Literature DB >> 12972148

Viroporins.

Maria Eugenia Gonzalez1, Luis Carrasco.   

Abstract

Viroporins are a group of proteins that participate in several viral functions, including the promotion of release of viral particles from cells. These proteins also affect cellular functions, including the cell vesicle system, glycoprotein trafficking and membrane permeability. Viroporins are not essential for the replication of viruses, but their presence enhances virus growth. Comprising some 60-120 amino acids, viroporins have a hydrophobic transmembrane domain that interacts with and expands the lipid bilayer. Some viroporins also contain other motifs, such as basic amino acid residues or a domain rich in aromatic amino acids that confers on the protein the ability to interact with the interfacial lipid bilayer. Viroporin oligomerization gives rise to hydrophilic pores at the membranes of virus-infected cells. As the list of known viroporins steadily grows, recent research efforts focus on deciphering the actions of the viroporins poliovirus 2B, alphavirus 6K, HIV-1 Vpu and influenza virus M2. All these proteins can enhance the passage of ions and small molecules through membranes depending on their concentration gradient. Future work will lengthen the list of viroporins and will provide a deeper understanding of their mechanisms of action.

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Year:  2003        PMID: 12972148     DOI: 10.1016/s0014-5793(03)00780-4

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  171 in total

1.  Open reading frame E3-10.9K of subspecies B1 human adenoviruses encodes a family of late orthologous proteins that vary in their predicted structural features and subcellular localization.

Authors:  Kathryn M Frietze; Samuel K Campos; Adriana E Kajon
Journal:  J Virol       Date:  2010-08-25       Impact factor: 5.103

2.  Oligomerization state and supramolecular structure of the HIV-1 Vpu protein transmembrane segment in phospholipid bilayers.

Authors:  Jun-Xia Lu; Simon Sharpe; Rodolfo Ghirlando; Wai-Ming Yau; Robert Tycko
Journal:  Protein Sci       Date:  2010-10       Impact factor: 6.725

3.  NMR structure and ion channel activity of the p7 protein from hepatitis C virus.

Authors:  Roland Montserret; Nathalie Saint; Christophe Vanbelle; Andrés Gerardo Salvay; Jean-Pierre Simorre; Christine Ebel; Nicolas Sapay; Jean-Guillaume Renisio; Anja Böckmann; Eike Steinmann; Thomas Pietschmann; Jean Dubuisson; Christophe Chipot; François Penin
Journal:  J Biol Chem       Date:  2010-07-28       Impact factor: 5.157

Review 4.  Ion channels as antivirus targets.

Authors:  Xin Liang; Zhi-Yuan Li
Journal:  Virol Sin       Date:  2010-07-28       Impact factor: 4.327

5.  Holin triggering in real time.

Authors:  Rebecca White; Shinobu Chiba; Ting Pang; Jill S Dewey; Christos G Savva; Andreas Holzenburg; Kit Pogliano; Ry Young
Journal:  Proc Natl Acad Sci U S A       Date:  2010-12-27       Impact factor: 11.205

6.  Secondary structure, dynamics, and architecture of the p7 membrane protein from hepatitis C virus by NMR spectroscopy.

Authors:  Gabriel A Cook; Stanley J Opella
Journal:  Biochim Biophys Acta       Date:  2010-08-18

Review 7.  Comparative NMR studies demonstrate profound differences between two viroporins: p7 of HCV and Vpu of HIV-1.

Authors:  Gabriel A Cook; Hua Zhang; Sang Ho Park; Yan Wang; Stanley J Opella
Journal:  Biochim Biophys Acta       Date:  2010-08-18

Review 8.  The human T-cell leukemia virus type 1 p13II protein: effects on mitochondrial function and cell growth.

Authors:  D M D'Agostino; M Silic-Benussi; H Hiraragi; M D Lairmore; V Ciminale
Journal:  Cell Death Differ       Date:  2005-08       Impact factor: 15.828

9.  Conformational changes induced by a single amino acid substitution in the trans-membrane domain of Vpu: implications for HIV-1 susceptibility to channel blocking drugs.

Authors:  Sang Ho Park; Stanley J Opella
Journal:  Protein Sci       Date:  2007-08-31       Impact factor: 6.725

10.  Identification of the cellular prohibitin 1/prohibitin 2 heterodimer as an interaction partner of the C-terminal cytoplasmic domain of the HIV-1 glycoprotein.

Authors:  Vanessa Emerson; Denise Holtkotte; Tanya Pfeiffer; I-Hsuan Wang; Martina Schnölzer; Tore Kempf; Valerie Bosch
Journal:  J Virol       Date:  2009-11-11       Impact factor: 5.103

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