Skip NavigationSkip to Content
Return Return to Search Results

Antiretroviral potential of human tripartite motif-5 and related proteins

  1. Author:
    Zhang, F. W.
    Hatziioannou, T.
    Perez-Caballero, D.
    Derse, D.
    Bieniasz, P. D.

  2. Author Address

    Rockefeller Univ, Aaron Diamond AIDS Res Ctr, New York, NY 10016 USA. Rockefeller Univ, Lab Retrovirol, New York, NY 10016 USA. NCI, HIV Drug Resistance Program, NIH, Frederick, MD 21702 USA.;Bieniasz, PD, Rockefeller Univ, Aaron Diamond AIDS Res Ctr, 455 1st Ave, New York, NY 10016 USA.;pbienias@adarc.org
    1. Year: 2006
    2. Date: Sep
  2. Journal: Virology
    1. 353
    2. 2
    3. Pages: 396-409
  4. Type of Article: Article
  5. ISSN: 0042-6822
  1. Abstract:

    TRIM5 alpha is a potent inhibitor of infection by diverse retroviruses and is encoded by one of a large family of TRIM genes. We found that several TRIM motifs among a panel of selected human TRIM proteins (TRIM1, 5, 6, 18, 19, 2122, 34) could inhibit infection when artificially targeted to an incoming HIV-1 capsid. Conversely, when ectopically expressed as authentic full-length proteins, most lacked activity against a panel of retroviruses. The exceptions were TRIM1, TRIM5 and TRIM34 proteins. Weak but specific inhibition of HIV-2/SIVMAc and EIAV by TRIM34 was noted, and human TRIM5 a modestly, but specifically, inhibited an HIV-I strain carrying a mutation in the cyclophilin binding loop (G89V). Restriction activity observed in ectopic expression assays was sometimes not detectable in corresponding RNAi-based knockdown experiments. However, endogenous owl monkey TRIMCyp potently inhibited an SIVAGM strain. Overall, sporadic examples of intrinsic antiretroviral activity exist in this panel of TRIM proteins. (c) 2006 Elsevier Inc. All rights reserved.

    See More

  1. Keywords:

External Sources

  1. View Full Text
  2. DOI: 10.1016/j.virol.2006.05.035
  3. View record in Web of Science®
  4. WOS: 000240930900015

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