Definition of a domain of GLVR1 which is necessary for infection by gibbon ape leukemia virus and which is highly polymorphic between species

Johann, S V; Zeijl, Marja van; Cekleniak, Julie; O’Hara, Brian J.

doi:10.1128/jvi.67.11.6733-6736.1993

Cited by 71 publications

(56 citation statements)

References 16 publications

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“…Study of AS208 binding will be useful to investigate the expression of amphotropic envelope-binding sites on potential target cells for gene therapy, as, for example, in purified subpopulations of hematopoietic progenitors. As reported for Glvr-1 (19), Ram-1 appeared to be polymorphic between mammalian species, with only certain alleles coding for functional virus receptors. The molecular basis of receptor function could be conveniently studied by using AS208 binding for a rapid screening of functional and nonfunctional mutant or chimeric molecules.…”

Section: Discussionsupporting

confidence: 62%

See 1 more Smart Citation

Receptor-binding properties of a purified fragment of the 4070A amphotropic murine leukemia virus envelope glycoprotein

Battini

Rodrigues

Müller

et al. 1996

J Virol

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A 208-amino-acid amino-terminal fragment of the 4070A amphotropic murine leukemia virus envelope glycoprotein contains all of the determinants required to recognize cell surface amphotropic receptors. This fragment was fused with a streptavidin-binding tag, expressed in Sf9 insect cells by using a baculovirus vector, and purified to homogeneity. The 125 I-labeled purified fragment (AS208) specifically bound various cell lines susceptible to amphotropic murine leukemia virus infection. The number of AS208-binding sites was in the range of 7 ؋ 10 4 to 17 ؋ 10 4 per cell. Quantitative analysis of binding revealed that AS208-binding sites are heterogeneous with regard to ligand binding affinity or that cooperativity exists between receptors. Competition experiments showed that the concentration of AS208 required to inhibit virus entry was lower than that required to inhibit the binding of virus particles at the cell surface. Taken together, these data suggested that amphotropic envelope-binding sites present at the cell surface do not act independently and do not participate equally in virus infection.

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Section: Discussionsupporting

confidence: 62%

“…Alleles associated with susceptibility or resistance to infection have been isolated. Sequence comparison and chimeric receptor molecules led to the identification of determinants interacting with SU molecules in the third and fourth extracellular loops of the Rec-1 (1,51) and Ram-1 (19,35,48) proteins, respectively.…”

mentioning

confidence: 99%

Receptor-binding properties of a purified fragment of the 4070A amphotropic murine leukemia virus envelope glycoprotein

Battini

Rodrigues

Müller

et al. 1996

J Virol

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“…Moreover, the hypothesis that region A should be intracellular in PiT1 and extracellular in PiT2 seems in conflict with the observation that a PiT2 mutant with PiT1 region A sequence is receptor for both PiT1 and PiT2 cognate viruses [36] but shows unimpaired P i uptake function compared to PiT2 (P. Bøttger and L. Pedersen, unpublished work). Taken together the current data on receptor and transport functions of PiT1, PiT2, Pho4, and chimeras derived from these are all in favor [23,26,36,37,[45][46][47][48][49][50][51][52][53][54][55], or at least are not in conflict with [41], an extracellular position of region A. Thus, the most likely membrane topology of both PiT1 and PiT2 is that proposed by Salau¨n et al for PiT2 [23] (Fig.…”

supporting

confidence: 76%

Evolutionary and experimental analyses of inorganic phosphate transporter PiT family reveals two related signature sequences harboring highly conserved aspartic acids critical for sodium‐dependent phosphate transport function of human PiT2

Bøttger

Pedersen

2005

The FEBS Journal

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The mammalian members of the inorganic phosphate (P i ) transporter (PiT) family, the type III sodium-dependent phosphate (NaP i ) transporters PiT1 and PiT2, have been assigned housekeeping P i transport functions and are suggested to be involved in chondroblastic and osteoblastic mineralization and ectopic calcification. The PiT family members are conserved throughout all kingdoms and use either sodium (Na + ) or proton (H + ) gradients to transport P i . Sequence logo analyses revealed that independent of their cation dependency these proteins harbor conserved signature sequences in their N-and C-terminal ends with the common core consensus sequence GANDVANA. With the exception of 10 proteins from extremophiles all 109 proteins analyzed carry an aspartic acid in one or both of the signature sequences. We changed either of the highly conserved aspartates, Asp28 and Asp506, in the N-and C-terminal signature sequences, respectively, of human PiT2 to asparagine and analyzed P i uptake function in Xenopus laevis oocytes. Both mutant proteins were expressed at the cell surface of the oocytes but exhibited knocked out NaP i transport function. Human PiT2 is also a retroviral receptor and we have previously shown that this function can be exploited as a control for proper processing and folding of mutant proteins. Both mutant transporters displayed wild-type receptor functions implying that their overall architecture is undisturbed. Thus the presence of an aspartic acid in either of the PiT family signature sequences is critical for the Na + -dependent P i transport function of human PiT2. The conservation of the aspartates among proteins using either Na + -or H + -gradients for P i transport suggests that they are involved in H + -dependent P i transport as well. Current results favor a membrane topology model in which the N-and C-terminal PiT family signature sequences are positioned in intra-and extracellular loops, respectively, suggesting that they are involved in related functions on either side of the membrane. The present data are in agreement with a possible role of the signature sequences in translocation of cations.Abbreviations 10A1, an MLV isolate related to AM-MLV; AM-MLV, amphotropic MLV; CHO, Chinese hamster ovary; FeLV-B, feline leukemia virus subgroup B; GALV, gibbon ape leukemia virus; MLV, murine leukemia virus; NaP i , sodium-dependent phosphate; PiT, inorganic phosphate transporter; RADAR, rapid automatic detection and alignment of repeats.

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“…These results demonstrate a striking similarity between determinants important for viral recognition on three otherwise unrelated retroviral receptors (2,5,15). Interestingly, the cellular receptor for gibbon ape leukemia virus contains a tyrosine (at position 549) which is immediately adjacent to a charged amino acid required for infection, but the importance of this aromatic residue remains to be determined (14,21,24).…”

Section: Discussionmentioning

confidence: 81%

Identification and characterization of the viral interaction determinant of the subgroup A avian leukosis virus receptor

Zingler

Bélanger

Peters

et al. 1995

J Virol

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The cellular receptor for subgroup A avian leukosis viruses (ALV-A) has a small, 83-amino-acid extracellular domain containing a motif that is related in sequence to the ligand binding repeats of the low-density lipoprotein receptor. Extensive mutagenesis of the ALV-A receptor has identified two acidic amino acids (Asp-46 and Glu-47) and an adjacent aromatic amino acid (Trp-48) in the carboxy-terminal portion of this low-density lipoprotein receptor-related motif that are crucial for efficient viral entry. In addition, a 19-aminoacid peptide derived from this region efficiently and specifically blocked subgroup A viral infection when oxidized to form a disulfide bond previously predicted to form in the native receptor (C. Bélanger, K. Zingler, and J. A. T. Young, J. Virol. 69:1019-1024, 1995). Thus, the charged and aromatic amino acid determinants that are required for viral infection appear to lie on a small loop region of the ALV-A receptor. Previously, a single aromatic and one or more charged residues on the CD4 receptor for human and simian immunodeficiency viruses, and the MCAT receptor for ecotropic murine leukemia viruses, were shown to be important for viral entry. These results suggest that different retroviruses may recognize related determinants on structurally divergent cellular receptors.

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Definition of a domain of GLVR1 which is necessary for infection by gibbon ape leukemia virus and which is highly polymorphic between species

Cited by 71 publications

References 16 publications

Receptor-binding properties of a purified fragment of the 4070A amphotropic murine leukemia virus envelope glycoprotein

Receptor-binding properties of a purified fragment of the 4070A amphotropic murine leukemia virus envelope glycoprotein

Evolutionary and experimental analyses of inorganic phosphate transporter PiT family reveals two related signature sequences harboring highly conserved aspartic acids critical for sodium‐dependent phosphate transport function of human PiT2

Identification and characterization of the viral interaction determinant of the subgroup A avian leukosis virus receptor

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