Conformational changes between human immunodeficiency virus type 1 nucleocapsid protein NCp7 and its precursor NCp15 as detected by anti-NCp7 monoclonal antibodies
| Autor: | Richard Benarous, Thierry Delaunay, Jean-Luc Darlix, Valérie Tanchou, Monique Bodéus, Bernard P. Roques |
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| Rok vydání: | 1995 |
| Předmět: |
Protein Conformation
medicine.drug_class Molecular Sequence Data Human immunodeficiency virus (HIV) Gene Products gag Proviral dna Biosensing Techniques HIV Antibodies Biology medicine.disease_cause Monoclonal antibody Binding Competitive gag Gene Products Human Immunodeficiency Virus Epitope Antigen-Antibody Reactions Mice Viral Proteins Capsid Virology medicine Animals Humans Amino Acid Sequence Protein Precursors Zinc finger Mice Inbred BALB C Antibodies Monoclonal Zinc Fingers Nucleocapsid Proteins Molecular biology Rats HIV-1 RNA Transfer Lys Capsid Proteins Female Primer (molecular biology) Peptides Epitope Mapping |
| Zdroj: | Journal of General Virology. 76:2457-2466 |
| ISSN: | 1465-2099 0022-1317 |
| DOI: | 10.1099/0022-1317-76-10-2457 |
| Popis: | The nucleocapsid protein NCp15 of human immunodeficiency virus type 1 (HIV-1) is a small basic protein with two zinc fingers. It is required for virion morphogenesis and synthesis of proviral DNA. As the first step in our study of the structural domains involved in the various functions of this protein, 18 monoclonal antibodies (MAbs) were isolated. The epitopes of NCp7 recognized by the MAbs were mapped using synthetic peptides representing overlapping sequences and truncated forms of NCp7. These anti-NCp7 MAbs were investigated by ELISA and real-time biospecific interaction analysis (BIAcore). Five classes of anti-NCp7 MAbs were characterized. Three classes (14 MAbs) were directed against continuous epitopes, one in the N-terminal part, another next to the second zinc finger and the third in the C-terminal part of the protein. Two other classes comprised four MAbs reacting only with the entire NCp7 and not with any of the small overlapping peptides used, suggesting that these MAbs were directed against conformational epitopes. The anti-NCp7 MAbs directed against linear epitopes were able to react efficiently with both NCp7 and NCp15, the NCp7 precursor, whereas the anti-NCp7 MAbs directed against conformational epitopes did not react with NCp15. Interestingly, most of the anti-NCp7 MAbs directed against conformational epitopes were capable of inhibiting the tight interaction between NCp7 and the HIV-1 replication primer tRNA(Lys,3). In contrast, most of the MAbs directed against linear epitopes did not inhibit this interaction. |
| Databáze: | OpenAIRE |
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