Conformational and linear epitopes on virus-like particles of human papillomavirus type 33 identified by monoclonal antibodies to the minor capsid protein L2
| Autor: | Jan M. M. Walboomers, Christoph Volpers, Rolf E. Streeck, Martin Sapp, Peter J.F. Snijders |
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| Rok vydání: | 1995 |
| Předmět: |
medicine.drug_class
viruses Molecular Sequence Data Biology Monoclonal antibody Epitope Epitopes Mice Capsid Antigen Antibody Specificity Virology medicine Animals Humans Amino Acid Sequence Antigens Viral Papillomaviridae chemistry.chemical_classification Mice Inbred BALB C Antibodies Monoclonal virus diseases Oncogene Proteins Viral Uterine Cervical Dysplasia Fusion protein Molecular biology Amino acid chemistry DNA Viral biology.protein Capsid Proteins Antibody Epitope Mapping Conformational epitope |
| Zdroj: | Journal of General Virology. 76:2661-2667 |
| ISSN: | 1465-2099 0022-1317 |
| Popis: | The organization of epitopes on the minor capsid protein L2 of human papillomavirus (HPV) type 33 has been analysed using three monoclonal antibodies (MAbs) generated against a large fragment of the L2 protein (amino acids 82-259) expressed as a glutathione S-transferase fusion protein. The topology of the L2 epitopes has been investigated with respect to the structure of HPV-33 virus-like particles (VLPs). Two of the MAbs reacted with linear epitopes which were mapped to amino acids 153-160 and 163-170, respectively. These epitopes were accessible in denatured but not in native VLPs consisting of L1 and L2, suggesting an internal location. The third antibody was unable to detect denatured L2 protein but reacted with native VLPs. This is the first demonstration of an apparent conformational epitope of the HPV L2 protein. A model for the putative orientation of L2 in the papillomavirus capsid is deduced from the location of these and other antigenic sites. |
| Databáze: | OpenAIRE |
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