Interferon Effect on Cellular Functions: Enhancement of Virus Induced Inhibition of Host Cell Protein Synthesis in Interferon-Treated Cells

1974 ◽  
Vol 29 (9-10) ◽  
pp. 623-629 ◽  
Author(s):  
M Suh ◽  
G Bodo ◽  
W Wolf ◽  
G Viehhauser ◽  
C Jungwirth
Keyword(s):  
Protein Synthesis ◽  
Chick Embryo ◽  
Host Cell ◽  
Total Protein ◽  
Cell Protein ◽  
Cellular Functions ◽  
Amino Acid Incorporation ◽  
Host Cell Proteins ◽  
Mouse Cells ◽  
Embryo Fibroblasts

Abstract Total protein synthesis in mouse cells but not in confluent chick embryo fibroblasts (CEF) is inhibited shortly after infection with vaccinia virus. This inhibition by the infecting virus is enhanced drastically if the mouse cells have been pretreated with homologous interferon pre­parations. The enhanced reduction of protein synthesis also occurs if the cells are treated with actinomycin D and is therefore to a large extent caused by an enhanced inhibition of amino acid incorporation into host cell proteins. Enhanced inhibition of total protein synthesis during the early stages of infection may be a prerequisite for the complete degeneration of the cells (lysis) which occurs later. Various alterations of mouse cells and chick embryo fibroblasts due to exposure to homologous interferon preparations are discussed with respect to the antiviral state induced in these cells

Protein synthesis in different cell lines infected with orthoreovirus serotype 3: inhibition of host-cell protein synthesis correlates with accelerated viral multiplication and cell killing

1993 ◽  
Vol 71 (1-2) ◽  
pp. 81-85 ◽  
Author(s):  
Carole Danis ◽  
Guy Lemay
Keyword(s):  
Protein Synthesis ◽  
Host Cell ◽  
Cell Lines ◽  
Cell Killing ◽  
Cell Protein ◽  
Protein Synthesis Inhibition ◽  
Cytopathic Effects ◽  
Viral Multiplication ◽  
Host Cell Proteins ◽  
Mammalian Cell Lines

In this study, we examined the viral multiplication of human reovirus serotype 3 in mammalian cell lines of different species and tissue origins. All cell lines supported viral multiplication to a similar extent, although the kinetics was significantly different in some of these lines. The appearance of infectious virus was delayed in few cell lines. These cell lines also exhibited a much slower rate of cell killing, and in contrast to the others, did not exhibit an inhibition of the synthesis of host-cell proteins. We conclude that the inhibition correlates with rapid cell killing and viral multiplication, while being unrelated to efficient total viral production.Key words: reovirus, protein synthesis inhibition, viral multiplication, cytopathic effects.

Effect of adenovirus on metabolism of specific host mRNAs: transport control and specific translational discrimination

1983 ◽  
Vol 3 (7) ◽  
pp. 1212-1221 ◽  
Author(s):  
A Babich ◽  
L T Feldman ◽  
J R Nevins ◽  
J E Darnell ◽  
C Weinberger
Keyword(s):  
Protein Synthesis ◽  
Host Cell ◽  
Cellular Protein ◽  
Host Protein ◽  
Cell Protein ◽  
Viral Mrna ◽  
Initiation Of Translation ◽  
Viral Mutant ◽  
Cellular Mrnas ◽  
Cellular Protein Synthesis

We have studied the adenovirus-induced inhibition of host cell protein synthesis and the effect of infection on the overall metabolism of host cell mRNA during the late phase of adenovirus infection by following the fate of a number of cellular mRNAs complementary to specific cloned DNA segments. At a time in infection when the rate of total cellular protein synthesis is drastically (greater than 90%) reduced, transcription of specific cellular genes is undiminished. However, the transport of newly synthesized cellular mRNA to the cytoplasm is greatly decreased. This decreased appearance of new mRNA in the cytoplasm cannot account for the observed cessation of cell specific protein synthesis, however, since the concentration of several preexisting cellular mRNAs, including the mRNA for actin, remains unchanged throughout the course of infection. The preexisting mRNA is intact, capped, and functional as judged by its ability to direct protein synthesis in vitro in a cap-dependent fashion. The interruption in host translation appears to operate at the level of initiation directly, since we find that fewer ribosomes are associated with a given cellular mRNA after infection than before infection. Furthermore, the in vivo inhibition of cellular protein synthesis does not appear to be the result of competition with viral mRNA, since conditions which prevent the efficient initiation of translation of viral mRNA (infection with a viral mutant) do not result in the recovery of cell translation. Thus, it appears that a late adenovirus gene product directly mediates a shutoff of host protein synthesis.

scholarly journals Improving Chinese hamster ovary host cell protein ELISA using Ella®: an automated microfluidic platform

BioTechniques ◽  
2020 ◽  
Vol 69 (3) ◽  
pp. 186-192
Author(s):  
Kathleen Van Manen-Brush ◽  
Jacob Zeitler ◽  
John R White ◽  
Paul Younge ◽  
Samantha Willis ◽  
...  
Keyword(s):  
Host Cell ◽  
Chinese Hamster Ovary ◽  
Expression System ◽  
Chinese Hamster ◽  
Cell Protein ◽  
Enzyme Linked Immunosorbent Assay ◽  
Host Cell Proteins ◽  
Common Technique ◽  
Automated Instrument ◽  
Cell Expression

Chinese hamster ovary (CHO) cells are a mammalian cell line used in the production of therapeutic proteins. Host cell proteins (HCPs) are process-related impurities that are derived from the host cell expression system. During biopharmaceutical drug development, removal of HCPs is required. Enzyme-linked immunosorbent assay (ELISA) is a common technique to quantitate HCPs, but is a labor-intensive process that takes up to 7 h. Ella® is an automated instrument that utilizes microfluidics and glass nanoreactors to quantitate HCPs in 75 min using similar ELISA reagents. The antibodies and antigens are captured on three distinct glass nanoreactors, resulting in sensitive reproducible data. Our results indicate that Ella quantitates CHO HCPs with precision, accuracy, sensitivity and trends comparable with our traditional CHO HCP ELISA.

In Vitro Evaluation of Plasticizer Activity on the Growth and Metabolism of Chick Embryo Fibroblasts and on the Development of Chick Embryo Lungs

1992 ◽  
Vol 20 (6) ◽  
pp. 475-482 ◽  
Author(s):  
G Stabellini ◽  
O Fiocchi ◽  
A Pellati ◽  
A Caruso
Keyword(s):  
Cell Proliferation ◽  
Protein Synthesis ◽  
Chick Embryo ◽  
Primary Cultures ◽  
Embryonic Cells ◽  
Cytostatic Effect ◽  
Dna And Protein Synthesis ◽  
Embryo Fibroblasts ◽  
Ethylhexyl Phthalate

Administration of di(2-ethylhexyl) phthalate (DEHP) to primary cultures of chick embryo fibroblasts brought about a decrease in cell proliferation rate after 48 h and an inhibition of both DNA and protein synthesis measured by [3H]thymidine and [3H]leucine, respectively, after 48h. The growth of chick embryo lung rudiments in vitro was also depressed by DEHP treatment. Lung rudiment were smaller in DEHP-treated embryos after 6 days' treatment. These results indicate that DEHP has a cytostatic effect on embryonic cells and tissues. L'administration de di(2-éthylhexyl) phthalate (DEHP) à des cultures primaires de fibroblastes d'embryon de poulet a provoqué une diminution du taux de prolifération cellulaire après 48 heures et une inhibition de la synthèse à la fois d'ADN et de protéines mesurée, respectivement, par [3H]thymidine et [3H]leucine après 48 h. La croissance des ébauches pulmonaires de l'embryon de poulet in vitro a également été abaissée par le traitement DEHP. Les ébauches pulmonaires étaient plus petites dans les embryons traités au DEHP après un traitement de 6 jours. Ces résultats indiquent que le DEHP a un effet cytostatique sur les cellules et tissus embryonnaires.

Lodish model and regulation of ribosomal protein synthesis by insulin-deficient chick embryo fibroblasts

Biochemistry ◽  
1981 ◽  
Vol 20 (9) ◽  
pp. 2550-2558 ◽  
Author(s):  
George G. Ignotz ◽  
Shigeru Hokari ◽  
Robert M. DePhilip ◽  
Kinji Tsukada ◽  
Irving Lieberman
Keyword(s):  
Protein Synthesis ◽  
Chick Embryo ◽  
Ribosomal Protein ◽  
Embryo Fibroblasts ◽  
Ribosomal Protein Synthesis
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