The envelope glycoprotein of human endogenous retrovirus HERV-W induces cellular resistance to spleen necrosis virus

2003 ◽  
Vol 148 (4) ◽  
pp. 659-675 ◽  
Author(s):  
V. G. Ponferrada ◽  
B. S. Mauck ◽  
D. P. Wooley
Keyword(s):  
Envelope Glycoprotein ◽  
Endogenous Retrovirus ◽  
Human Endogenous Retrovirus ◽  
Necrosis Virus ◽  
Cellular Resistance ◽  
Spleen Necrosis Virus ◽  
Spleen Necrosis

scholarly journals Envelope Gene of the Human Endogenous Retrovirus HERV-W Encodes a Functional Retrovirus Envelope

2001 ◽  
Vol 75 (7) ◽  
pp. 3488-3489 ◽  
Author(s):  
Dong Sung An ◽  
Yi-ming Xie ◽  
Irvin S. Y. Chen
Keyword(s):  
Human Immunodeficiency Virus ◽  
Functional Properties ◽  
Envelope Glycoprotein ◽  
Endogenous Retrovirus ◽  
Human Endogenous Retrovirus ◽  
Envelope Gene ◽  
Membrane Glycoprotein ◽  
Herv Family ◽  
Immunodeficiency Virus

ABSTRACT A member of the human endogenous retrovirus (HERV) family termed HERV-W encodes a highly fusogenic membrane glycoprotein that appears to be expressed specifically in the placenta. It is unclear whether the glycoproteins of the HERVs can serve as functional retrovirus envelope proteins to confer infectivity on retrovirus particles. We found that the HERV-W envelope glycoprotein can form pseudotypes with human immunodeficiency virus type 1 virions and confers tropism for CD4-negative cells. Thus, the HERV-W env gene represents the first HERV env gene demonstrated to encode the functional properties of a retrovirus envelope glycoprotein.

scholarly journals Spliced Spleen Necrosis Virus Vector RNA Is Not Encapsidated: Implications for Retroviral Replication and Vector Design

2004 ◽  
Vol 9 (4) ◽  
pp. 557-565 ◽  
Author(s):  
Adrienne Goodrich ◽  
Zahida Parveen ◽  
Ralph Dornburg ◽  
Matthias J Schnell ◽  
Roger J Pomerantz
Keyword(s):  
Virus Vector ◽  
Necrosis Virus ◽  
Spleen Necrosis Virus ◽  
Retroviral Replication ◽  
Spleen Necrosis

scholarly journals An Envelope Glycoprotein of the Human Endogenous Retrovirus HERV-W Is Expressed in the Human Placenta and Fuses Cells Expressing the Type D Mammalian Retrovirus Receptor

2000 ◽  
Vol 74 (7) ◽  
pp. 3321-3329 ◽  
Author(s):  
Jean-Luc Blond ◽  
Dimitri Lavillette ◽  
Valérie Cheynet ◽  
Olivier Bouton ◽  
Guy Oriol ◽  
...  
Keyword(s):  
Envelope Glycoprotein ◽  
Expression Vector ◽  
Physiological Role ◽  
Endogenous Retrovirus ◽  
Open Reading Frame ◽  
Human Endogenous Retrovirus ◽  
Membrane Glycoprotein ◽  
Reading Frame ◽  
Herv Family ◽  
Type D

ABSTRACT A new human endogenous retrovirus (HERV) family, termed HERV-W, was recently described (J.-L. Blond, F. Besème, L. Duret, O. Bouton, F. Bedin, H. Perron, B. Mandrand, and F. Mallet, J. Virol. 73:1175–1185, 1999). HERV-W mRNAs were found to be specifically expressed in placenta cells, and an env cDNA containing a complete open reading frame was recovered. In cell-cell fusion assays, we demonstrate here that the product of the HERV-W env gene is a highly fusogenic membrane glycoprotein. Transfection of an HERV-W Env expression vector in a panel of cell lines derived from different species resulted in formation of syncytia in primate and pig cells upon interaction with the type D mammalian retrovirus receptor. Moreover, envelope glycoproteins encoded by HERV-W were specifically detected in placenta cells, suggesting that they may play a physiological role during pregnancy and placenta formation.

scholarly journals The Nucleocapsid Domain Is Responsible for the Ability of Spleen Necrosis Virus (SNV) Gag Polyprotein To Package both SNV and Murine Leukemia Virus RNA

1999 ◽  
Vol 73 (11) ◽  
pp. 9170-9177 ◽  
Author(s):  
Jeanine L. Certo ◽  
Timur O. Kabdulov ◽  
Michelle L. Paulson ◽  
Jeffrey A. Anderson ◽  
Wei-Shau Hu
Keyword(s):  
Murine Leukemia Virus ◽  
Viral Vector ◽  
Leukemia Virus ◽  
Gene Products ◽  
Rna Packaging ◽  
Packaging Signal ◽  
Necrosis Virus ◽  
Spleen Necrosis Virus ◽  
Spleen Necrosis ◽  
Murine Leukemia

ABSTRACT Murine leukemia virus (MLV)-based vector RNA can be packaged and propagated by the proteins of spleen necrosis virus (SNV). We recently demonstrated that MLV proteins cannot support the replication of an SNV-based vector; RNA analysis revealed that MLV proteins cannot efficiently package SNV-based vector RNA. The domain in Gag responsible for the specificity of RNA packaging was identified using chimericgag-pol expression constructs. A competitive packaging system was established by generating a cell line that expresses one viral vector RNA containing the MLV packaging signal (Ψ) and another viral vector RNA containing the SNV packaging signal (E). The chimericgag-pol expression constructs were introduced into the cells, and vector titers as well as the efficiency of RNA packaging were examined. Our data confirm that Gag is solely responsible for the selection of viral RNAs. Furthermore, the nucleocapsid (NC) domain in the SNV Gag is responsible for its ability to interact with both SNV E and MLV Ψ. Replacement of the SNV NC with the MLV NC generated a chimeric Gag that could not package SNV RNA but retained its ability to package MLV RNA. A construct expressing SNV gag-MLVpol supported the replication of both MLV and SNV vectors, indicating that the gag and pol gene products from two different viruses can functionally cooperate to perform one cycle of retroviral replication. Viral titer data indicated that SNVcis-acting elements are not ideal substrates for MLVpol gene products since infectious viruses were generated at a lower efficiency. These results indicate that the nonreciprocal recognition between SNV and MLV extends beyond the Gag-RNA interaction and also includes interactions between Pol and othercis-acting elements.

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