scholarly journals Studies on the mechanism of 1,3-butadiene-induced leukemogenesis: the potential role of endogenous murine leukemia virus.

1990 ◽  
Vol 86 ◽  
pp. 49-55 ◽  
Author(s):  
R D Irons
Keyword(s):  
Murine Leukemia Virus ◽  
Potential Role ◽  
Leukemia Virus ◽  
Murine Leukemia

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.

Role of carbohydrate in biological functions of Friend murine leukemia virus gp71.

1977 ◽  
Vol 21 (1) ◽  
pp. 35-40 ◽  
Author(s):  
W Schäfer ◽  
P J Fischinger ◽  
J J Collins ◽  
D P Bolognesi
Keyword(s):  
Murine Leukemia Virus ◽  
Leukemia Virus ◽  
Biological Functions ◽  
Murine Leukemia

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.

Role of the 207–218 peptide region of Moloney murine leukemia virus integrase in enzyme catalysis

2010 ◽  
Vol 495 (1) ◽  
pp. 28-34 ◽  
Author(s):  
Mónica L. Acevedo ◽  
José Jaime Arbildúa ◽  
Octavio Monasterio ◽  
Héctor Toledo ◽  
Oscar León
Keyword(s):  
Murine Leukemia Virus ◽  
Enzyme Catalysis ◽  
Leukemia Virus ◽  
Moloney Murine Leukemia Virus ◽  
Peptide Region ◽  
Murine Leukemia

scholarly journals Role of Chimeric Murine Leukemia Virusenv β-Turn Polyproline Spacers in Receptor Cooperation

2001 ◽  
Vol 75 (18) ◽  
pp. 8478-8486 ◽  
Author(s):  
Sandrine Valsesia-Wittmann
Keyword(s):  
Murine Leukemia Virus ◽  
Leukemia Virus ◽  
Cooperative Effect ◽  
Cell Surface Receptor ◽  
Moloney Murine Leukemia Virus ◽  
Binding Domains ◽  
N Terminus ◽  
Surface Receptor ◽  
Murine Leukemia

ABSTRACT We have previously reported a set of Moloney murine leukemia virus derived envelopes retargeted to the Pit-2 phosphate transporter molecule, by insertion of the Pit-2 binding domain (BD) at the N terminus of the ecotropic retroviral envelope glycoproteins (S. Valsesia-Wittmann et al., J. Virol. 70:2059-2064, 1996). The resulting chimeric envelopes share two BDs: an additional N-terminal BD (Pit-2 BD) and the BD of the ecotropic envelope (mCAT-1 BD). By inserting a variety of different amino acid spacers between the two binding domains, we showed that retroviruses can potentially use the targeted cell surface receptor Pit-2, the ecotropic retroviral receptor mCAT-1, or both receptors cooperatively for entry into target cell (S. Valsesia-Wittmann et al., EMBO J 6:1214–1223, 1997). An extreme example of receptor cooperativity was encountered when envelopes with specific proline-rich interdomain spacers (PRO spacers) were tested: both receptors had to be coexpressed at the surface of the targeted cells to cooperatively allow infection. Here, we characterized the role of PRO spacer in the cooperation of receptors. We have shown that the particular organization of the PRO spacer—a β-turn polyproline—was responsible for the cooperative effect. In the native configuration of the viruses, the structure masked the regions located downstream of the PRO spacer, thus the mCAT-1 BD. After interaction with the targeted Pit-2 receptor, the BD of the backbone envelope became accessible, and we demonstrated that interaction between the mCAT-1 BD and the mCAT-1 receptor is absolutely necessary. This interaction leads to natural fusion triggering and entry of viruses into targeted cells.

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