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Biomedical subjects

G Bodo

Publications and source records attributed to G Bodo.

At least 19 recordsLinked to original sources
PubMed1992

The effect of metal binding on the structure of annexin V and implications for membrane binding.

The structure of annexin V, crystallised in the presence of two calcium or barium ions for each protein molecule, was solved by molecular replacement to 0.24 nm resolution. The two metal ions are found in domains I and IV, i.e. on the same side of the channel that lies in the centre of the molecule. The structures of the barium and calcium form are extremely close, the only differences localised in the metal-binding sites that lie on the surface of the molecule. The occupancies of the metal ions, however, are lower for barium than for calcium, expressing the lower affinity of the protein for the former. The packing of the annexin molecules in the crystal asymmetric unit may represent a model for the calcium driven association of membrane-bound annexins that leads to membrane fusion.

Annexin A5↗
PubMed1989

Crystallization and preliminary X-ray studies of human vascular anticoagulant protein.

The human vascular anticoagulant protein, a 36 kDa member of the annexin/lipocortin family, has been crystallized using polyethylene glycol 20,000, by the vapour diffusion method. The crystals are monoclinic, space group P2(1), cell dimensions a = 83.9 A, b = 80.9 A, c = 71.4 A, beta = 108.7 degrees and diffract to at least 2.2 A resolution.

Annexins↗
PubMed1989

Vascular anticoagulant beta: a novel human Ca2+/phospholipid binding protein that inhibits coagulation and phospholipase A2 activity. Its molecular cloning, expression and comparison with VAC-alpha.

A cDNA was cloned coding for a new member of the human Ca2+-modulated phospholipid-binding protein family termed annexins. Due to its 56% identity to the human vascular anticoagulant (VAC) the new protein is named VAC-beta, renaming the previous VAC as VAC-alpha. Northern analysis detects one hybridizing mRNA species of 2.2 kb in human placenta. Genomic Southern blot analysis shows a VAC-beta gene of comparable complexity to the VAC-alpha gene. The cDNA was expressed in Escherichia coli and the recombinant protein purified to homogeneity. Antiserum raised against VAC-beta weakly cross-reacts with VAC-alpha. The properties of VAC-beta as an anticoagulant and as an inhibitor of phospholipase A2 activity were analyzed and compared to those of VAC-alpha.

Amino Acid Sequence↗
PubMed1988

Cloning and expression of cDNA for human vascular anticoagulant, a Ca2+-dependent phospholipid-binding protein.

Based on sequence information from tryptic peptides an almost full-size cDNA coding for the human vascular anticoagulant was isolated from a placental cDNA library and sequenced. The coding region was cloned into an Escherichia coli expression vector and the protein expressed at high levels. The recombinant protein was purified and found to be indistinguishable from its natural counterpart in several biological assays.

Amino Acid Sequence↗
PubMed1985

Interferon therapy for bronchial papillomatosis controlled by papillomavirus-DNA hybridization.

In biopsy specimens from a patient with tracheal and bronchial papillomatosis, human papillomavirus (HPV) type 11 DNA was identified. Treatment with leukocyte interferon was initiated, and the results of therapy was monitored by molecular hybridization of biopsy specimens with phosphorus 32-labeled HPV type 11 DNA after interferon application. There was no improvement of the clinical course, although two of five biopsy specimens showed a considerable reduction in the amount of HPV type 11. We discuss the reasons for the insufficient effect of therapy and propose molecular hybridization as an additional method for therapy control in viral diseases.

Bronchial Neoplasms↗
PubMed1985

Sensitivity of ortho- and paramyxovirus replication to human interferon alpha.

Replication of the influenza virus strains Influenza Ao/WSN (H0N1), fowl plague (Hav1N1) and B-Lee/40 (ATCC) and the paramyxovirus, New Castle disease virus (Victoria) are highly sensitive to human interferon type alpha in Madin Darby bovine kidney cells. Pretreatment of cells with human interferon type alpha resulted in protection of the cells against viral cytopathic effect. The inhibition of the orthomyxovirus strains used in this study and New Castle disease virus replication is mediated by an inhibition of viral protein synthesis. Residual WSN virus particles released from interferon treated cells showed the same structural protein pattern as virus particles isolated from control cells. Glycosylation of the viral structural components appeared to be unaffected by interferon.

Animals↗
PubMed1982

Production of monoclonal antibodies to human IFN-alpha and their use for analysis of the antigenic composition of various natural interferons.

We have established three hybridoma cell lines (designated EBI-1, -2, and -3) secreting immunoglobulin G (IgG) antibodies specific for human alpha-interferon (HuIFN-alpha) by fusing P3X63Ag8.6.5.3 myeloma cells with spleen cells of mice immunized with human "lymphoblastoid" (NC-37) interferon (IFN). The antibodies were used to study the antigenic diversity of a number of IFNs derived from blood leukocytes and lymphoid cell lines. When incubated with 10 U of IFN, EBI-1 antibodies completely neutralized the antiviral activity of HuIFN-alpha rA produced in E coli as well as of IFN produced spontaneously in several lymphoblastoid cell lines. In contrast, only 60-70% of alpha-interferon (IFN-alpha) induced in leukocytes, lymphoma, or lymphoblastoid cell lines by Sendai virus or poly (I):(C) could be neutralized by the antibody; furthermore, IFN-alpha produced spontaneously in bromodeoxyuridine-treated lymphoma cells was also only partially neutralized. EBI-2 and EBI-3 antibodies were tested against a smaller set of samples and found to react similarly. Our results indicate that human IFN-alpha subtypes can be grouped into at least two antigenically distinguishable subsets, one of which being represented by IFN-alpha A, and that these subsets can be expressed differently under different conditions in a given cell type.

Animals↗
PubMed1982

Interferon inhibits establishment of fibroblast infection with avian retroviruses.

Pretreatment of chick embryo fibroblasts (CEF) with low doses of homologous interferon (16 u/ml) drastically inhibits cell transformation by, and replication of Rous sarcoma virus (RSV). Treatment of chick cells with 16 u/ml of interferon before de novo infection with a transformation defective (td) mutant-RSV, also resulted in a reduction of extracellular virus particles. This was determined by infectivity titrations, virus associated reverse transcriptase (RT) activity and measurement of metabolically radioactively labelled virus particles. The viral proteins pr 180, pr 76, p 27, p 19 and p 12 were still synthesized in interferon-treated cells in an unaltered form, although at slightly reduced levels. No difference in the pattern of structural proteins could be detected between virus particles harvested from cells treated with interferon and from control cells. In contrast to de novo infected cells, concentrations of interferon as high as 200 u/ml had no influence on the reversible transformation of cloned fibroblasts infected with a temperature sensitive mutant of RSV. In addition, fibroblasts infected with td-SR-RSV-D before addition of interferon showed only a marginal effect on formation of infectious virus even after treatment with 200-500 u/ml of interferon. This was not caused by interferon-resistance of the td-SR-RSV-D infected cells since viral protein synthesis by superinfecting Vesicular stomatitis virus (VSV) was as sensitive to interferon as in cells not preinfected with retrovirus. Our results support the notion that exogenous infection of fibroblasts with avian retrovirus is inhibited by interferon during an early phase of the replication cycle.

Animals↗
PubMed1982

[Interferon/Controlled study in 3-year survival of patients with osteosarcoma (author's transl)].

In eight patients with osteosarcoma we conducted a controlled tolerance study with human lymphoblast interferon. Interferon was applied for 12 months and the control period after stopping interferon has lasted 12-42 months up to now. 4 out of 8 patients who received interferon did not show any adverse reaction concerning clinical and laboratory tests during the course of a 1-year application and during the follow-up period, resp. Only reversible thrombopenias and an increase in the alpha 2-globulins fraction were observed in the interferon and in the control group, resp. All of the 8 patients have up to now survived tumor-free.

Adolescent↗
PubMed1980

Enhancement of NK, but not K cell activity by different interferons.

Two different interferons derived either from a human lymphoblastoid cell line (Namalva) or from human fibroblasts were tested for their ability to modulate natural killer (NK) or killer (K) cell activity. The lymphoblastoid interferon was purified by ion-exchange chromatography on SP-Sephadex C-25 and gel filtration on Sephadex G-100, the fibroblast-derived interferon was purified by chromatography on porous glass beads. Evidence is presented that NK cell activity is enhanced by both of these interferons being active to a similar extent. When tissue culture cells are employed as targets for measurement of K cell activity, the augmentation of cytotoxicity by interferons has to be attributed to the inherent NK cell activity. With the use of the autologous hapten-coated target cells and of affinity chromatography purified antibodies, the cytotoxicity is displayed solely by K cells and this activity is not enhanced by either interferons tested.

Antibody-Dependent Cell Cytotoxicity↗
PubMed1978

RNA methylation in vaccinia virus-infected chick embryo fibroblasts treated with homologous interferon.

Interferon-pretreatment of vaccinia-infected chick embryo fibroblasts resulted in a greater than 50% decrease in ribose methylation of the penultimate "cap" nucleotide in virus-specific mRNA. However, in contrast to results obtained with cell-free systems, in intact infected cells there was (a) no detectable reduction in methylation of the 5'-ultimate m7G of viral mRNA; (b) a virus specificity of the interferon-induced change in mRNA "CAP"-methylation seems unlikely and (c) analysis of the ribosomal and transfer RNA fractions isolated from interferon-treated and control cells revealed identical patterns of methylated nucleotides. Thus, the interferon-induced change in methylation is specific for mRNA "CAPS".

Cells, Cultured↗
PubMed1978

Impairment by interferon of mitogen-induced DNA synthesis in chick lymphocytes.

Chick interferon preparations inhibit mitogen-induced DNA synthesis of chicken peripheral and spleen lymphocytes. Mock interferon preparations showed also some inhibition of mitogen-induced DNA synthesis. The degree of inhibition is concentration dependent but varies also with the relative time of addition of homologous interferon and mitogen. Addition of the interferon preparations 6 h before mitogen resulted in a stronger inhibition of DNA synthesis than if the interferon preparations and mitogen were added at the same time. The interferon preparations seem to affect the metabolism of lymphocytes in a mroe general way and not only the trigger mechanism of the mitogenic response since addition of interferon even 24 h after the mitogen inhibits the induced DNA synthesis.

Animals↗