Skip NavigationSkip to Content
Return Return to Search Results

Characterization of the murine leukemia virus protease and its comparison with the human immunodeficiency virus type 1 protease

  1. Author:
    Feher, A.
    Boross, P.
    Sperka, T.
    Miklossy, G.
    Kadas, J.
    Bagossi, P.
    Oroszlan, S.
    Weber, I. T.
    Tozser, J.

  2. Author Address

    Debrecen Univ Med, Dept Biochem & Mol Biol, Res Ctr Mol Med, Med & Hlth Sci Ctr, H-4012 Debrecen, Hungary. Natl Canc Inst, HIV Drug Resistant Program, Frederick, MD USA. Georgia State Univ, Dept Biol, Atlanta, GA USA.;Tozser, J, Debrecen Univ Med, Dept Biochem & Mol Biol, Res Ctr Mol Med, Med & Hlth Sci Ctr, H-4012 Debrecen, Hungary.;tozser@indi.biochem.dote.hu
    1. Year: 2006
    2. Date: May
  2. Journal: Journal of General Virology
    1. 87
    2. Pages: 1321-1330
  4. Type of Article: Article
  5. ISSN: 0022-1317
  1. Abstract:

    The protease (PR) of Murine leukemia virus (MLV) was expressed in Escherichia coli, purified to homogeneity and characterized by using various assay methods, including HPLC-based, photometric and fluorometric activity measurements. The specificity of the bacterially expressed PR was similar to that of virion-extracted PR. Compared with human immunodeficiency virus type 1 (HIV-1) PR, the pH optimum of the MLV enzyme was higher. The specificity of the MLV PR was further compared with that of HIV-1 PR by using various oligopeptides representing naturally occurring cleavage sites in MLV and HIV-1, as well as by using bacterially expressed proteins having part of the MLV Gag. Inhibitors designed against HIV-1 PR were also active on MLV PR, although all of the tested ones were substantially less potent on this enzyme than on HIV-1 PR. Nevertheless, amprenavir, the most potent inhibitor against MLV PR, was also able to block Gag processing in MLV-infected cells. These results indicate that, in spite of the similar function in the life cycle of virus infection, the two PRs are only distantly related in their specificity.

    See More

  1. Keywords:

External Sources

  1. View Full Text
  2. DOI: 10.1099/vir.0.81382-0
  3. View record in Web of Science®
  4. WOS: 000237155300030

Library Notes

  1. No notes added.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel