Anti-VPg antibody inhibition of the poliovirus replicase reaction and production of covalent complexes of VPg-related proteins and RNA

Margaret H. Baron; David Baltimore

doi:10.1016/0092-8674(82)90279-3

Anti-VPg antibody inhibition of the poliovirus replicase reaction and production of covalent complexes of VPg-related proteins and RNA

Margaret H. Baron
, David Baltimore

Research output: Contribution to journal › Article › peer-review

24 Scopus citations

Abstract

Anti-VPg antibodies inhibited host-factor-dependent RNA synthesis by the poliovirus replicase but not oligo(U)-primed synthesis, implicating VPg in the de novo initiation of replicase products. Complexes of VPg-related polypeptide and newly made RNA could be immunoprecipitated by anti-VPg antibody from the host-factor-stimulated products of the replicase reaction. The complexes appeared to be covalently linked and involved 50 to 150 nucleotide chains of RNA that were RNAase-T1-resistant and could be largely poly(U).

Original language	English
Pages (from-to)	745-752
Number of pages	8
Journal	Cell
Volume	30
Issue number	3
DOIs	https://doi.org/10.1016/0092-8674(82)90279-3
State	Published - Oct 1982
Externally published	Yes

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@article{2f159cfb6de343f6b4685e0023a1fded,

title = "Anti-VPg antibody inhibition of the poliovirus replicase reaction and production of covalent complexes of VPg-related proteins and RNA",

abstract = "Anti-VPg antibodies inhibited host-factor-dependent RNA synthesis by the poliovirus replicase but not oligo(U)-primed synthesis, implicating VPg in the de novo initiation of replicase products. Complexes of VPg-related polypeptide and newly made RNA could be immunoprecipitated by anti-VPg antibody from the host-factor-stimulated products of the replicase reaction. The complexes appeared to be covalently linked and involved 50 to 150 nucleotide chains of RNA that were RNAase-T1-resistant and could be largely poly(U).",

author = "Baron, \{Margaret H.\} and David Baltimore",

note = "Funding Information: M. H. B. is a predoctoral scholar of the Insurance Medical Scientist Scholarship Fund and a fellow of the Danforth Foundation. D. 6. is an American Cancer Society Professor of Microbiology. We thank Dr. Andrew Laudano of M. I. T. for generous provision of a control peptide. This research was supported by grants from the National Institute of Allergy and Infectious Disease and from the National Cancer Institute.",

year = "1982",

month = oct,

doi = "10.1016/0092-8674(82)90279-3",

language = "English",

volume = "30",

pages = "745--752",

journal = "Cell",

issn = "0092-8674",

publisher = "Elsevier B.V.",

number = "3",

}

TY - JOUR

T1 - Anti-VPg antibody inhibition of the poliovirus replicase reaction and production of covalent complexes of VPg-related proteins and RNA

AU - Baron, Margaret H.

AU - Baltimore, David

N1 - Funding Information: M. H. B. is a predoctoral scholar of the Insurance Medical Scientist Scholarship Fund and a fellow of the Danforth Foundation. D. 6. is an American Cancer Society Professor of Microbiology. We thank Dr. Andrew Laudano of M. I. T. for generous provision of a control peptide. This research was supported by grants from the National Institute of Allergy and Infectious Disease and from the National Cancer Institute.

PY - 1982/10

Y1 - 1982/10

N2 - Anti-VPg antibodies inhibited host-factor-dependent RNA synthesis by the poliovirus replicase but not oligo(U)-primed synthesis, implicating VPg in the de novo initiation of replicase products. Complexes of VPg-related polypeptide and newly made RNA could be immunoprecipitated by anti-VPg antibody from the host-factor-stimulated products of the replicase reaction. The complexes appeared to be covalently linked and involved 50 to 150 nucleotide chains of RNA that were RNAase-T1-resistant and could be largely poly(U).

AB - Anti-VPg antibodies inhibited host-factor-dependent RNA synthesis by the poliovirus replicase but not oligo(U)-primed synthesis, implicating VPg in the de novo initiation of replicase products. Complexes of VPg-related polypeptide and newly made RNA could be immunoprecipitated by anti-VPg antibody from the host-factor-stimulated products of the replicase reaction. The complexes appeared to be covalently linked and involved 50 to 150 nucleotide chains of RNA that were RNAase-T1-resistant and could be largely poly(U).

UR - https://www.scopus.com/pages/publications/0020200618

U2 - 10.1016/0092-8674(82)90279-3

DO - 10.1016/0092-8674(82)90279-3

M3 - Article

C2 - 6291782

AN - SCOPUS:0020200618

SN - 0092-8674

VL - 30

SP - 745

EP - 752

JO - Cell

JF - Cell

IS - 3

ER -

Anti-VPg antibody inhibition of the poliovirus replicase reaction and production of covalent complexes of VPg-related proteins and RNA

Abstract

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