Characterization of the antigenic domains of the major core protein (p26) of equine infectious anemia virus
| Autor: | Keith E. Rushlow, Ronald C. Montelaro, Charles J. Issel, Susan Payne, Young-Hae Chong |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Antigenicity
Recombinant Fusion Proteins viruses animal diseases Blotting Western Restriction Mapping Immunology Microbiology Virus Epitope Equine infectious anemia Epitopes Virology Animals Horses biology Immune Sera Viral Core Proteins Immunogenicity Lentivirus Infections biology.organism_classification Fusion protein Insect Science DNA Viral Humoral immunity HIV-1 Research Article Infectious Anemia Virus Equine |
| Zdroj: | Journal of Virology. 65:1007-1012 |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.65.2.1007-1012.1991 |
| Popis: | A panel of recombinant trpLE-gag fusion proteins and synthetic peptides was used in Western immunoblot and enzyme-linked immunosorbent assays to identify segments of the major core protein (p26) of equine infectious anemia virus that are antigenic in horses during experimental and natural infections with the virus. The predominant humoral immune response was directed toward a highly immunogenic domain composed of 83 amino acids from the carboxy terminus of p26. The observed immunogenicity of p26 resembled that reported for p24 of human immunodeficiency virus type 1, suggesting the conservation of structural motifs in the lentiviral core proteins which are responsible for their observed immunogenicity during persistent lentivirus infections. |
| Databáze: | OpenAIRE |
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