Abstract
Indirect enzyme linked immunosorbant assays (ELISAs) utilizing the three major structural proteins (M, N, and G(L)) of equine arteritis virus (EAV) expressed from recombinant baculoviruses were developed. A large panel of sera collected from uninfected horses, and from animals experimentally and naturally infected with EAV or vaccinated with the modified live virus vaccine against equine viral arteritis, were used to characterize the humoral immune response of horses to the three major EAV structural proteins. The data suggest that the M protein was the major target of the equine antibody response to EAV. The responses of individual animals varied and ELISAs that utilized individual EAV structural proteins were not reliable for detecting antibodies in all sera that contained neutralizing antibodies to EAV. An ELISA based on a cocktail of all three EAV structural proteins, however, was used successfully to detect antibodies in most equine sera that were positive in the standard serum neutralization assay following natural or experimental EAV infection (100% specificity, 92.3% sensitivity). In contrast, this ELISA did not reliably detect antibodies in the sera of vaccinated horses. EAV frequently causes a persistent infection in stallions and all sera from carrier stallions evaluated in this study had obvious reactivity with the N protein, whereas seropositive non-carrier stallions, mares and geldings did not respond consistently to the N protein. Copyright (C) 1998 Elsevier Science B.V.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 127-137 |
| Number of pages | 11 |
| Journal | Journal of Virological Methods |
| Volume | 76 |
| Issue number | 1-2 |
| DOIs | |
| State | Published - Dec 1 1998 |
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Keywords
- Antibody specificity
- Baculovirus
- Enzyme linked immunosorbant assay (ELISA)
- Equine arteritis virus (EAV)
- Structural proteins
ASJC Scopus subject areas
- Virology
Cite this
Detection of antibodies to equine arteritis virus by enzyme linked immunosorbant assays utilizing G(L), M and N proteins expressed from recombinant baculoviruses. / Hedges, Jodi F.; Balasuriya, Udeni B R; Ahmad, Shabbir; Timoney, Peter J.; McCollum, William H.; Yilma, Tilahun; Maclachlan, Nigel J.
In: Journal of Virological Methods, Vol. 76, No. 1-2, 01.12.1998, p. 127-137.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Detection of antibodies to equine arteritis virus by enzyme linked immunosorbant assays utilizing G(L), M and N proteins expressed from recombinant baculoviruses
AU - Hedges, Jodi F.
AU - Balasuriya, Udeni B R
AU - Ahmad, Shabbir
AU - Timoney, Peter J.
AU - McCollum, William H.
AU - Yilma, Tilahun
AU - Maclachlan, Nigel J
PY - 1998/12/1
Y1 - 1998/12/1
N2 - Indirect enzyme linked immunosorbant assays (ELISAs) utilizing the three major structural proteins (M, N, and G(L)) of equine arteritis virus (EAV) expressed from recombinant baculoviruses were developed. A large panel of sera collected from uninfected horses, and from animals experimentally and naturally infected with EAV or vaccinated with the modified live virus vaccine against equine viral arteritis, were used to characterize the humoral immune response of horses to the three major EAV structural proteins. The data suggest that the M protein was the major target of the equine antibody response to EAV. The responses of individual animals varied and ELISAs that utilized individual EAV structural proteins were not reliable for detecting antibodies in all sera that contained neutralizing antibodies to EAV. An ELISA based on a cocktail of all three EAV structural proteins, however, was used successfully to detect antibodies in most equine sera that were positive in the standard serum neutralization assay following natural or experimental EAV infection (100% specificity, 92.3% sensitivity). In contrast, this ELISA did not reliably detect antibodies in the sera of vaccinated horses. EAV frequently causes a persistent infection in stallions and all sera from carrier stallions evaluated in this study had obvious reactivity with the N protein, whereas seropositive non-carrier stallions, mares and geldings did not respond consistently to the N protein. Copyright (C) 1998 Elsevier Science B.V.
AB - Indirect enzyme linked immunosorbant assays (ELISAs) utilizing the three major structural proteins (M, N, and G(L)) of equine arteritis virus (EAV) expressed from recombinant baculoviruses were developed. A large panel of sera collected from uninfected horses, and from animals experimentally and naturally infected with EAV or vaccinated with the modified live virus vaccine against equine viral arteritis, were used to characterize the humoral immune response of horses to the three major EAV structural proteins. The data suggest that the M protein was the major target of the equine antibody response to EAV. The responses of individual animals varied and ELISAs that utilized individual EAV structural proteins were not reliable for detecting antibodies in all sera that contained neutralizing antibodies to EAV. An ELISA based on a cocktail of all three EAV structural proteins, however, was used successfully to detect antibodies in most equine sera that were positive in the standard serum neutralization assay following natural or experimental EAV infection (100% specificity, 92.3% sensitivity). In contrast, this ELISA did not reliably detect antibodies in the sera of vaccinated horses. EAV frequently causes a persistent infection in stallions and all sera from carrier stallions evaluated in this study had obvious reactivity with the N protein, whereas seropositive non-carrier stallions, mares and geldings did not respond consistently to the N protein. Copyright (C) 1998 Elsevier Science B.V.
KW - Antibody specificity
KW - Baculovirus
KW - Enzyme linked immunosorbant assay (ELISA)
KW - Equine arteritis virus (EAV)
KW - Structural proteins
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UR - http://www.scopus.com/inward/citedby.url?scp=0032401156&partnerID=8YFLogxK
U2 - 10.1016/S0166-0934(98)00131-1
DO - 10.1016/S0166-0934(98)00131-1
M3 - Article
VL - 76
SP - 127
EP - 137
JO - Journal of Virological Methods
JF - Journal of Virological Methods
SN - 0166-0934
IS - 1-2
ER -