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.

scholarly journals Localization of the intrachain disulfide bonds of the envelope glycoprotein 71 from Friend murine leukemia virus

1992 ◽  
Vol 203 (1-2) ◽  
pp. 71-73
Author(s):  
Monica LINDER ◽  
Dietmar LINDER ◽  
Josef HAHNEN ◽  
Hans-Henning SCHOTT ◽  
Stephan STIRM
Keyword(s):  
Envelope Glycoprotein ◽  
Murine Leukemia Virus ◽  
Disulfide Bonds ◽  
Leukemia Virus ◽  
Murine Leukemia

Cell Surface Binding Proteins for the Major Envelope Glycoprotein of Murine Leukemia Virus

1979 ◽  
Vol 162 (2) ◽  
pp. 304-309 ◽  
Author(s):  
D. R. Twardzik ◽  
A. K. Fowler ◽  
O. S. Weislow ◽  
G. A. Hegamyer ◽  
A. Hellman
Keyword(s):  
Cell Surface ◽  
Envelope Glycoprotein ◽  
Murine Leukemia Virus ◽  
Binding Proteins ◽  
Leukemia Virus ◽  
Surface Binding ◽  
Cell Surface Binding ◽  
Murine Leukemia

scholarly journals Susceptibility of BALB/c mice carrying various DBA/2 genes to development of Friend murine leukemia virus-induced erythroleukemia.

1985 ◽  
Vol 162 (5) ◽  
pp. 1579-1587 ◽  
Author(s):  
S Ruscetti ◽  
R Matthai ◽  
M Potter
Keyword(s):  
Structural Gene ◽  
Envelope Glycoprotein ◽  
Murine Leukemia Virus ◽  
Leukemia Virus ◽  
Regulatory Gene ◽  
Constitutive Expression ◽  
Newborn Mice ◽  
Unique Protein ◽  
Mink Cell ◽  
Murine Leukemia

Using a series of BALB/c mice congenic for various DBA/2 genes, we were able to establish that DBA/2 mice carry a gene on chromosome 5, at or near the Rmcfr locus, that plays a major role in resistance to early erythroleukemia induced by injection of Friend murine leukemia virus (F-MuLV) into newborn mice. The fact that this gene controls the replication of mink cell focus-inducing (MCF) viruses strengthens the case for these viruses playing a crucial role in the development of erythroleukemia, since failure to replicate MCF viruses results in resistance to early erythroleukemia. The expression of the Rmcfr gene is correlated with the constitutive expression of an MCF virus-related envelope glycoprotein that apparently blocks the receptor for MCF viruses, preventing their spread. Thus, the Rmcfr gene is either a structural gene for this unique protein, which can block the receptor for MCF viruses, or is a regulatory gene that controls expression of such a structural gene. Although the Rmcfr gene is clearly involved in resistance to the early erythroleukemia induced by F-MuLV, it appears to have no effect on the late myeloid, lymphoid or erythroid diseases that appear in DBA/2 and other strains of mice after injection of F-MuLV, consistent with data indicating that replication of MCF viruses is not required for the development of these late diseases. Our studies with congenic and backcross mice also indicate that, in addition to the Rmcfr gene, other genes of DBA/2 origin may contribute to resistance to F-MuLV-induced early erythroleukemia by mechanisms other than blocking the replication of MCF viruses.

scholarly journals Influence of GlycoGag on the Incorporation of Host Membrane Proteins Into the Envelope of the Moloney Murine Leukemia Virus

2021 ◽  
Vol 1 ◽  
Author(s):  
Mariam Maltseva ◽  
Marc-André Langlois
Keyword(s):  
Murine Leukemia Virus ◽  
Viral Particle ◽  
Leukemia Virus ◽  
Viral Envelope ◽  
Host Protein ◽  
Viral Population ◽  
Phenotypic Characterization ◽  
Particle Level ◽  
Protein Incorporation ◽  
Murine Leukemia

Analysis of viral particle heterogeneity produced from infected cells has been limited by the inefficiency of traditional analytical methods to characterize large populations of viruses at an individual particle level. Flow virometry (FVM) is an emerging technique based on flow cytometry principles that enables a high throughput, multiparametric, and phenotypic characterization of viruses at a single particle resolution. Here, we performed FVM to analyze surface markers found on Murine Leukemia Virus (MLV) and glycosylated Gag-deficient (glycoGag) MLV. The glycoGag viral accessory protein has several roles in the MLV viral infection cycle including directing retroviral assembly and particle release at lipid rafts. Based on previous studies, we hypothesize that glycoGag modulates host protein incorporation into the viral envelope during viral assembly and budding. Here, by using FVM, we reveal that glycoGag is associated with an increased incorporation of the host-derived tetraspanins CD81 and CD63 along with the lipid raft marker and immune antigen Thy1.2 during the assembly and release of viral particles from infected NIH 3T3, EL4, and primary CD4+ T cells. Moreover, we show differences in the uptake of host proteins by viruses that are released from the two cell lines and primary T lymphocytes. Additionally, at the individual viral particle level, we observed a degree of expression heterogeneity of host-derived antigens within the viral population. Finally, certain cellular antigens can show either enrichment or exclusion from the viral envelope depending on whether glycoGag is expressed by the virus. This suggests that glycoGag is involved in a mechanism of selective host protein incorporation into the viral envelope.

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