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PDZD8 is a novel moesin-interacting cytoskeletal regulatory protein that suppresses infection by herpes simplex virus type 1.

Abstract
The host cytoskeleton plays a central role in the life cycle of many viruses yet our knowledge of cytoskeletal regulators and their role in viral infection remains limited. Recently, moesin and ezrin, two members of the ERM (Ezrin/Radixin/Moesin) family of proteins that regulate actin and plasma membrane cross-linking and microtubule (MT) stability, have been shown to inhibit retroviral infection. To further understand how ERM proteins function and whether they also influence infection by other viruses, we identified PDZD8 as a novel moesin-interacting protein. PDZD8 is a poorly understood protein whose function is unknown. Exogenous expression of either moesin or PDZD8 reduced the levels of stable MTs, suggesting that these proteins functioned as part of a cytoskeletal regulatory complex. Additionally, exogenous expression or siRNA-mediated knockdown of either factor affected Herpes Simplex Virus type 1 (HSV-1) infection, identifying a cellular function for PDZD8 and novel antiviral properties for these two cytoskeletal regulatory proteins.
AuthorsMatthew S Henning, Patricia Stiedl, Denis S Barry, Robert McMahon, Scott G Morham, Derek Walsh, Mojgan H Naghavi
JournalVirology (Virology) Vol. 415 Issue 2 Pg. 114-21 (Jul 05 2011) ISSN: 1096-0341 [Electronic] United States
PMID21549406 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
CopyrightPublished by Elsevier Inc.
Chemical References
  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins
  • Cytoskeletal Proteins
  • Microfilament Proteins
  • PDZD8 protein, human
  • moesin
Topics
  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins (genetics, metabolism)
  • Cell Line
  • Cytoskeletal Proteins (genetics, metabolism)
  • Down-Regulation
  • Herpes Simplex (metabolism, virology)
  • Herpesvirus 1, Human (physiology)
  • Humans
  • Microfilament Proteins (genetics, metabolism)
  • Microtubules (chemistry, metabolism)
  • Protein Binding
  • Virus Replication

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