Medical Journals

Deletion of a Cys-his Motif from the Alpharetrovirus Nucleocapsid Domain Reveals Late Domain Mutant-like Budding Defects.

Authors:
  • Lee Eun-Gyung
  • Linial Maxine L

From: Division of Basic Sciences, Fred Hutchinson Cancer Research Center, 1100 Fairview Ave. N., Seattle, WA 98109-1024, USA.

Virology

  • Publish Date: Mar 2006
  • ISSN: 0042-6822
  • Volume: 347
  • Issue: 1
  • Pages: 226-33
  • Medium: Print
  • Language: English
  • Citation (JAMA): Lee Eun-Gyung, Linial Maxine L, et al. Deletion of a Cys-his Motif from the Alpharetrovirus Nucleocapsid Domain Reveals Late Domain Mutant-like Budding Defects.. Virology Mar 2006;347:226-33

Abstract

The Rous sarcoma virus (RSV) Gag polyprotein is the only protein required for virus assembly and release. We previously found that deletion of either one of the two Cys-His (CH) motifs in the RSV nucleocapsid (NC) protein did not abrogate Gag-Gag interactions, RNA binding, or packaging but greatly reduced virus production (E-G. Lee, A. Alidina et al., J. Virol. 77: 2010-2020, 2003). In this report, we have further investigated the effects of mutations in the CH motifs on virus assembly and release. Precise deletion of either CH motif, without affecting surrounding basic residues, reduced virus production by approximately 10-fold, similar to levels seen for late (L) domain mutants. Strikingly, transmission electron microscopy revealed that virions of both DeltaCH1 and DeltaCH2 mutants were assembled normally at the plasma membrane but were arrested in budding. Virus particles remained tethered to the membrane or to each other, reminiscent of L domain mutants, although the release defect appears to be independent of the L domain functions. Therefore, two CH motifs are likely to be required for budding independent of a requirement for either Gag-Gag interactions or RNA packaging.

Mesh Headings (Keywords): Amino Acid Motifs, Amino Acid Sequence, Animals, Avian Sarcoma Viruses, Cell Line, Microscopy, Electron, Molecular Sequence Data, Nucleocapsid Proteins, Phenotype, Protein Structure, Tertiary, Quail, Retroviridae Proteins, Sequence Deletion, Transfection, Two-Hybrid System Techniques, Virus Assembly


Check for Full Text / PubMed Unique Identifier (PMID): 16406458


This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.

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The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.


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