8 results on '"Foa-Tomasi, L."'
Search Results
2. Human herpesvirus 6 strain groups: a nomenclature
- Author
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Ablashi, D., Agut, H., Berneman, Zwi Nisan, Campadelli-Fiume, G., Carrigan, D., Checcerini-Nelli, L., Chandran, B., Chou, S., Collandre, H., Dambaugh, T., Dewhurst, S., DiLuca, D., Foa-Tomasi, L., Fleckenstein, B., Frenkel, N., Gallo, R., Gompels, U., Hall, C., Jones, M., Lawrence, G., Martin, Manuella, Montagnier, L., Neipel, F., Nicholas, J., Pellett, P., Razzaque, A., Torrelli, G., Thompson, B., Salahuddin, S., Wyatt, L., and Yamanishi, K.
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- 1993
3. Establishment and characterization of a persistent infection of MDBK cells with herpes simplex virus
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Mannini-Palenzona, A., Bartoletti, A. M., Foa -Tomasi, L., Baserga, M., Tognon, M., and Roberto MANSERVIGI
4. Selection of a monoclonal antibody specific for variant B human herpesvirus 6-infected mononuclear cells
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Elisa Avitabile, Gabriella Campadelli-Fiume, Laura Foà-Tomasi, Foa-tomasi L., Avitabile E., and Campadelli-fiume G.
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medicine.drug_class ,viruses ,Human herpesvirus 6 ,Herpesvirus 6, Human ,Spleen ,Antibodies, Viral ,Monoclonal antibody ,Immunofluorescence ,Peripheral blood mononuclear cell ,Mice ,Affinity chromatography ,Antibody Specificity ,Virology ,medicine ,Animals ,Humans ,Hybridomas ,Variant B human herpesvirus 6 ,biology ,medicine.diagnostic_test ,Antibodies, Monoclonal ,Proteins ,virus diseases ,biology.organism_classification ,Molecular biology ,Molecular Weight ,medicine.anatomical_structure ,Monoclonal antibody derivation ,Monoclonal ,Leukocytes, Mononuclear ,biology.protein ,Antibody - Abstract
A monoclonal antibody, designated as MAb 6E2, specific for human herpesvirus 6 variant B (HHV-6B) was derived from the spleen of a mouse immunized with lysates of HHV-6B(Z29) cord blood mononuclear cells. MAb 6E2 reacts by immunofluorescence with all the HHV-6B strains tested (Z29, CV, Hashimoto and SF) and fails to react with variant A prototypes, GS and U1102. The immunofluorescence staining was punctate and localized to the cytoplasm. The protein reacting with MAb 6E2 was identified as protein 48 000 in apparent Mr value by immunoaffinity chromatography of lysates of HHV-6B-infected mononuclear cells. © 1995.
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- 1995
5. Herpes simplex virus (HSV) glycoprotein h is partially processed in a cell line that expresses the glycoprotein and fully processed in cells infected with deletion or is mutants in the known hsv glycoproteins
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Franca Serafini-Cessij, Roberto Manservigi, Rita Gualandri, Renato Brandimarti, Elisa Avitabile, Laura Foà-Tomasi, Ambra Boscaro, Fabio Dall'olioj, Gabriella Campadelli Fiume, Foa-Tomasi L., Avitabile E., Boscaro A., Brandimarti R., Gualandri R., Manservigi R., Dall'olioj F., Serafini-Cessij F., and Campadelli Fiume G.
- Subjects
Animals Cell Line Chromosome Deletion Genes, Viral Mannose/metabolism *Mutation Oligosaccharides/isolation & purification Plasmids Protein Processing, Post-Translational Recombinant Proteins/biosynthesis/isolation & purification Recombination, Genetic Restriction Mapping Simplexvirus/*genetics Vero Cells Viral Envelope Proteins/biosynthesis/*genetics/isolation & purification ,Genes, Viral ,Viral protein ,Restriction Mapping ,Mutant ,Oligosaccharides ,Biology ,medicine.disease_cause ,Virus ,Cell Line ,symbols.namesake ,Viral Envelope Proteins ,Virology ,medicine ,Animals ,Simplexvirus ,Vero Cells ,Recombination, Genetic ,chemistry.chemical_classification ,Golgi apparatus ,Herpesvirus glycoprotein B ,Molecular biology ,Recombinant Proteins ,Herpes simplex virus ,chemistry ,Cell culture ,Mutation ,symbols ,Chromosome Deletion ,Glycoprotein ,Mannose ,Protein Processing, Post-Translational ,Plasmids - Abstract
Cell lines that constitutively express herpes simplex virus 1 (HSV-1) glycoprotein H (gH-1 ) failed to synthesize the mature form of gH and accumulated a precursor-like form of the glycoprotein, which was retained intracellularly, most likely in RER. Fine-structure analysis of the oligosaccharides present in recombinant gH revealed oligosaccharides processed by RER enzymes; sialylated complex-type and biantennary oligosaccharides, which are assembled in the trans-Golgi, were absent. A small fraction had the characteristics of oligosaccharides processed by the early mannosidases of the Golgi. These findings suggest that a defect in the transport out of RER to the Golgi may account for the intracellular retention of the immature form of gH in cells that express the glycoprotein constitutively. Upon superinfection of cells expressing gH-1 with HSV-2, recombinant gH-1 underwent maturation, indicating that a viral function is required to attain full processing of gH. The known HSV glycoproteins do not appear to carry out this function, since in cells infected with deletion mutants in gD, gG, gE, and gE-gl, with a spontaneous gC- mutant, or with a temperature-sensitive mutant in gB, maturation of gH occurred independently of the presence or of the maturation of the single glycoproteins tested. The present findings together with previous observations on HSV, human CMV, and the EBV homologue of gH suggest that inability of gH to undergo full processing in the absence of viral protein (s) is a property of gH.
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- 1991
6. Polyvalent and monoclonal antibodies identify major immunogenic proteins specific for human herpesvirus 7-infected cells and have weak cross-reactivity with human herpesvirus 6
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Elisa Avitabile, Gabriella Campadelli-Fiume, Laura Foà-Tomasi, Liu Ke, Foa-Tomasi L., Avitabile E., Ke L., and Campadelli-Fiume G.
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Antigenicity ,medicine.drug_class ,Herpesvirus 6, Human ,Blotting, Western ,Enzyme-Linked Immunosorbent Assay ,Herpesvirus 7, Human ,Cross Reactions ,medicine.disease_cause ,Monoclonal antibody ,Antibodies, Viral ,Cross-reactivity ,Herpesviridae ,Virus ,Monocytes ,Mice ,Viral Proteins ,Immune system ,Virology ,medicine ,Animals ,Humans ,Antigens, Viral ,Cells, Cultured ,chemistry.chemical_classification ,biology ,Antibodies, Monoclonal ,biology.organism_classification ,Fetal Blood ,Molecular biology ,Animals *Antibodies, Monoclonal *Antibodies, Viral Antigens, Viral/analysis/*immunology/isolation & purification Blotting, Western/methods Cells, Cultured Cross Reactions Electrophoresis, Polyacrylamide Gel Enzyme-Linked Immunosorbent Assay/methods Female Fetal Blood Herpesvirus 6, Human/*immunology Herpesvirus 7, Human/*immunology Humans Mice/immunology Monocytes Rabbits/immunology Viral Proteins/analysis/*immunology/isolation & purification ,chemistry ,Human herpesvirus 6 ,Electrophoresis, Polyacrylamide Gel ,Female ,Rabbits ,Glycoprotein - Abstract
Hyperimmune rabbit and mouse sera raised to human herpesvirus 7 (HHV-7)-infected cells and an immune human serum identified 20 [35S]methionine-[35S]cysteine-labelled proteins specific for HHV-7-infected cord blood mononuclear cells, ranging in apparent M(r) from 136K to 30K. The major proteins had apparent M(r) values of 121K, 100K, 87K, 85K, 60K, 51K, 46K, 42K, 40K and 36K. The human serum also identified seven [3H]glucosamine-labelled glycoproteins, with apparent M(r) values of 100K, 89K, 82K, 67K, 63K, 53K and 41K. Four monoclonal antibodies (MAbs) specific for HHV7-infected cells were derived. Two reacted with a family of five antigenically related polypeptides (87K, 85K, 70K, 61K and 57K in apparent M(r)), designated as the p85 complex. Two reacted with 121K and 51K M(r) proteins designated as p121 and p51, respectively. Human sera react with high frequency with the p85 complex and to a lesser extent with p121; hence these two proteins appear to be immunodominant for both humans and laboratory animals. The hyperimmune mouse serum and some of the MAbs showed some cross-reactivity with HHV-6A(U1102)- and 6B(Z29)-infected cells. The implications of cross-reactivity with respect to the human immune response to HHV-6 and -7 infections and prevalence analyses are discussed.
- Published
- 1994
7. Individual herpes simplex virus 1 glycoproteins display characteristic rates of maturation from precursor to mature form both in infected cells and in cells that constitutively express the glycoproteins
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Elisa Avitabile, Maria Teresa Lombardo, Franca Serafini-Cessi, Laura Foà-Tomasi, Gabriella Campadelli-Fiume, Campadelli-Fiume G., Lombardo M.T., Foa-Tomasi L., Avitabile E., and Serafini-Cessi F.
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Phosphonoacetic Acid ,Cancer Research ,Virion morphogenesis ,Immunoprecipitation ,Morphogenesis ,Kidney ,medicine.disease_cause ,Maturation rate ,Herpesviridae ,Virus ,Cell Line ,Viral Envelope Proteins ,Cricetinae ,Virology ,Alphaherpesvirinae ,Tumor Cells, Cultured ,medicine ,Animals ,Humans ,Simplexvirus ,Herpes simplex viru ,Protein Precursors ,Laryngeal Neoplasms ,Glycoproteins ,chemistry.chemical_classification ,Mesocricetus ,biology ,Fibroblasts ,biology.organism_classification ,Molecular biology ,Herpesvirus glycoprotein B ,Infectious Diseases ,Herpes simplex virus ,chemistry ,Carcinoma, Squamous Cell ,Glycoprotein ,Protein Processing, Post-Translational - Abstract
Pulse-chase experiments in conjunction with quantitative immunoprecipitation have been used to study the time-course of conversion from precursor to mature form of herpes simplex virus 1 glycoproteins C, D and B (gC, gD, and gB). The experimental systems employed were two infected cell lines and cells that constitutively express gD or gB. The relative rates of conversion among the glycoproteins did not vary in the systems used; the rate of maturation of gC was about two-fold higher than that of gD which, in turn, was about one and a half-fold higher than that of gB. Treatment with phosphonoacetate which inhibits viral DNA synthesis and hence virion morphogenesis induced a striking increase in the time course of conversion of immature gC, gD, and gB to fully glycosylated forms when measured late in the infection. The model of HSV glycoproteins maturation as integral components of the virion envelope is discussed. © 1988.
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- 1988
8. Glycoprotein D of herpes simplex virus encodes a domain which precludes penetration of cells expressing the glycoprotein by superinfecting herpes simplex virus
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Bernard Roizman, Laura Foà-Tomasi, Gabriella Campadelli-Fiume, Renato Brandimarti, Sun Qi, Elisa Avitabile, Campadelli-Fiume G., Qi S., Avitabile E., Foa-Tomasi L., Brandimarti R., and Roizman B.
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Genes, Viral ,viruses ,Immunology ,Restriction Mapping ,Viral Plaque Assay ,Biology ,medicine.disease_cause ,Transfection ,Microbiology ,Epitope ,Virus ,Cell Line ,Restriction map ,Viral Envelope Proteins ,Viral entry ,Virology ,medicine ,Baby hamster kidney cell ,Animals ,Simplexvirus ,Virus quantification ,Antibodies, Monoclonal ,Molecular biology ,Herpes simplex virus ,Animals Antibodies, Monoclonal Cell Line DNA, Viral/genetics Genes, Viral Mutation Phenotype Restriction Mapping Simplexvirus/*genetics/isolation & purification Transfection Viral Envelope Proteins/biosynthesis/*genetics/isolation & purification Viral Plaque Assay ,Phenotype ,Insect Science ,DNA, Viral ,Mutation ,Research Article - Abstract
Earlier studies have shown that herpes simplex viruses adsorb to but do not penetrate permissive baby hamster kidney clonal cell lines designated the BJ series and constitutively expressing the herpes simplex virus 1 (HSV-1) glycoprotein D (gD). To investigate the mechanism of the restriction, the following steps were done. First, wild-type HSV-1 strain F [HSV-1(F)] virus was passaged blindly serially on clonal line BJ-1 and mutant viruses [HSV-1(F)U] capable of penetration were selected. The DNA fragment capable of transferring the capacity to infect BJ cells by marker transfer contains the gD gene. The mutant gD, designated gDU, differed from wild-type gD only in the substitution of Leu-25 by proline. gDU reacted with monoclonal antibodies which neutralize virus and whose epitopes encompass known functional domains involved in virus entry into cells. It did not react with the monoclonal antibody AP7 previously shown to react with an epitope which includes Leu-25. Second, cell lines expressing gDU constitutively were constructed and cloned. Unlike the clonal cell lines constitutively expressing gD (e.g., the BJ cell line), those expressing gDU were infectable by both HSV-1(F) and HSV-1(F)U. Lastly, exposure of BJ cells to monoclonal antibody AP7 rendered the cells capable of being infected with HSV-1(F). The results indicate that (i) gD expresses a specific function, determined by sequences at or around Leu-25, which blocks entry of virus into cells synthesizing gD, (ii) the gD which blocks penetration by superinfecting virus is located in the plasma membrane, (iii) the target of the restriction to penetration is the identical domain of the gD molecule contained in the envelope of the superinfecting virus, and (iv) the molecular basis of the restriction does not involve competition for a host protein involved in entry, as was previously thought.
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