Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0271276 (Hudson)
 1,066 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Recent studies using radiolabeled rotavirus lysates have demonstrated a 35-kilodalton viral protein that binds specifically to the surface of MA104 cells (N. Fukuhara, O. Yoshie, S. Kitakoa, and T. Konno, J. Virol. 62:2209-2218, 1988; M. Sabara, J. Gilchrist, G.R. Hudson, and L.A. Babiuk, J. Virol. 53:58-66, 1985). The binding protein was identified as vp7, an outer capsid glycoprotein and the product of rotavirus gene 9. These studies concluded that vp7 mediated viral attachment to MA104 cells and that the binding of a soluble viral protein to a cell monolayer mirrored the attachment of infectious rotavirus to permissive tissue culture cells. In the process of determining which viral protein adheres to the in vivo target cell in rotavirus infection, the mammalian enterocyte, we found that a similar 35-kilodalton rhesus rotavirus (RRV) protein bound to both MA104 cells and murine enterocytes. However, further analysis of this protein by immunoprecipitation, inhibition of glycosylation, and partial proteolysis showed that it was not the RRV gene 9 product, vp7, but the gene 8 product, NS35. Similar results were obtained by using porcine rotavirus (OSU) and bovine rotavirus (NCDV) strains. Binding studies using the in vitro-expressed products of RRV genes 8 and 9 confirmed these results. Since double-shelled virions inhibited the binding of NS35 to cells, we looked for the presence of this protein in preparations of purified virus. Examination of density gradient-purified virus preparations revealed biochemical and immunological evidence that NS35 copurifies in small amounts with double-shelled virions. Thus, these studies clearly demonstrated that when rotavirus proteins are prepared in a soluble form from infected cells, NS35, and not vp7, binds to the surfaces of MA104 cells and murine enterocytes. The observations do not confirm previous experimental results which supported the hypothesis that vp7 was the viral attachment protein. They are consistent with but do not prove the hypothesis that NS35 functions as the rotavirus attachment protein.
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PMID:NS35 and not vp7 is the soluble rotavirus protein which binds to target cells. 215 20

Previous experiments demonstrated that an antigenic site responsible for virus neutralization and cell attachment was located on a 14,000-molecular-weight fragment of the major bovine rotavirus (BRV) glycoprotein (M. Sabara, J. E. Gilchrist, G. R. Hudson, and L. A. Babiuk, J. Virol. 53:58-66, 1985). However, it was necessary to investigate whether this fragment also had the ability to induce the production of neutralizing antibodies. Upon immunization of mice, the bovine serum albumin-conjugated 14,000-molecular-weight fragment, the unconjugated 14,000-molecular-weight fragment, and the native glycoprotein all induced a similar neutralizing antibody response, albeit to a lesser extent than did the infectious, whole virus. In addition, immuno-blot enzyme-linked immunosorbent assay analysis of the reactivity of anti-peptide serum versus anti-glycoprotein serum with the glycoprotein was very comparable. These results suggest that the 14,000-molecular-weight fragment may represent not only a biologically active region but also an immunodominant area of the glycoprotein.
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PMID:Immunogenicity of a bovine rotavirus glycoprotein fragment. 241 12

A 2.5-kilobase cDNA clone (AF7), encoding 785 amino acids, was isolated from a rat liver cDNA library constructed in the expression vector lambda gt11. M13 vector sequence analysis yielded a deduced protein primary structure that was 89% homologous to the prototype alpha 1-inhibitor III (alpha 1I3) sequence presented in the preceding paper by Braciak et al. (Braciak, T. A., Northemann, W., Hudson, G. O., Shields, B. R., Gehring, M. R., and Fey, G. H. (1988) J. Biol. Chem. 263, 3999-4012) with regard to exact matches and 92% homologous when considering chemically conserved residues. The clone also possessed 100% homology to the putative bait region of a variant clone (pRLA1I3/27J) of alpha 1I3. Such sequence data demonstrates that the AF7 clone corresponds to a member of the family of variant alpha 1I3 mRNAs. Furthermore, this report presents the entire mRNA sequence corresponding to the 3'-half of alpha 1I3 variant 27J. We have utilized AF7 cDNA to study the expression of alpha 1I3 messenger RNA encoding this liver-specific glycoprotein under conditions known to alter hepatic gene expression. Our data reveal that alpha 1I3 mRNA expression is not only regulated during the acute-phase response but is also modulated in response to a variety of changing physiological conditions, most notably liver development. Steady state levels of mRNA were quantified using Northern blot techniques and laser densitometry. During acute phase response initiated by turpentine injection, the relative abundance of alpha 1I3 mRNA decreased 4-5-fold over a period of 24 h. Following partial hepatectomy, the regenerating liver expressed six-fold less alpha 1I3 mRNA than untreated liver after 24 h. This reduced level was maintained over a 2-day period. We have also demonstrated that alpha 1I3 mRNA expression is developmentally regulated. Fetal rat liver did not contain detectable concentrations of rat alpha 1I3 mRNA even as late as 4 days prior to birth. However, trace amounts were observed from birth until approximately 20 days of age when alpha 1I3 mRNA levels increased 10-fold to maximal adult quantities over the following 2 or 3 weeks. During the course of pregnancy, alpha 1I3 mRNA remained essentially constant until approximately 4 days prior to birth when a precipitous decline to 40% of the original level was noted. Subsequently, normal values were gradually restored over a 30-day postpartum period.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Characterization and hepatic expression of rat alpha 1-inhibitor III mRNA. 245 89

The Epstein-Barr virus glycoprotein gp85 has been mapped to the Epstein-Barr virus DNA open reading frame BXLF2 (R. Baer, A. Bankier, M. Biggin, P. Deininger, P. Farrell, T. Gibson, G. Hatfull, G. Hudson, S. Stachwell, C. Sequin, P. Tufnell, and B. Barrell, Nature [London] 310:207-211, 1984). A gp85-specific monoclonal antibody reacts with the BXLF2 in vitro transcription-translation product. The monoclonal antibody also precipitates an 85-kilodalton protein from rodent cells transfected with the BXLF2 open reading frame DNA. In these cells, gp85 localizes to the cytoplasm and nuclear rim rather than to the plasma membrane as in lymphocytes. Northern (RNA) blot hybridization and analysis of a cDNA clone containing BXLF2 indicate that gp85 is translated from an unspliced, late, 2.5-kilobase transcript. Similarities between the predicted amino acid sequences of gp85 and herpes simplex virus gH (D. McGeoch and A. Davison, Nucleic Acids Res. 14:4281-4292, 1986) are noted.
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PMID:Identification of the Epstein-Barr virus gp85 gene. 283 72

The Epstein-Barr virus DNA open reading frame BALF4 (R. Baer, A.T. Bankier, M.D. Biggin, P.L. Deininger, P.J. Farrell, T.J. Gibson, G. Hatfull, G.S. Hudson, S.C. Stachwell, C. Sequin, P.S. Tuffnell, and B.G. Barrell, Nature [London] 310:207-211, 1984), which by nucleotide sequence comparison could encode a protein similar to herpes simplex virus gB (P.E. Pellett, M.D. Biggin, B. Barrell, and B. Roizman, J. Virol. 56:807-813, 1985), has now been shown to encode a 110-kilodalton glycoprotein. Late infectious cycle RNAs of 3.0 and 1.8 kilobases are transcribed from BALF4. Translation of these RNAs in vitro, transcription and translation of BALF4 in vitro, or metabolic labeling of cells in the presence of tunicamycin and immunoprecipitation with BALF4-specific sera results in identification of a 93-kilodalton precursor to gp110. Since N-glycosidase F only reduces the size of gp110 to 105 kilodaltons, gp110 probably has both N- and O-linked glycosylation, gp110 is an abundant glycoprotein in Epstein-Barr virus-infected cells. In infected lymphocytes and in 3T3 cells, in which the gene is expressed from a recombinant expression vector, most of the protein is cytoplasmic and perinuclear. In contrast to gB, gp110 was not detected in the infected-cell plasma membrane. In cells replicating Epstein-Barr virus, gp110 localized to the inner and outer nuclear membrane lamellae and to endoplasmic reticulum structures which sometimes contained enveloped virus. gp110 may play an important role in modifying infected intracellular membranes.
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PMID:Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB. 302 78

Two inhibitors of glycosylation, glucosamine and tunicamycin, were utilized to examine the effect of glycosylation inhibition in mouse neuroblastoma N18 cells on the degradation of membrane glycoproteins synthesized before addition of the inhibitor. Treatment with 10 mM-glucosamine resulted in inhibition of glycosylation after 2h, as measured by [3H]fucose incorporation into acid-insoluble macromolecules, and in a decreased rate of glycoprotein degradation. However, these results were difficult to interpret since glucosamine also significantly inhibited protein synthesis, which in itself could cause the alteration in glycoprotein degradation [Hudson & Johnson (1977) Biochim. Biophys. Acta 497, 567-577]. N18 cells treated with 5 microgram of tunicamycin/ml, a more specific inhibitor of glycosylation, showed a small decrease in protein synthesis relative to its effect on glycosylation, which was inhibited by 85%. Tunicamycin-treated cells also showed a marked decrease in glycoprotein degradation in experiments with intact cells. The inhibition of glycoprotein degradation by tunicamycin was shown to be independent of alterations in cyclic AMP concentration. Polyacrylamide-gel electrophoresis of isolated membranes from N18 cells, double-labelled with [14C]fucose and [3H]fucose, revealed heterogeneous turnover rates for specific plasma-membrane glycoproteins. Comparisons of polyacrylamide gels of isolated plasma membranes from [3H]fucose-labelled control cells and [14C]fucose-labelled tunicamycin-treated cells revealed that both rapidly and slowly metabolized, although not all, membrane glycoproteins became resistant to degradation after glycosylation inhibition.
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PMID:The relationship between glycosylation and glycoprotein metabolism of mouse neuroblastoma N18 cells. 747 93