Transfer of mouse anti-xenotropic virus neutralizing factor to human lipoproteins

Levy, Jay A.; Dimpfl, J.; Hardman, David A.; Kane, John P.

doi:10.1128/jvi.42.2.365-371.1982

Cited by 7 publications

(2 citation statements)

References 15 publications

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“…Together, these results imply that the X-receptors of mice must be polymorphic and that susceptibilities to infections by X-MLVs and P-MLVs are regulated by these polymorphisms and also by inherited interference factors that differentially interact with X-receptors of distinct mouse strains. In addition, a lipoprotein factor in the sera of most mouse strains specifically inactivates X-MLVs and P-MLVs but not other host range classes of MLVs (15,(21)(22)(23). X-MLV gene expression is also partially silenced in certain mouse cells (13, 19a).…”

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confidence: 99%

Polymorphisms of the Cell Surface Receptor Control Mouse Susceptibilities to Xenotropic and Polytropic Leukemia Viruses

Marin

Tailor

Nouri

et al. 1999

J Virol

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The differential susceptibilities of mouse strains to xenotropic and polytropic murine leukemia viruses (X-MLVs and P-MLVs, respectively) are poorly understood but may involve multiple mechanisms. Recent evidence has demonstrated that these viruses use a common cell surface receptor (the X-receptor) for infection of human cells. We describe the properties of X-receptor cDNAs with distinct sequences cloned from five laboratory and wild strains of mice and from hamsters and minks. Expression of these cDNAs in resistant cells conferred susceptibilities to the same viruses that naturally infect the animals from which the cDNAs were derived. Thus, a laboratory mouse (NIH Swiss) X-receptor conferred susceptibility to P-MLVs but not to X-MLVs, whereas those from humans, minks, and several wild mice (Mus dunni, SC-1 cells, and Mus spretus) mediated infections by both X-MLVs and P-MLVs. In contrast, X-receptors from the resistant mouse strain Mus castaneus and from hamsters were inactive as viral receptors. These results suggest that X-receptor polymorphisms are a primary cause of resistances of mice to members of the X-MLV/P-MLV family of retroviruses and are responsible for the xenotropism of X-MLVs in laboratory mice. By site-directed mutagenesis, we substituted sequences between the X-receptors ofM. dunni and NIH Swiss mice. The NIH Swiss protein contains two key differences (K500E in presumptive extracellular loop 3 [ECL 3] and a T582 deletion in ECL 4) that are both required to block X-MLV infections. Accordingly, a single inverse mutation in the NIH Swiss protein conferred X-MLV susceptibility. Furthermore, expression of an X-MLV envelope glycoprotein in Chinese hamster ovary cells interfered efficiently with X-MLV and P-MLV infections mediated by X-receptors that contained K500 and/or T582 but had no effect on P-MLV infections mediated by X-receptors that lacked these amino acids. In contrast, moderate expression of a P-MLV (MCF247) envelope glycoprotein did not cause substantial interference, suggesting that X-MLV and P-MLV glycoproteins interfere nonreciprocally with X-receptor-mediated infections. We conclude that P-MLVs have become adapted to utilize X-receptors that lack K500 and T582. A penalty for this adaptation is a reduced ability to interfere with superinfection. Because failure of interference is a hallmark of several exceptionally pathogenic retroviruses, we propose that it contributes to P-MLV-induced diseases.

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confidence: 99%

Polymorphisms of the Cell Surface Receptor Control Mouse Susceptibilities to Xenotropic and Polytropic Leukemia Viruses

Marin

Tailor

Nouri

et al. 1999

J Virol

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“…Prominent among these appears to be their participation in reverse cholesterol transport (Fielding & Fielding, 1982;Glomset, 1968). Additionally, they are also implicated in a number of other processes such as blood coagulation (Bareowcliffe et al, 1982;Carson, 1981), inhibition of viral infection (Kane etal., 1979;Levy et al, 1982), inhibition of infection by protozoal parasites (Ormerod & Venkatesan, 1982), delivery of cholesterol to steroidogenic cells (Chen etal., 1980;McNamara et al, 1981;Ohashi et al, 1981), degradation of bacterial endotoxins (Ulevitch et al, 1981), inhibition of LDL oxidation (Klimov, 1987;Kunitake et al, 1992;Ohta et al, 1989;Parthasarathy et al, 1990), and perhaps stimulation of vascular endothelium (Tauber et al, 1981).…”

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confidence: 99%

Identification of Proteins Associated with Apolipoprotein A-I-Containing Lipoproteins Purified by Selected-Affinity Immunosorption

Kunitake¹,

Carilli²,

Lau³

et al. 1994

Biochemistry

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The isolation of apolipoprotein A-I-containing lipoproteins [Lp(A-I)] by selected-affinity immunosorption minimizes the loss of associated proteins that occurs during the isolation of high-density lipoproteins (HDL) by sequential ultracentrifugation. We have used two-dimensional gel electrophoretic analysis to separate the proteins associated with Lp(A-I). Using a combination of amino acid sequencing of transblotted proteins and Western blotting with specific antisera, we have identified a number of associated proteins. The positions of the apolipoproteins (apo) A-I, A-II, A-IV, C-III, D, and E were located on the gels. Lecithin-cholesterol acyltransferase and cholesteryl ester transfer protein were identified in association with Lp(A-I) to a greater extent than found associated with HDL after centrifugation. In addition to those proteins previously identified in association with HDL, we detected a number of plasma proteins associated with Lp(A-I), namely, fibrinogen, haptoglobin, proline-rich protein (C4b-binding protein), and apolipoprotein J (SP40,40 sulfated glycoprotein). The co-isolation of these proteins with Lp(A-I) does not appear to be an artifact in that they have very low affinity for a sham column containing covalently bound preimmune goat IgG in place of the anti-apoA-I IgG. These findings suggest that in addition to apolipoproteins that exist largely in association with lipoproteins there is another class of proteins which exist in lipoprotein-associated form and in the dispersed state. Detection and identification of these lipoprotein-associated proteins may aid in the mechanistic determination of a number of observed functions attributed to HDL.

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Speciation of HDL

Kane

1986

Lipoprotein Deficiency Syndromes

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Transfer of mouse anti-xenotropic virus neutralizing factor to human lipoproteins

Cited by 7 publications

References 15 publications

Polymorphisms of the Cell Surface Receptor Control Mouse Susceptibilities to Xenotropic and Polytropic Leukemia Viruses

Polymorphisms of the Cell Surface Receptor Control Mouse Susceptibilities to Xenotropic and Polytropic Leukemia Viruses

Identification of Proteins Associated with Apolipoprotein A-I-Containing Lipoproteins Purified by Selected-Affinity Immunosorption

Speciation of HDL

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