Antigenic properties of recombinant glycosylated and nonglycosylatedPneumocystis carinii glycoprotein A polypeptides expressed in baculovirus-infected insect cells
| Autor: | Patricia J. Simpson-Haidaris, Francis Gigliotti, Constantine G. Haidaris, D. J. Fisher |
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| Rok vydání: | 1998 |
| Předmět: |
Male
Antigenicity Antigens Fungal Glycosylation Recombinant Fusion Proteins Blotting Western Genetic Vectors Bioengineering Spodoptera Biology Applied Microbiology and Biotechnology Biochemistry Epitope Cell Line law.invention Fungal Proteins Epitopes chemistry.chemical_compound Antigen law parasitic diseases Animals Lung Molecular Biology chemistry.chemical_classification Membrane Glycoproteins Pneumocystis Tunicamycin Ferrets Antibodies Monoclonal Virology respiratory tract diseases chemistry Pneumocystis carinii Cell culture Recombinant DNA Glycoprotein Baculoviridae Biotechnology |
| Zdroj: | Molecular Biotechnology. 9:91-97 |
| ISSN: | 1559-0305 1073-6085 |
| DOI: | 10.1007/bf02760811 |
| Popis: | Since a continuous culture system is not yet available for the opportunistic fungal pathogen Pneumocystis carinii, obtaining suitable amounts of purified P. carinii antigens free of mammalian-host lung contaminants is difficult. Hence, production of recombinant antigen possessing epitopes found in native P. carinii antigens is critical for immunological studies. We utilized the baculovirus expression vector system (BEVS) in insect cells to determine whether B-cell epitopes present in the protein core of a native P. carinii surface glycoprotein were conserved in the recombinant polypeptide, and to investigate its glycosylation by insect cells. B-cell epitopes were retained, but the insect cells appeared to hyperglycosylate the recombinant protein. |
| Databáze: | OpenAIRE |
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