scholarly journals The Role of the Membrane-spanning Domain Sequence in Glycoprotein-mediated Membrane Fusion

1999 ◽  
Vol 10 (9) ◽  
pp. 2803-2815 ◽  
Author(s):  
Gwen M. Taylor ◽  
David Avram Sanders
Keyword(s):  
Membrane Fusion ◽  
Murine Leukemia Virus ◽  
Leukemia Virus ◽  
Envelope Proteins ◽  
Viral Fusion ◽  
Virus Envelope ◽  
Membrane Spanning ◽  
Membrane Spanning Domains ◽  
Murine Leukemia

The role of glycoprotein membrane-spanning domains in the process of membrane fusion is poorly understood. It has been demonstrated that replacing all or part of the membrane-spanning domain of a viral fusion protein with sequences that encode signals for glycosylphosphatidylinositol linkage attachment abrogates membrane fusion activity. It has been suggested, however, that the actual amino acid sequence of the membrane-spanning domain is not critical for the activity of viral fusion proteins. We have examined the function of Moloney murine leukemia virus envelope proteins with substitutions in the membrane-spanning domain. Envelope proteins bearing substitutions for proline 617 are processed and incorporated into virus particles normally and bind to the viral receptor. However, they possess greatly reduced or undetectable capacities for the promotion of membrane fusion and infectious virus particle formation. Our results imply a direct role for the residues in the membrane-spanning domain of the murine leukemia virus envelope protein in membrane fusion and its regulation. They also support the thesis that membrane-spanning domains possess a sequence-dependent function in other protein-mediated membrane fusion events.

scholarly journals Role of intron-contained sequences in formation of moloney murine leukemia virus env mRNA.

1984 ◽  
Vol 4 (11) ◽  
pp. 2289-2297 ◽  
Author(s):  
L S Hwang ◽  
J Park ◽  
E Gilboa
Keyword(s):  
Splice Site ◽  
Murine Leukemia Virus ◽  
Leukemia Virus ◽  
Splice Junction ◽  
Moloney Murine Leukemia Virus ◽  
Expression Vectors ◽  
Virus Envelope ◽  
Cellular Genes ◽  
Murine Leukemia

Formation of the Moloney murine leukemia virus envelope mRNA involves the removal of a 5,185-base pair-long intron. Deletion analysis of two Moloney murine leukemia virus-derived expression vectors revealed the existence of two short regions within the viral intron which are required for the efficient formation of the spliced RNA species. One region was present upstream from the 3' splice junction, extended at least 85 nucleotides beyond the splice site, and was not more than 165 nucleotides long. As yeast polymerase II introns, the Moloney murine leukemia virus intron contains the sequence 5'-TACTAAC-3' 15 nucleotides upstream from the 3' splice site. A second region located in the middle of the intron, within a 560-nucleotide-long sequence, was also essential for formation of the spliced RNA species. The efficient splicing of the env mRNA in the absence of expression of viral genes raises the possibility that similar mechanisms are used to remove introns of (some) cellular genes.

scholarly journals Asymmetric Requirement for Cholesterol in Receptor-Bearing but Not Envelope-Bearing Membranes for Fusion Mediated by Ecotropic Murine Leukemia Virus

2002 ◽  
Vol 76 (13) ◽  
pp. 6701-6709 ◽  
Author(s):  
Xiongbin Lu ◽  
Ying Xiong ◽  
Jonathan Silver
Keyword(s):  
Murine Leukemia Virus ◽  
Mammalian Cells ◽  
Insect Cells ◽  
Leukemia Virus ◽  
Cell System ◽  
Membrane Rafts ◽  
Cell Physiology ◽  
Virus Envelope ◽  
Murine Leukemia

ABSTRACT We show that fusion mediated by ecotropic murine leukemia virus envelope is dependent on cholesterol in receptor-bearing membranes. The effect is >10 times larger in insect cells than mammalian cells, probably because the former can be more extensively depleted of cholesterol. The fact that cholesterol is apparently not needed in envelope-bearing membranes suggests that it plays a role in an asymmetric step in membrane fusion and argues against a class of models in which cholesterol is important in symmetric fusion intermediates. The insect cell system has promise for clarifying the role of membrane rafts in other aspects of cell physiology.

scholarly journals Suppression of Rat Bone Marrow Cells by Friend Murine Leukemia Virus Envelope Proteins

Virology ◽  
1998 ◽  
Vol 242 (2) ◽  
pp. 357-365 ◽  
Author(s):  
Stefan Mazgareanu ◽  
Justus G. Müller ◽  
Stefanie Czub ◽  
Simone Schimmer ◽  
Martin Bredt ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Murine Leukemia Virus ◽  
Bone Marrow Cells ◽  
Leukemia Virus ◽  
Envelope Proteins ◽  
Virus Envelope ◽  
Murine Leukemia ◽  
Rat Bone ◽  
Marrow Cells

Role of intron-contained sequences in formation of moloney murine leukemia virus env mRNA

1984 ◽  
Vol 4 (11) ◽  
pp. 2289-2297
Author(s):  
L S Hwang ◽  
J Park ◽  
E Gilboa
Keyword(s):  
Splice Site ◽  
Murine Leukemia Virus ◽  
Leukemia Virus ◽  
Splice Junction ◽  
Moloney Murine Leukemia Virus ◽  
Expression Vectors ◽  
Virus Envelope ◽  
Cellular Genes ◽  
Murine Leukemia

Formation of the Moloney murine leukemia virus envelope mRNA involves the removal of a 5,185-base pair-long intron. Deletion analysis of two Moloney murine leukemia virus-derived expression vectors revealed the existence of two short regions within the viral intron which are required for the efficient formation of the spliced RNA species. One region was present upstream from the 3' splice junction, extended at least 85 nucleotides beyond the splice site, and was not more than 165 nucleotides long. As yeast polymerase II introns, the Moloney murine leukemia virus intron contains the sequence 5'-TACTAAC-3' 15 nucleotides upstream from the 3' splice site. A second region located in the middle of the intron, within a 560-nucleotide-long sequence, was also essential for formation of the spliced RNA species. The efficient splicing of the env mRNA in the absence of expression of viral genes raises the possibility that similar mechanisms are used to remove introns of (some) cellular genes.

scholarly journals Palmitoylation of the Murine Leukemia Virus Envelope Protein Is Critical for Lipid Raft Association and Surface Expression

2002 ◽  
Vol 76 (23) ◽  
pp. 11845-11852 ◽  
Author(s):  
Min Li ◽  
Chinglai Yang ◽  
Suxiang Tong ◽  
Armin Weidmann ◽  
Richard W. Compans
Keyword(s):  
Lipid Rafts ◽  
Lipid Raft ◽  
Murine Leukemia Virus ◽  
Leukemia Virus ◽  
Viral Fusion ◽  
Deficient Mutant ◽  
Wild Type ◽  
Virus Envelope ◽  
Env Protein ◽  
Murine Leukemia

ABSTRACT To investigate the association of the murine leukemia virus (MuLV) Env protein with lipid rafts, we compared wild-type and palmitoylation-deficient mutant Env proteins by using extraction with the mild detergent Triton X-100 (TX-100) followed by a sucrose gradient flotation assay. We found that the wild-type MuLV Env protein was resistant to ice-cold TX-100 treatment and floated to the top of the gradients. In contrast, we observed that the palmitoylation-deficient mutant Env protein was mostly soluble when extracted by ice-cold TX-100 and stayed at the bottom of the gradients. Both the wild-type and mutant Env proteins were found to be soluble when treated with methyl-β-cyclodextrin before extraction with ice-cold TX-100 or when treated with ice-cold octyl-β-glucoside instead of TX-100. These results indicate that the MuLV Env protein is associated with lipid rafts and that palmitoylation of the Env protein is critical for lipid raft association. Although the palmitoylation-deficient Env mutant was synthesized at a level similar to that of the wild-type Env, it was found to be expressed at reduced levels on the cell surface. We observed syncytium formation activity with both the wild-type and mutant Env proteins, indicating that palmitoylation or raft association is not required for MuLV viral fusion activity.

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