Characterization of the antigenic domains of the major core protein (p26) of equine infectious anemia virus.
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.
Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pennsylvania 15261.
Y H
YH
Chong
S L
SL
Payne
C J
CJ
Issel
R C
RC
Montelaro
K E
KE
Rushlow
D000818:Animals; D015153:Blotting, Western; D004279:DNA, Viral / Q000235:genetics; D000939:Epitopes / Q000032:analysis*; D015497:HIV-1 / Q000276:immunology; D006736:Horses; D007106:Immune Sera; D004860:Infectious Anemia Virus, Equine / Q000235:genetics / Q000276:immunology*; D011993:Recombinant Fusion Proteins / Q000276:immunology; D015183:Restriction Mapping; D014758:Viral Core Proteins / Q000235:genetics / Q000276:immunology*
D004279:DNA, Viral; D000939:Epitopes; D007106:Immune Sera; D011993:Recombinant Fusion Proteins; D014758:Viral Core Proteins