Bovine leukemia virus protease: comparison with human T-lymphotropic virus and human immunodeficiency virus proteases.

Bovine leukemia virus protease: comparison with human T-lymphotropic virus and human immunodeficiency virus proteases. Research Abstract Details 

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Bovine leukemia virus protease: comparison with human T-lymphotropic virus and human immunodeficiency virus proteases. Abstract Text:

Sperka,Gabriella ,Yunfeng Tie, Bagossi, Zahuczky, Boross,Krisztina ,Robert W Harrison,Irene T Weber, ,

Bovine leukemia virus (BLV) is a valuable model system for understanding human T-lymphotropic virus 1 (HTLV-1); the availability of an infectious BLV clone, together with animal-model systems, will help to explore anti-HTLV-1 strategies. Nevertheless, the specificity and inhibitor sensitivity of the BLV protease (PR) have not been characterized in detail. To facilitate such studies, a molecular model for the enzyme was built. The specificity of the BLV PR was studied with a set of oligopeptides representing naturally occurring cleavage sites in various retroviruses. Unlike HTLV-1 PR, but similar to the human immunodeficiency virus 1 (HIV-1) enzyme, BLV PR was able to hydrolyse the majority of the peptides, mostly at the same position as did their respective host PRs, indicating a broad specificity. When amino acid residues of the BLV PR substrate-binding sites were replaced by equivalent ones of the HIV-1 PR, many substitutions resulted in inactive protein, indicating a great sensitivity to mutations, as observed previously for the HTLV-1 PR. The specificity of the enzyme was studied further by using a series of peptides containing amino acid substitutions in a sequence representing a naturally occurring HTLV-1 PR cleavage site. Also, inhibitors of HIV-1 PR, HTLV-1 PR and other retroviral proteases were tested on the BLV PR. Interestingly, the BLV PR was more susceptible than the HTLV-1 PR to the inhibitors tested. Therefore, despite the specificity differences, in terms of mutation intolerance and inhibitor susceptibility of the PR, BLV and the corresponding animal-model systems may provide good models for testing of PR inhibitors that target HTLV-1.

Bovine leukemia virus protease: comparison with human T-lymphotropic virus and human immunodeficiency virus proteases. Publishing Authors By Initials

T Sperka,G ,Y Tie,P Bagossi,G Zahuczky,P Boross,K ,RW Harrison,IT Weber,J ,

For similar proteins: viral proteins research abstracts see: proteins: viral proteins research

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Bovine leukemia virus protease: comparison with human T-lymphotropic virus and human immunodeficiency virus proteases. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of general virology

VOLUME: 88

Page Numbers: 2052-63

Journal Abbreviation: J. Gen. Virol.

ISSN: 0022-1317

DAY: 3

MONTH: Jul

YEAR: 2007

Bovine leukemia virus protease: comparison with human T-lymphotropic virus and human immunodeficiency virus proteases. Information

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LANGUAGE: eng

NlmUniqueID: 77340

Bovine leukemia virus protease: comparison with human T-lymphotropic virus and human immunodeficiency virus proteases. Keywords Mesh Terms:

KEYWORDS: Viral Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Bovine leukemia virus protease: comparison with human T-lymphotropic virus and human immunodeficiency virus proteases. Information

Substance Name: Peptide Hydrolases

Registry Number: EC 3.4.-

Grant and Affiliation Information for Bovine leukemia virus protease: comparison with human T-lymphotropic virus and human immunodeficiency virus proteases.

AFFILIATION: Department of Biochemistry and Molecular Biology, Research Center for Molecular Medicine, Medical and Health Science Center, University of Debrecen, Hungary.

Country: England

AGENCY: United States FIC

GRANT: TW01001

ACRONYM: TW

MEDLINETA: J Gen Virol

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