scholarly journals Dysfunction of Bovine Endogenous Retrovirus K2 Envelope Glycoprotein Is Related to Unsuccessful Intracellular Trafficking

2014 ◽  
Vol 88 (12) ◽  
pp. 6896-6905 ◽  
Author(s):  
Y. Nakaya ◽  
T. Miyazawa
Keyword(s):  
Envelope Glycoprotein ◽  
Intracellular Trafficking ◽  
Endogenous Retrovirus

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 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 Mason-Pfizer Monkey Virus Envelope Glycoprotein Cycling and Its Vesicular Co-Transport with Immature Particles

Viruses ◽  
2018 ◽  
Vol 10 (10) ◽  
pp. 575 ◽  
Author(s):  
Petra Prokšová ◽  
Jan Lipov ◽  
Jaroslav Zelenka ◽  
Eric Hunter ◽  
Hana Langerová ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Life Cycle ◽  
Host Cell ◽  
Envelope Glycoprotein ◽  
Crucial Role ◽  
Intracellular Trafficking ◽  
Virus Envelope ◽  
Trans Golgi Network ◽  
Golgi Network ◽  
Putative Mechanism

The envelope glycoprotein (Env) plays a crucial role in the retroviral life cycle by mediating primary interactions with the host cell. As described previously and expanded on in this paper, Env mediates the trafficking of immature Mason-Pfizer monkey virus (M-PMV) particles to the plasma membrane (PM). Using a panel of labeled RabGTPases as endosomal markers, we identified Env mostly in Rab7a- and Rab9a-positive endosomes. Based on an analysis of the transport of recombinant fluorescently labeled M-PMV Gag and Env proteins, we propose a putative mechanism of the intracellular trafficking of M-PMV Env and immature particles. According to this model, a portion of Env is targeted from the trans-Golgi network (TGN) to Rab7a-positive endosomes. It is then transported to Rab9a-positive endosomes and back to the TGN. It is at the Rab9a vesicles where the immature particles may anchor to the membranes of the Env-containing vesicles, preventing Env recycling to the TGN. These Gag-associated vesicles are then transported to the plasma membrane.

scholarly journals Reconstitution of the Ancestral Glycoprotein of Human Endogenous Retrovirus K and Modulation of Its Functional Activity by Truncation of the Cytoplasmic Domain

2009 ◽  
Vol 83 (24) ◽  
pp. 12790-12800 ◽  
Author(s):  
Kirsten Hanke ◽  
Philipp Kramer ◽  
Sandra Seeher ◽  
Nadine Beimforde ◽  
Reinhard Kurth ◽  
...  
Keyword(s):  
Intracellular Trafficking ◽  
Mammalian Cells ◽  
Endogenous Retrovirus ◽  
Endogenous Retroviruses ◽  
Human Endogenous Retrovirus ◽  
Back Mutation ◽  
Genes Encoding ◽  
Carboxy Terminal ◽  
Processing Stability ◽  
First Time

ABSTRACT Endogenous retroviruses present in the human genome provide a rich record of ancient infections. All presently recognized elements, including the youngest and most intact proviruses of the human endogenous retrovirus K(HML-2) [HERV-K(HML-2)] family, have suffered postinsertional mutations during their time of chromosomal residence, and genes encoding the envelope glycoprotein (Env) have not been spared these mutations. In this study, we have, for the first time, reconstituted an authentic Env of a HERV-K(HML-2) provirus by back mutation of putative postinsertional amino acid changes of the protein encoded by HERV-K113. Aided by codon-optimized expression, we demonstrate that the reconstituted Env regained its ability to be incorporated into retroviral particles and to mediate entry. The original ancient HERV-K113 Env was synthesized as a moderately glycosylated gp95 precursor protein cleaved into surface and transmembrane (TM) subunits. Of the nine N-linked oligosaccharides, four are part of the TM subunit, contributing 15 kDa to its apparent molecular mass of 41 kDa. The carbohydrates, as well as the cytoplasmic tail, are critical for efficient intracellular trafficking, processing, stability, and particle incorporation. Whereas deletions of the carboxy-terminal 6 residues completely abrogated cleavage and virion association, more extensive truncations slightly enhanced incorporation but dramatically increased the ability to mediate entry of pseudotyped lentiviruses. Although the first HERV-K(HML-2) elements infected human ancestors about 30 million years ago, our findings indicate that their glycoproteins are in most respects remarkably similar to those of classical contemporary retroviruses and can still mediate efficient entry into mammalian cells.

scholarly journals Immunotherapy-induced antibodies to endogenous retroviral envelope glycoprotein confer tumor protection in mice

PLoS ONE ◽  
2021 ◽  
Vol 16 (4) ◽  
pp. e0248903
Author(s):  
Byong H. Kang ◽  
Noor Momin ◽  
Kelly D. Moynihan ◽  
Murillo Silva ◽  
Yingzhong Li ◽  
...  
Keyword(s):  
Envelope Glycoprotein ◽  
Tumor Antigens ◽  
Humoral Response ◽  
Endogenous Retrovirus ◽  
B16f10 Cells ◽  
Tumor Protection ◽  
Prophylactic Vaccination ◽  
Allogeneic Tumor Cell ◽  
Env Protein ◽  
Subcutaneous Inoculation

Following curative immunotherapy of B16F10 tumors, ~60% of mice develop a strong antibody response against cell-surface tumor antigens. Their antisera confer prophylactic protection against intravenous challenge with B16F10 cells, and also cross-react with syngeneic and allogeneic tumor cell lines MC38, EL.4, 4T1, and CT26. We identified the envelope glycoprotein (env) of a murine endogenous retrovirus (ERV) as the antigen accounting for the majority of this humoral response. A systemically administered anti-env monoclonal antibody cloned from such a response protects against tumor challenge, and prophylactic vaccination against the env protein protects a majority of naive mice from tumor establishment following subcutaneous inoculation with B16F10 cells. These results suggest the potential for effective prophylactic vaccination against analogous HERV-K env expressed in numerous human cancers.

scholarly journals The lupus susceptibility locus Sgp3 encodes the suppressor of endogenous retrovirus expression SNERV

2018 ◽  
Author(s):  
Rebecca S Treger ◽  
Scott D Pope ◽  
Yong Kong ◽  
Maria Tokuyama ◽  
Manabu Taura ◽  
...  
Keyword(s):  
Long Terminal Repeat ◽  
Zinc Finger ◽  
Envelope Glycoprotein ◽  
Transcriptional Regulator ◽  
Zinc Finger Proteins ◽  
Endogenous Retrovirus ◽  
Terminal Repeat ◽  
Susceptibility Locus ◽  
Chromatin Modifications ◽  
Lupus Pathogenesis

Elevated endogenous retrovirus (ERV) transcription and anti-ERV antibody reactivity are implicated in lupus pathogenesis. Overproduction of non-ecotropic ERV (NEERV) envelope glycoprotein, gp70, and resultant nephritis occur in lupus-prone mice. However, a NEERV repressor has not been identified to test if this association is causal. Here we identified suppressor of NEERV (Snerv) 1 & 2, Kruppel-associated box zinc finger proteins (KRAB-ZFP) that repressed NEERV by binding the NEERV long terminal repeat to recruit the transcriptional regulator KAP1. Germline Snerv1/2 deletion increased activating chromatin modifications, transcription, and gp70 expression from NEERV loci. F1 crosses of lupus-prone NZB and 129 mice to Snerv1/2-/- mice failed to restore NEERV repression, demonstrating that loss of SNERV underlies the lupus autoantigen gp70 overproduction that promotes nephritis in susceptible mice. Increased ERV expression in lupus patients was inversely correlated with expression of three putative ERV-suppressing KRAB-ZFP, suggesting that KRAB-ZFP-mediated ERV misexpression may contribute to human lupus pathogenesis.

scholarly journals The Envelope Glycoprotein of Human Endogenous Retrovirus Type W Uses a Divergent Family of Amino Acid Transporters/Cell Surface Receptors

2002 ◽  
Vol 76 (13) ◽  
pp. 6442-6452 ◽  
Author(s):  
Dimitri Lavillette ◽  
Mariana Marin ◽  
Alessia Ruggieri ◽  
François Mallet ◽  
François-Loïc Cosset ◽  
...  
Keyword(s):  
Amino Acid ◽  
Envelope Glycoprotein ◽  
Syncytium Formation ◽  
Endogenous Retrovirus ◽  
Intact Protein ◽  
Human Endogenous Retrovirus ◽  
Amino Acid Transporters ◽  
Protein Coding ◽  
Surface Receptors ◽  
Coding Regions

ABSTRACT The human endogenous retrovirus type W (HERV-W) family includes proviruses with intact protein-coding regions that appear to be under selection pressure, suggesting that some HERV-W proviruses may remain active in higher primates. The envelope glycoprotein (Env) encoded by HERV-W is highly fusogenic, is naturally expressed in human placental syncytiatrophoblasts, and has been reported to function as a superantigen in lymphocyte cultures. Recent evidence suggested that HERV-W Env can mediate syncytium formation by interacting with the human sodium-dependent neutral amino acid transporter type 2 (hASCT2; gene name, SLC1A5) (J.-L. Blond, D. Lavillette, V. Cheynet, O. Bouton, G. Oriol, S. Chapel-Fernandez, B. Mandrand, F. Mallet, and F.-L. Cosset, J. Virol. 74:3321-3329, 2000) and that it can pseudotype human immunodeficiency virus cores (D. S. An, Y. Xie, and I. S. Y. Chen, J. Virol. 75:3488-3489, 2001). By using cell-cell fusion and pseudotype virion infection assays, we found that HERV-W Env efficiently uses both hASCT2 and the related transporter hASCT1 (gene name, SLC1A4) as receptors. In addition, although HERV-W Env mediates only slight syncytium formation or infection of mouse cells, it utilizes the mouse transporters mASCT1 and mASCT2 when their sites for N-linked glycosylation are eliminated by mutagenesis. Consistent with their role as a battlefield in host-virus coevolution, the viral recognition regions in ASCT1 and ASCT2 of humans and mice are highly divergent compared with other regions of these proteins, and their ratios of nonsynonymous to synonymous nucleotide sequence changes are extremely large. The recognition of ASCT1 and ASCT2 despite this divergence of their sequences strongly suggests that the use of both receptors has been highly advantageous for survival and evolution of the HERV-W family of retroviruses.

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