scholarly journals The receptors for gibbon ape leukemia virus and amphotropic murine leukemia virus are not downregulated in productively infected cells

Retrovirology ◽  
2011 ◽  
Vol 8 (1) ◽  
Author(s):  
Meihong Liu ◽  
Maribeth V Eiden
Keyword(s):  
Murine Leukemia Virus ◽  
Leukemia Virus ◽  
Amphotropic Murine Leukemia Virus ◽  
Infected Cells ◽  
Gibbon Ape Leukemia Virus ◽  
Murine Leukemia

scholarly journals Entry of Amphotropic Murine Leukemia Virus Is Influenced by Residues in the Putative Second Extracellular Domain of Its Receptor, Pit2

1998 ◽  
Vol 72 (6) ◽  
pp. 4956-4961 ◽  
Author(s):  
Betsy D. Leverett ◽  
Karen B. Farrell ◽  
Maribeth V. Eiden ◽  
Carolyn A. Wilson
Keyword(s):  
Murine Leukemia Virus ◽  
Leukemia Virus ◽  
Critical Role ◽  
Functional Characterization ◽  
Extracellular Domain ◽  
Receptor Function ◽  
Amphotropic Murine Leukemia Virus ◽  
Fold Reduction ◽  
Gibbon Ape Leukemia Virus ◽  
Murine Leukemia

ABSTRACT Human cells express distinct but related receptors for the gibbon ape leukemia virus (GALV) and the amphotropic murine leukemia virus (A-MuLV), termed Pit1 and Pit2, respectively. Pit1 is not able to function as a receptor for A-MuLV infection, while Pit2 does not confer susceptibility to GALV. Previous studies of chimeric receptors constructed by interchanging regions of Pit1 and Pit2 failed to clarify the determinants unique to Pit2 which correlate with A-MuLV receptor function. In order to identify which regions of Pit2 are involved in A-MuLV receptor function, we exchanged the putative second and third extracellular domains of Pit1, either individually or together, with the corresponding regions of Pit2. Our functional characterization of these receptors indicates a role for the putative second extracellular domain (domain II) in A-MuLV infection. We further investigated the influence of domain II with respect to A-MuLV receptor function by performing site-specific mutagenesis within this region of Pit2. Many of the mutations had little or no effect on receptor function. However, the substitution of serine for methionine at position 138 (S138M) in a Pit1 chimera containing domain II of Pit2 resulted in a 1,000-fold reduction in A-MuLV receptor function. Additional mutations made within domain II of the nonfunctional S138M mutant restored receptor function to nearly wild-type efficiency. The high degree of tolerance for mutations as well as the compensatory effect of particular substitutions observed within domain II suggests that an element of secondary structure within this region plays a critical role in the interaction of the receptor with A-MuLV.

scholarly journals 536. Dual-Vector Prodrug Activator Gene Therapy Using Retroviral Replicating Vectors Derived from Amphotropic Murine Leukemia Virus and Gibbon Ape Leukemia Virus

2015 ◽  
Vol 23 ◽  
pp. S215
Author(s):  
Shuji Kubo ◽  
Misato Takagi-Kimura ◽  
Christopher R. Logg ◽  
Kip Hermann ◽  
Noriyuki Kasahara
Keyword(s):  
Gene Therapy ◽  
Murine Leukemia Virus ◽  
Leukemia Virus ◽  
Dual Vector ◽  
Amphotropic Murine Leukemia Virus ◽  
Gibbon Ape Leukemia Virus ◽  
Murine Leukemia

scholarly journals Single Amino Acid Insertion in Loop 4 Confers Amphotropic Murine Leukemia Virus Receptor Function upon Murine Pit1

1998 ◽  
Vol 72 (5) ◽  
pp. 4524-4527 ◽  
Author(s):  
Mikkel D. Lundorf ◽  
Finn S. Pedersen ◽  
Bryan O’Hara ◽  
Lene Pedersen
Keyword(s):  
Amino Acid ◽  
Murine Leukemia Virus ◽  
Leukemia Virus ◽  
Feline Leukemia Virus ◽  
Single Amino Acid ◽  
Receptor Function ◽  
Amphotropic Murine Leukemia Virus ◽  
Gibbon Ape Leukemia Virus ◽  
Murine Leukemia

ABSTRACT Pit1 is the human receptor for gibbon ape leukemia virus (GALV) and feline leukemia virus subgroup B (FeLV-B), while the related human protein Pit2 is a receptor for amphotropic murine leukemia virus (A-MuLV). The A-MuLV-related isolate 10A1 can utilize both Pit1 and Pit2 as receptors. A stretch of amino acids named region A was identified in Pit1 (residues 550 to 558 in loop 4) as critical for GALV and FeLV-B receptor function. We have here investigated the role of region A in A-MuLV and 10A1 entry. Insertion of a single amino acid in region A of mouse Pit1 resulted in a functional A-MuLV receptor, showing that region A plays a role in A-MuLV infection. Moreover, the downregulation of 10A1 receptor function by changes in region A of human Pit1 indicates that this region is also involved in 10A1 entry. Therefore, region A seems to play a role in infection by all viruses utilizing Pit1 and/or Pit2 as receptors.

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