| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
Department of Biochemistry
and1 Department of Veterinary Science, Louisiana State University and Louisiana Agricultural Research Experiment Station, Baton Rouge, Louisiana 70803
and2 Frederick Cancer Research Facility, National Cancer Institute, Frederick, Maryland 21701, U.S.A.
The reported serological relatedness between the major glycoproteins of human immunodeficiency virus (HIV gp120) and equine infectious anaemia virus (EIAV gp90) was examined using purified antigens in radioimmunoprecipitation (RIP), radioimmunoassay (RIA) and immunoblot assays with reference serum from acquired immunodeficiency syndrome (AIDS) patients, an anti-gp120 goat serum and EIAV-infected horse serum. To assess the contributions of glycoprotein oligosaccharide and peptide components to any observed reactivities, antigens treated with endoglycosidase F to remove carbohydrate were assayed in parallel with the intact glycoprotein. The results of the experiments indicated that the reactivity observed for each antigen was dependent on the immunoassay employed. The RIP and RIA analyses demonstrated that HIV gp120 is equally reactive with the AIDS patient serum, the goat anti-gp120 serum and the EIAV-infected horse serum, whereas the EIAV gp90 reacted only with the horse serum. In immunoblot assays, the HIV gp120 reacted with AIDS patient serum, but not with the EIAV-infected horse serum. Deglycosylation of the HIV gp120 evidently increased its reactivity with the AIDS patient serum, had no significant effect on its reactivity with the goat antiserum, and essentially abolished its reactivity with the EIAV reference serum. Thus, it appears that the serological cross-reactivity observed between HIV gp120 and sera from EIAV-infected horses can be attributed to the oligosaccharide rather than the peptide components of the viral glycoprotein. These studies also emphasize the necessity of employing several assay procedures in assessing lentivirus antigenicity.
Keywords: EIAV, HIV, glycoproteins, cross-reactivity
Present address: Hepatitis/AIDS Diagnostic Program, Abbott Laboratories, Abbott Park, Illinois 60064, U.S.A.
Received 2 February 1988;
accepted 5 April 1988.
This article has been cited by other articles:
|
|
 |
|
  S. Jin, C. J. Issel, and R. C. Montelaro Serological Method Using Recombinant S2 Protein To Differentiate Equine Infectious Anemia Virus (EIAV)-Infected and EIAV-Vaccinated Horses Clin. Vaccine Immunol., November 1, 2004; 11(6): 1120 - 1129. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. Baccam, R. J. Thompson, Y. Li, W. O. Sparks, M. Belshan, K. S. Dorman, Y. Wannemuehler, J. L. Oaks, J. L. Cornette, and S. Carpenter Subpopulations of Equine Infectious Anemia Virus Rev Coexist In Vivo and Differ in Phenotype J. Virol., November 15, 2003; 77(22): 12122 - 12131. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. M. Lonning, W. Zhang, and T. C. McGuire Gag Protein Epitopes Recognized by CD4+ T-Helper Lymphocytes from Equine Infectious Anemia Virus-Infected Carrier Horses J. Virol., May 1, 1999; 73(5): 4257 - 4265. [Abstract] [Full Text]
|
|
|
|
|
|
S. M. Lonning, W. Zhang, S. R. Leib, and T. C. McGuire Detection and Induction of Equine Infectious Anemia Virus-Specific Cytotoxic T-Lymphocyte Responses by Use of Recombinant Retroviral Vectors J. Virol., April 1, 1999; 73(4): 2762 - 2769. [Abstract] [Full Text]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |
