4.4 Article

Protein complexes associated with the Kaposi's sarcoma-associated herpesvirus-encoded LANA

Journal

VIROLOGY
Volume 364, Issue 2, Pages 317-329

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2007.03.010

Keywords

proteomics; latency-associated nuclear antigen; KSHV

Categories

Funding

  1. NCI NIH HHS [R01 CA091792-05, CA091792, R01 CA091792-06, R29 CA072150-06, R01 CA091792-03, R01 CA091792-02, R01 CA072150-12, CA108461, R29 CA072150, R01 CA072150, CA072510, R01 CA072150-08, R01 CA072150-11, R01 CA091792-01A1, R01 CA108461, R01 CA091792, R01 CA072150-09, R01 CA072150-10, R01 CA091792-04] Funding Source: Medline
  2. NIAID NIH HHS [R01 AI067037-01A2, AI067037, R01 AI067037] Funding Source: Medline
  3. NIDCR NIH HHS [R01 DE017338, R01 DE017338-01, R01 DE017338-02, R01 DE017338-03, R01 DE014136, DE017338, R01 DE014136-06, DE01436] Funding Source: Medline

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Kaposi's sarcoma-associated herpesvirus (KSHV) is the major biological cofactor contributing to development of Kaposi's sarcoma. KSHV establishes a latent infection in human B cells expressing the latency-associated nuclear antigen (LANA), a critical factor in the regulation of viral latency. LANA is known to modulate viral and cellular gene expression. We report here on some initial proteomic studies to identify cellular proteins associated with the amino and carboxy-terminal domains of LANA. The results of these studies show an association of known cellular proteins which support LANA functions and have identified additional LANA-associated proteins. These results provide new evidence for complexes involving LANA with a number of previously unreported functional classes of proteins including DNA polymerase, RNA helicase and cell cycle control proteins. The results also indicate that the amino terminus of LANA can interact with its carboxy-terminal domain. This interaction is potentially important for facilitating associations with other cell cycle regulatory proteins which include CENP-F identified in association with both the amino and carboxy-termini. These novel associations add to the diversity of LANA functions in relation to the maintenance of latency and subsequent transformation of KSHV infected cells. (c) 2007 Elsevier Inc. All rights reserved.

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