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Lysis of oncornaviruses by human serum. Isolation of the viral complement (C1) receptor and identification as p15E

Moloney leukemia virus activated both the classical and alternative pathways of human complement. About 500,000 virions were required to detect activation of the classical pathway whereas 5,000 times as many virions were necessary to initiate the alternative pathway, indicating that in this system o...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1978
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2184190/
https://www.ncbi.nlm.nih.gov/pubmed/632750
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description Moloney leukemia virus activated both the classical and alternative pathways of human complement. About 500,000 virions were required to detect activation of the classical pathway whereas 5,000 times as many virions were necessary to initiate the alternative pathway, indicating that in this system only the former is of biological significance. Disruption of the virus with Triton X-100 destroyed its ability to initiate the alternative pathway without affecting its ability to activate the classical pathway. After ultracentrifugation of disrupted virus the active component could be recovered in the supernate and was isolated by isoelectric focusing in granulated gels. Sodium dodecyl sulfate-polyacrylamide gel electrophoretic and analysis and cyanogen bromide digestion studies revealed that the activity resided in a methionine-containing protein having a pI of 7.5 and a molecular weight of approximately equal to 15,000 daltons. The purified protein interacts strongly with Clq and efficiently activates Cl. RNase and lipolytic enzymes had no effect on the isolated protein but incubation with trypsin resulted in loss of activity. Enzymatic digestion studies of surface-labeled virus indicate that the active protein is a viral membrane protein. On the basis of these results it is concluded that the complement receptor of Moloney leukemia virus is the surface protein p15E.
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spelling pubmed-21841902008-04-17 Lysis of oncornaviruses by human serum. Isolation of the viral complement (C1) receptor and identification as p15E J Exp Med Articles Moloney leukemia virus activated both the classical and alternative pathways of human complement. About 500,000 virions were required to detect activation of the classical pathway whereas 5,000 times as many virions were necessary to initiate the alternative pathway, indicating that in this system only the former is of biological significance. Disruption of the virus with Triton X-100 destroyed its ability to initiate the alternative pathway without affecting its ability to activate the classical pathway. After ultracentrifugation of disrupted virus the active component could be recovered in the supernate and was isolated by isoelectric focusing in granulated gels. Sodium dodecyl sulfate-polyacrylamide gel electrophoretic and analysis and cyanogen bromide digestion studies revealed that the activity resided in a methionine-containing protein having a pI of 7.5 and a molecular weight of approximately equal to 15,000 daltons. The purified protein interacts strongly with Clq and efficiently activates Cl. RNase and lipolytic enzymes had no effect on the isolated protein but incubation with trypsin resulted in loss of activity. Enzymatic digestion studies of surface-labeled virus indicate that the active protein is a viral membrane protein. On the basis of these results it is concluded that the complement receptor of Moloney leukemia virus is the surface protein p15E. The Rockefeller University Press 1978-03-01 /pmc/articles/PMC2184190/ /pubmed/632750 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Lysis of oncornaviruses by human serum. Isolation of the viral complement (C1) receptor and identification as p15E
title Lysis of oncornaviruses by human serum. Isolation of the viral complement (C1) receptor and identification as p15E
title_full Lysis of oncornaviruses by human serum. Isolation of the viral complement (C1) receptor and identification as p15E
title_fullStr Lysis of oncornaviruses by human serum. Isolation of the viral complement (C1) receptor and identification as p15E
title_full_unstemmed Lysis of oncornaviruses by human serum. Isolation of the viral complement (C1) receptor and identification as p15E
title_short Lysis of oncornaviruses by human serum. Isolation of the viral complement (C1) receptor and identification as p15E
title_sort lysis of oncornaviruses by human serum. isolation of the viral complement (c1) receptor and identification as p15e
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2184190/
https://www.ncbi.nlm.nih.gov/pubmed/632750