Kalbitzer, Hans Robert1, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 1996-04-181996-08-191996-12
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Journal of Virology
Source Genre: Journal
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Publ. Info: American Society for Microbiology (ASM)
Pages: - Volume / Issue: 70 (12) Sequence Number: - Start / End Page: 9051 - 9054 Identifier: ISSN: 0022-538X
CoNE: https://pure.mpg.de/cone/journals/resource/954925419045