The mechanisms of reovirus uncoating and gene activation in vivo

Samuel C. Silverstein; Caroline Astell; Daniel H. Levin; Michael Schonberg; George Acs

doi:10.1016/0042-6822(72)90571-5

The mechanisms of reovirus uncoating and gene activation in vivo

Samuel C. Silverstein, Caroline Astell, Daniel H. Levin, Michael Schonberg, George Acs

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

113 Scopus citations

Abstract

Reovirus is concentrated in lysosomes soon after penetrating L cells. Hydrolases contained within the lysosomal compartment digest the outer layer of viral capsomeres but do not degrade the viral core proteins which form the subviral particle (SVP). Parental SVPs have been recovered from reovirus-infected cells. These SVPs are similar, but not identical, in morphology and protein composition to SVPs produced in vitro by chymotrypsin digestion of intact virus. Moreover, they catalyze the synthesis of ssRNA molecules which hybridize specifically with all ten segments of the double-stranded viral genome.

Original language	English
Pages (from-to)	797-806
Number of pages	10
Journal	Virology
Volume	47
Issue number	3
DOIs	https://doi.org/10.1016/0042-6822(72)90571-5
State	Published - Mar 1972
Externally published	Yes

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title = "The mechanisms of reovirus uncoating and gene activation in vivo",

abstract = "Reovirus is concentrated in lysosomes soon after penetrating L cells. Hydrolases contained within the lysosomal compartment digest the outer layer of viral capsomeres but do not degrade the viral core proteins which form the subviral particle (SVP). Parental SVPs have been recovered from reovirus-infected cells. These SVPs are similar, but not identical, in morphology and protein composition to SVPs produced in vitro by chymotrypsin digestion of intact virus. Moreover, they catalyze the synthesis of ssRNA molecules which hybridize specifically with all ten segments of the double-stranded viral genome.",

author = "Silverstein, \{Samuel C.\} and Caroline Astell and Levin, \{Daniel H.\} and Michael Schonberg and George Acs",

note = "Funding Information: i This work was supported by Grants AI-08697 and CA-08751 from the National Institutes of Health and Grant P-299 from the American Cancer Society and by the Muscular Dystrophy Associations of America.",

year = "1972",

month = mar,

doi = "10.1016/0042-6822(72)90571-5",

language = "English",

volume = "47",

pages = "797--806",

journal = "Virology",

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publisher = "Academic Press Inc.",

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T1 - The mechanisms of reovirus uncoating and gene activation in vivo

AU - Silverstein, Samuel C.

AU - Astell, Caroline

AU - Levin, Daniel H.

AU - Schonberg, Michael

AU - Acs, George

N1 - Funding Information: i This work was supported by Grants AI-08697 and CA-08751 from the National Institutes of Health and Grant P-299 from the American Cancer Society and by the Muscular Dystrophy Associations of America.

PY - 1972/3

Y1 - 1972/3

N2 - Reovirus is concentrated in lysosomes soon after penetrating L cells. Hydrolases contained within the lysosomal compartment digest the outer layer of viral capsomeres but do not degrade the viral core proteins which form the subviral particle (SVP). Parental SVPs have been recovered from reovirus-infected cells. These SVPs are similar, but not identical, in morphology and protein composition to SVPs produced in vitro by chymotrypsin digestion of intact virus. Moreover, they catalyze the synthesis of ssRNA molecules which hybridize specifically with all ten segments of the double-stranded viral genome.

AB - Reovirus is concentrated in lysosomes soon after penetrating L cells. Hydrolases contained within the lysosomal compartment digest the outer layer of viral capsomeres but do not degrade the viral core proteins which form the subviral particle (SVP). Parental SVPs have been recovered from reovirus-infected cells. These SVPs are similar, but not identical, in morphology and protein composition to SVPs produced in vitro by chymotrypsin digestion of intact virus. Moreover, they catalyze the synthesis of ssRNA molecules which hybridize specifically with all ten segments of the double-stranded viral genome.

UR - https://www.scopus.com/pages/publications/0015304204

U2 - 10.1016/0042-6822(72)90571-5

DO - 10.1016/0042-6822(72)90571-5

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AN - SCOPUS:0015304204

SN - 0042-6822

VL - 47

SP - 797

EP - 806

JO - Virology

JF - Virology

IS - 3

ER -

The mechanisms of reovirus uncoating and gene activation in vivo

Abstract

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