The effect of deoxymannojirimycin on the processing of the influenza viral glycoproteins
Deoxymannojirimycin (dMM) was tested as an inhibitor of the processing of the oligosaccharide portion of viral and cellular N-linked glycoproteins. The NWS strain of influenza virus was grown in MDCK cells in the presence of various amounts of dMM, and the glycoproteins were labeled by the addition...
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Published in | Archives of biochemistry and biophysics Vol. 235; no. 2; pp. 579 - 588 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
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San Diego, CA
Elsevier Inc
01.12.1984
Elsevier |
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Abstract | Deoxymannojirimycin (dMM) was tested as an inhibitor of the processing of the oligosaccharide portion of viral and cellular N-linked glycoproteins. The NWS strain of influenza virus was grown in MDCK cells in the presence of various amounts of dMM, and the glycoproteins were labeled by the addition of 2-[
3H]mannose to the medium. At levels of 10 μg/ml dMM or higher, most of the viral glycopeptides became susceptible to digestion by endoglucosaminidase H, and the liberated oligosaccharide migrated mostly like a Hexose
9GlcNAc on a calibrated column of Bio-Gel P-4. This oligosaccharide was characterized as a typical Man
9GlcNAc by a variety of chemical and enzymatic procedures. Deoxymannojirimycin gave rise to similar oligosaccharide structures in the cellular glycoproteins. In both the viral and the cellular glycoproteins, this inhibitor caused a significant increase in the amount of [
3H]mannose present in the glycoproteins. Deoxymannojirimycin did not inhibit the incorporation of [
3H]leucine into protein in MDCK cells, nor did it affect the yield or infectivity of NWS virus particles. However, its effect on mannose incorporation into lipid-linked saccharides depended on the incubation time, the virus strain, and the cell line. Thus, high concentrations of dMM showed some inhibition of mannose incorporation into lipid-linked oligosaccharides with the NWS strain in a 3-h incubation, but no inhibition was observed after 48 h of incubation. On the other hand, the PR8 strain was much more sensitive to dMM inhibition, and mannose incorporation into lipid-linked oligosaccharides was strongly inhibited when the virus was raised in chick embryo cells, but less inhibition was observed when this virus was grown in MDCK cells. Nevertheless, in these cases also, the major oligosaccharide structure in the glycoproteins was the Man
9GlcNAc
2 species. |
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AbstractList | Deoxymannojirimycin (dMM) was tested as an inhibitor of the processing of the oligosaccharide portion of viral and cellular N-linked glycoproteins. The NWS strain of influenza virus was grown in MDCK cells in the presence of various amounts of dMM, and the glycoproteins were labeled by the addition of 2-[
3H]mannose to the medium. At levels of 10 μg/ml dMM or higher, most of the viral glycopeptides became susceptible to digestion by endoglucosaminidase H, and the liberated oligosaccharide migrated mostly like a Hexose
9GlcNAc on a calibrated column of Bio-Gel P-4. This oligosaccharide was characterized as a typical Man
9GlcNAc by a variety of chemical and enzymatic procedures. Deoxymannojirimycin gave rise to similar oligosaccharide structures in the cellular glycoproteins. In both the viral and the cellular glycoproteins, this inhibitor caused a significant increase in the amount of [
3H]mannose present in the glycoproteins. Deoxymannojirimycin did not inhibit the incorporation of [
3H]leucine into protein in MDCK cells, nor did it affect the yield or infectivity of NWS virus particles. However, its effect on mannose incorporation into lipid-linked saccharides depended on the incubation time, the virus strain, and the cell line. Thus, high concentrations of dMM showed some inhibition of mannose incorporation into lipid-linked oligosaccharides with the NWS strain in a 3-h incubation, but no inhibition was observed after 48 h of incubation. On the other hand, the PR8 strain was much more sensitive to dMM inhibition, and mannose incorporation into lipid-linked oligosaccharides was strongly inhibited when the virus was raised in chick embryo cells, but less inhibition was observed when this virus was grown in MDCK cells. Nevertheless, in these cases also, the major oligosaccharide structure in the glycoproteins was the Man
9GlcNAc
2 species. Deoxymannojirimycin (dMM) was tested as an inhibitor of the processing of the oligosaccharide portion of viral and cellular N-linked glycoproteins. The NWS strain of influenza virus was grown in MDCK cells in the presence of various amounts of dMM, and the glycoproteins were labeled by the addition of 2-[3H]mannose to the medium. At levels of 10 micrograms/ml dMM or higher, most of the viral glycopeptides became susceptible to digestion by endoglucosaminidase H, and the liberated oligosaccharide migrated mostly like a Hexose9GlcNAc on a calibrated column of Bio-Gel P-4. This oligosaccharide was characterized as a typical Man9GlcNAc by a variety of chemical and enzymatic procedures. Deoxymannojirimycin gave rise to similar oligosaccharide structures in the cellular glycoproteins. In both the viral and the cellular glycoproteins, this inhibitor caused a significant increase in the amount of [3H]mannose present in the glycoproteins. Deoxymannojirimycin did not inhibit the incorporation of [3H]leucine into protein in MDCK cells, nor did it affect the yield or infectivity of NWS virus particles. However, its effect on mannose incorporation into lipid-linked saccharides depended on the incubation time, the virus strain, and the cell line. Thus, high concentrations of dMM showed some inhibition of mannose incorporation into lipid-linked oligosaccharides with the NWS strain in a 3-h incubation, but no inhibition was observed after 48 h of incubation. On the other hand, the PR8 strain was much more sensitive to dMM inhibition, and mannose incorporation into lipid-linked oligosaccharides was strongly inhibited when the virus was raised in chick embryo cells, but less inhibition was observed when this virus was grown in MDCK cells. Nevertheless, in these cases also, the major oligosaccharide structure in the glycoproteins was the Man9GlcNAc2 species. |
Author | McDowell, William Legler, Gunter Tlusty, Annette Elbein, Alan D. Schwarz, Ralph |
Author_xml | – sequence: 1 givenname: Alan D. surname: Elbein fullname: Elbein, Alan D. organization: Department of Biochemistry, University of Texas Health Science Center, San Antonio, Texas 78284 U.S.A – sequence: 2 givenname: Gunter surname: Legler fullname: Legler, Gunter organization: Institute for Biochemistry, University of Cologne, Zulpicher Strasse 47, D-5000, Koln 1, West Germany – sequence: 3 givenname: Annette surname: Tlusty fullname: Tlusty, Annette organization: Institute for Biochemistry, University of Cologne, Zulpicher Strasse 47, D-5000, Koln 1, West Germany – sequence: 4 givenname: William surname: McDowell fullname: McDowell, William organization: Institute for Virology, Justus-Liebig Universität, Giessen, FRG – sequence: 5 givenname: Ralph surname: Schwarz fullname: Schwarz, Ralph organization: Institute for Virology, Justus-Liebig Universität, Giessen, FRG |
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Keywords | Virus Cell culture Molecular structure Reaction mechanism Orthomyxoviridae Molecular interaction Glycoproteins Inhibition Influenzavirus Biological activity Processing |
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Snippet | Deoxymannojirimycin (dMM) was tested as an inhibitor of the processing of the oligosaccharide portion of viral and cellular N-linked glycoproteins. The NWS... |
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SubjectTerms | 1-Deoxynojirimycin Alkaloids - pharmacology Analytical, structural and metabolic biochemistry Antiviral Agents - pharmacology Biological and medical sciences Chemical Phenomena Chemistry Fundamental and applied biological sciences. Psychology Glucosamine - analogs & derivatives Glucosamine - pharmacology Glycoproteins Glycoproteins - metabolism Indolizines Leucine - metabolism Lipids - analysis Mannose - metabolism Oligosaccharides - analysis Orthomyxoviridae - drug effects Orthomyxoviridae - metabolism Protein Processing, Post-Translational - drug effects Proteins Viral Proteins - biosynthesis Viral Proteins - metabolism |
Title | The effect of deoxymannojirimycin on the processing of the influenza viral glycoproteins |
URI | https://dx.doi.org/10.1016/0003-9861(84)90232-7 https://www.ncbi.nlm.nih.gov/pubmed/6240228 https://search.proquest.com/docview/75843398 |
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