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Safety and Efficacy of a Pentavalent Human–Bovine …

AB - The synthesis of avian rotavirus (AvRV-1) polypeptides in MA 104 cells was investigated. Extracts of cells labeled with either [35S]methionine or [3H]mannose were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Viral protein synthesis was detected first at 6 hours postinfection. Ten major viral polypeptides were detected at this time. The presence of five viral structural proteins (100K, 90K, 88K, 45K, and 37K) were demonstrated in AvRV-1-infected cells by immunoprecipitation analysis. One structural polypeptide (37K) was identified as a glycoprotein. Two viral polypeptides (30K and 28K) were identified as nonstructural glycoproteins. By tunicamycin inhibition of glycosylation, a 32K polypeptide was identified. This 32K polypeptide later was proven to be the precursor of 37K structural glycoprotein by immunoprecipitation analysis, beta-N-acetylglucosaminidase H (Endo H) treatment, and peptide mapping analysis. Avian rotavirus contained high-mannose oligosaccharide content in the glycoproteins similar to the glycoproteins of mammalian rotaviruses.

T1 - Arginine activates intestinal p70S6k and protein synthesis in piglet rotavirus enteritis

The synthesis of avian rotavirus (AvRV-1) polypeptides in MA 104 cells was investigated. Extracts of cells labeled with either [35S]methionine or [3H]mannose were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Viral protein synthesis was detected first at 6 hours postinfection. Ten major viral polypeptides were detected at this time. The presence of five viral structural proteins (100K, 90K, 88K, 45K, and 37K) were demonstrated in AvRV-1-infected cells by immunoprecipitation analysis. One structural polypeptide (37K) was identified as a glycoprotein. Two viral polypeptides (30K and 28K) were identified as nonstructural glycoproteins. By tunicamycin inhibition of glycosylation, a 32K polypeptide was identified. This 32K polypeptide later was proven to be the precursor of 37K structural glycoprotein by immunoprecipitation analysis, beta-N-acetylglucosaminidase H (Endo H) treatment, and peptide mapping analysis. Avian rotavirus contained high-mannose oligosaccharide content in the glycoproteins similar to the glycoproteins of mammalian rotaviruses.

Reverse transcription polymerase chain reaction - …

Rotavirus RNA polymerase requires the core shell protein to synthesize the double-stranded RNA genome’s profile, publications, research topics, and co-authors

N2 - The synthesis of avian rotavirus (AvRV-1) polypeptides in MA 104 cells was investigated. Extracts of cells labeled with either [35S]methionine or [3H]mannose were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Viral protein synthesis was detected first at 6 hours postinfection. Ten major viral polypeptides were detected at this time. The presence of five viral structural proteins (100K, 90K, 88K, 45K, and 37K) were demonstrated in AvRV-1-infected cells by immunoprecipitation analysis. One structural polypeptide (37K) was identified as a glycoprotein. Two viral polypeptides (30K and 28K) were identified as nonstructural glycoproteins. By tunicamycin inhibition of glycosylation, a 32K polypeptide was identified. This 32K polypeptide later was proven to be the precursor of 37K structural glycoprotein by immunoprecipitation analysis, beta-N-acetylglucosaminidase H (Endo H) treatment, and peptide mapping analysis. Avian rotavirus contained high-mannose oligosaccharide content in the glycoproteins similar to the glycoproteins of mammalian rotaviruses.

AB - We previously showed that phosphorylation of p70 S6 kinase (p70 S6k) in the intestine is increased during viral enteritis. In this study, we hypothesized that during rotavirus infection, oral Arg, which stimulates p70S6k activation, will further stimulate intestinal protein synthesis and mucosal recovery, whereas the p70S6k inhibitor rapamycin (Rapa) will inhibit mucosal recovery. Newborn piglets were fed a standard milk replacer diet supplemented with Arg (0.4 g·kg -1·d-1, twice daily by gavage), Rapa (2 mg·m-2·d-1), Arg 1 Rapa, or saline (controls). They were infected on d 6 of life with porcine rotavirus. Three days postinoculation, we measured the piglets' body weight, fecal rotavirus excretion, villus-crypt morphology, epithelial electrical resistance in Ussing chambers, and p70S6k activation by Western blotting and immunohistochemistry. We previously showed a 2-fold increase in jejunal protein synthesis during rotavirus diarrhea. In this experiment, Arg stimulated jejunal protein synthesis 1.3-fold above standard medium, and the Arg stimulation was partially inhibited by Rapa. Small bowel stimulation of p70S6k phosphorylation and p70S6k levels were inhibited .80% by Rapa. Immunohistochemistry revealed a major increase of p70S6k and ribosomal protein S6 phosphorylation in the crypt and lower villus of the infected piglets. However, in Arg-treated piglets, p70S6k activation occurred over the entire villus. Jejunal villi of the Rapa-treated group showed inactivation of p70S6k and a decrease in mucosal resistance (reflecting increased permeability), the latter of which was reversed by Arg. We conclude that, early in rotavirus enteritis, Arg has no impact on diarrhea but augments intestinal protein synthesis in part by p70S6k stimulation, while improving intestinal permeability via a mammalian target of rapamycin/p70S6k-independent mechanism.

ITGB1 Gene - GeneCards | ITB1 Protein | ITB1 Antibody

N2 - We previously showed that phosphorylation of p70 S6 kinase (p70 S6k) in the intestine is increased during viral enteritis. In this study, we hypothesized that during rotavirus infection, oral Arg, which stimulates p70S6k activation, will further stimulate intestinal protein synthesis and mucosal recovery, whereas the p70S6k inhibitor rapamycin (Rapa) will inhibit mucosal recovery. Newborn piglets were fed a standard milk replacer diet supplemented with Arg (0.4 g·kg -1·d-1, twice daily by gavage), Rapa (2 mg·m-2·d-1), Arg 1 Rapa, or saline (controls). They were infected on d 6 of life with porcine rotavirus. Three days postinoculation, we measured the piglets' body weight, fecal rotavirus excretion, villus-crypt morphology, epithelial electrical resistance in Ussing chambers, and p70S6k activation by Western blotting and immunohistochemistry. We previously showed a 2-fold increase in jejunal protein synthesis during rotavirus diarrhea. In this experiment, Arg stimulated jejunal protein synthesis 1.3-fold above standard medium, and the Arg stimulation was partially inhibited by Rapa. Small bowel stimulation of p70S6k phosphorylation and p70S6k levels were inhibited .80% by Rapa. Immunohistochemistry revealed a major increase of p70S6k and ribosomal protein S6 phosphorylation in the crypt and lower villus of the infected piglets. However, in Arg-treated piglets, p70S6k activation occurred over the entire villus. Jejunal villi of the Rapa-treated group showed inactivation of p70S6k and a decrease in mucosal resistance (reflecting increased permeability), the latter of which was reversed by Arg. We conclude that, early in rotavirus enteritis, Arg has no impact on diarrhea but augments intestinal protein synthesis in part by p70S6k stimulation, while improving intestinal permeability via a mammalian target of rapamycin/p70S6k-independent mechanism.

AB - We previously showed that phosphorylation of p70 S6 kinase (p70 S6k) in the intestine is increased during viral enteritis. In this study, we hypothesized that during rotavirus infection, oral Arg, which stimulates p70S6k activation, will further stimulate intestinal protein synthesis and mucosal recovery, whereas the p70S6k inhibitor rapamycin (Rapa) will inhibit mucosal recovery. Newborn piglets were fed a standard milk replacer diet supplemented with Arg (0.4 g·kg -1·d-1, twice daily by gavage), Rapa (2 mg·m-2·d-1), Arg 1 Rapa, or saline (controls). They were infected on d 6 of life with porcine rotavirus. Three days postinoculation, we measured the piglets' body weight, fecal rotavirus excretion, villus-crypt morphology, epithelial electrical resistance in Ussing chambers, and p70S6k activation by Western blotting and immunohistochemistry. We previously showed a 2-fold increase in jejunal protein synthesis during rotavirus diarrhea. In this experiment, Arg stimulated jejunal protein synthesis 1.3-fold above standard medium, and the Arg stimulation was partially inhibited by Rapa. Small bowel stimulation of p70S6k phosphorylation and p70S6k levels were inhibited .80% by Rapa. Immunohistochemistry revealed a major increase of p70S6k and ribosomal protein S6 phosphorylation in the crypt and lower villus of the infected piglets. However, in Arg-treated piglets, p70S6k activation occurred over the entire villus. Jejunal villi of the Rapa-treated group showed inactivation of p70S6k and a decrease in mucosal resistance (reflecting increased permeability), the latter of which was reversed by Arg. We conclude that, early in rotavirus enteritis, Arg has no impact on diarrhea but augments intestinal protein synthesis in part by p70S6k stimulation, while improving intestinal permeability via a mammalian target of rapamycin/p70S6k-independent mechanism.

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NUTRITIONAL ASPECTS OF HUMAN MILK PROTEINS

N2 - We previously showed that phosphorylation of p70 S6 kinase (p70 S6k) in the intestine is increased during viral enteritis. In this study, we hypothesized that during rotavirus infection, oral Arg, which stimulates p70S6k activation, will further stimulate intestinal protein synthesis and mucosal recovery, whereas the p70S6k inhibitor rapamycin (Rapa) will inhibit mucosal recovery. Newborn piglets were fed a standard milk replacer diet supplemented with Arg (0.4 g·kg -1·d-1, twice daily by gavage), Rapa (2 mg·m-2·d-1), Arg 1 Rapa, or saline (controls). They were infected on d 6 of life with porcine rotavirus. Three days postinoculation, we measured the piglets' body weight, fecal rotavirus excretion, villus-crypt morphology, epithelial electrical resistance in Ussing chambers, and p70S6k activation by Western blotting and immunohistochemistry. We previously showed a 2-fold increase in jejunal protein synthesis during rotavirus diarrhea. In this experiment, Arg stimulated jejunal protein synthesis 1.3-fold above standard medium, and the Arg stimulation was partially inhibited by Rapa. Small bowel stimulation of p70S6k phosphorylation and p70S6k levels were inhibited .80% by Rapa. Immunohistochemistry revealed a major increase of p70S6k and ribosomal protein S6 phosphorylation in the crypt and lower villus of the infected piglets. However, in Arg-treated piglets, p70S6k activation occurred over the entire villus. Jejunal villi of the Rapa-treated group showed inactivation of p70S6k and a decrease in mucosal resistance (reflecting increased permeability), the latter of which was reversed by Arg. We conclude that, early in rotavirus enteritis, Arg has no impact on diarrhea but augments intestinal protein synthesis in part by p70S6k stimulation, while improving intestinal permeability via a mammalian target of rapamycin/p70S6k-independent mechanism.

Pall ForteBio :: References in Literature

The eukaryotic initiation translation factor 2 (eIF2) represents a key point in the regulation of protein synthesis. This factor delivers the initiator Met-tRNA to the ribosome, a process that is conserved in all eukaryotic cells. Many types of stress reduce global translation by triggering the phosphorylation of the α subunit of eIF2, which reduces the formation of the preinitiation translation complexes. Early during rotavirus infection, eIF2α becomes phosphorylated, and even under these conditions viral protein synthesis is not affected, while most of the cell protein synthesis is blocked. Here, we found that the kinase responsible for the phosphorylation of eIF2α in rotavirus-infected cells is PKR, since in mouse embryonic fibroblasts deficient in the kinase domain of PKR, or in MA104 cells where the expression of PKR was knocked down by RNA interference, eIF2α was not phosphorylated upon rotavirus infection. The viral component responsible for the activation of PKR seems to be viral double-stranded RNA, which is found in the cytoplasm of infected cells, outside viroplasms. Taken together, these results suggest that rotaviruses induce the PKR branch of the interferon system and have evolved a mechanism to translate its proteins, surpassing the block imposed by eIF2α phosphorylation.

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