scholarly journals Definition of VPU sensitivity using a model VPU target and role of hydrophobicity of the membrane spanning domain in the viral envelope glycoprotein fusogenicity

2013 ◽  
Author(s):  
Sanath Kumar Janaka
Keyword(s):  
Envelope Glycoprotein ◽  
Viral Envelope ◽  
Viral Envelope Glycoprotein ◽  
Membrane Spanning ◽  
Definition Of

scholarly journals Role of Envelope Glycoprotein Complexes in Cell-Associated Spread of Human Cytomegalovirus

Viruses ◽  
2021 ◽  
Vol 13 (4) ◽  
pp. 614
Author(s):  
Nina Weiler ◽  
Caroline Paal ◽  
Kerstin Adams ◽  
Christopher Calcaterra ◽  
Dina Fischer ◽  
...  
Keyword(s):  
Human Cytomegalovirus ◽  
Envelope Glycoprotein ◽  
Infectious Virus ◽  
Viral Envelope ◽  
Accessory Proteins ◽  
Viral Growth ◽  
Cell Association ◽  
Quantitative Immunoblotting ◽  
Model Virus

The role of viral envelope glycoproteins, particularly the accessory proteins of trimeric and pentameric gH/gL-complexes, in cell-associated spread of human cytomegalovirus (HCMV) is unclear. We aimed to investigate their contribution in the context of HCMV variants that grow in a strictly cell-associated manner. In the genome of Merlin pAL1502, the glycoproteins gB, gH, gL, gM, and gN were deleted by introducing stop codons, and the mutants were analyzed for viral growth. Merlin and recent HCMV isolates were compared by quantitative immunoblotting for expression of accessory proteins of the trimeric and pentameric gH/gL-complexes, gO and pUL128. Isolates were treated with siRNAs against gO and pUL128 and analyzed regarding focal growth and release of infectious virus. All five tested glycoproteins were essential for growth of Merlin pAL1502. Compared with this model virus, higher gO levels were measured in recent isolates of HCMV, and its knockdown decreased viral growth. Knockdown of pUL128 abrogated the strict cell-association and led to release of infectivity, which allowed cell-free transfer to epithelial cells where the virus grew again strictly cell-associated. We conclude that both trimer and pentamer contribute to cell-associated spread of recent clinical HCMV isolates and downregulation of pentamer can release infectious virus into the supernatant.

What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion (Review)

1997 ◽  
Vol 14 (3) ◽  
pp. 97-112 ◽  
Author(s):  
Stewart R. Durell ◽  
Isabelle Martin ◽  
Jean-Marie Ruysschaert ◽  
Yechiel Shai ◽  
Robert Blumenthal
Keyword(s):  
Membrane Fusion ◽  
Envelope Glycoprotein ◽  
Viral Envelope ◽  
Fusion Peptides ◽  
Viral Envelope Glycoprotein

Cloning and epitope mapping of a functional partial fusion receptor for human cytomegalovirus gH

Microbiology ◽  
2000 ◽  
Vol 81 (1) ◽  
pp. 27-35 ◽  
Author(s):  
Brenda R. Baldwin ◽  
Chen-Ou Zhang ◽  
Susan Keay
Keyword(s):  
Human Cytomegalovirus ◽  
Viral Envelope ◽  
Nuclear Localization Signals ◽  
Synthetic Receptor ◽  
Hydrophilic Region ◽  
Receptor Cdna ◽  
Cell Membrane Protein ◽  
Membrane Spanning ◽  
Fusion Receptor

A cDNA clone encoding a partial putative human cytomegalovirus (HCMV) gH fusion receptor (CMVFR) was previously identified. In this report, the cDNA sequence of CMVFR was determined and the role of this CMVFR in HCMV/cell fusion was confirmed by rendering fusion-incompetent MOLT-4 cells susceptible to fusion following transfection with receptor cDNA. Blocking experiments using recombinant gH or either of two MAbs (against recombinant gH or purified viral gH:gL) provided additional evidence for the role of gH binding to this protein in virus fusion. An HCMV-binding domain of 12 aa in the middle hydrophilic region of CMVFR was identified by fusion blocking studies using synthetic receptor peptides. The 1368 bp cDNA of CMVFR contained a predicted ORF of 345 aa with two potential membrane-spanning domains and several possible nuclear localization signals. A search of sequence databases indicated that CMVFR is a novel protein. Further characterization of this cell membrane protein that confers susceptibility to fusion with the viral envelope should provide important information about the mechanism by which HCMV infects cells.

Human CD38 interferes with HIV‐1 fusion through a sequence homologous to the V3 loop of the viral envelope glycoprotein gp120.

2003 ◽  
Vol 17 (3) ◽  
pp. 1-20 ◽  
Author(s):  
Andrea Savarino ◽  
Thea Bensi ◽  
Annalisa Chiocchetti ◽  
Flavia Bottarel ◽  
Riccardo Mesturini ◽  
...  
Keyword(s):  
Envelope Glycoprotein ◽  
Viral Envelope ◽  
V3 Loop ◽  
Viral Envelope Glycoprotein ◽  
Envelope Glycoprotein Gp120 ◽  
Glycoprotein Gp120 ◽  
Hiv 1

scholarly journals THE VIRAL ENVELOPE GLYCOPROTEIN OF MURINE LEUKEMIA VIRUS AND THE PATHOGENESIS OF IMMUNE COMPLEX GLOMERULONEPHRITIS OF NEW ZEALAND MICE

1974 ◽  
Vol 140 (4) ◽  
pp. 1011-1027 ◽  
Author(s):  
Takashi Yoshiki ◽  
Robert C. Mellors ◽  
Mette Strand ◽  
J. T. August
Keyword(s):  
New Zealand ◽  
Immune Complex ◽  
Envelope Glycoprotein ◽  
Murine Leukemia Virus ◽  
Leukemia Virus ◽  
Viral Envelope ◽  
High Concentration ◽  
Immune Complex Glomerulonephritis ◽  
Viral Envelope Glycoprotein ◽  
Murine Leukemia

The use of monospecific antisera for the analysis by radioimmunoassay and immunofluorescence study of two major viral proteins, gp69/71 and p30 of murine leukemia virus, that could be of significance in the pathogenesis of immune complex glomerulonephritis of mice, particularly NZB and B/WF1 hybrid mice, yielded the following conclusions. A remarkably high concentration of viral envelope glycoprotein, gp69/71, was detected in the spleen and serum of New Zealand mice (NZB, NZW, B/WF1, and W/BF1); the concentration in the spleen was 10-fold greater than that found in AKR mice and 30-fold greater than that present in C57BL/6 mice. The gp69/71 was deposited along with bound immunoglobulins, apparently as an immune complex, in the diseased kidneys of mice, and the glomerular site and extent of deposition of gp69/71 was related to the severity of the glomerulonephritis. This study suggests that the pathogenesis of immune complex glomerulonephritis (and vasculitis) in mice is related to the expression of this specific viral envelope glycoprotein and to the host immune response to this protein.

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