Characterization of a panel of monoclonal antibodies and their use in the study of the antigenic diversity of bovine viral diarrhea virus

Wayne V. Corapi From the Diagnostic Laboratory, New York State College of Veterinary Medicine, Cornell University, Ithaca, NY 14853.

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Ruben O. Donis From the Diagnostic Laboratory, New York State College of Veterinary Medicine, Cornell University, Ithaca, NY 14853.

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Edward J. Dubovi From the Diagnostic Laboratory, New York State College of Veterinary Medicine, Cornell University, Ithaca, NY 14853.

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 PhD

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SUMMARY

A panel of 40 monoclonal antibodies (MAb) specific for bovine viral diarrhea virus (bvdv) was produced, and each MAb was characterized and grouped according to its viral protein specificity, immunoglobulin subclass, virus-neutralizing activity, and immunoreactivity with a large collection of bvdv isolates. The MAb were found to be specific for 1 of 3 sets of related viral-induced proteins found in cells infected with the Singer strain of bvdv. Group-1 MAb were specific for the 80- and 118-kilodalton (kD) proteins of bvdv. Group-2 MAb recognized 3 proteins with molecular sizes of 54, 56, and 58 kD. Group-3 MAb recognized a 43- and a 65-kD protein. The MAb belonged to either the IgGl, IgG2a, IgG2b, IgG3 subclasses or the IgE class of mouse immunoglobulin. All MAb in group 2 were able to neutralize bvdv and had neutralization titers that ranged from 24 to 1,600,000. The reactivity of the MAb with numerous field isolates of bvdv was highly variable. Both cytopathic and noncytopathic biotypes of bvdv were examined and had the same degree of antigenic variation. The greatest degree of variation was detected with group-2 MAb. The data demonstrate that bvdv isolates have a high degree of antigenic variation that is largely confined to the envelope glycoproteins associated with virus neutralization. The results also suggest that antigenic variability of this virus is important in the development and severity of the disease it causes.

SUMMARY

A panel of 40 monoclonal antibodies (MAb) specific for bovine viral diarrhea virus (bvdv) was produced, and each MAb was characterized and grouped according to its viral protein specificity, immunoglobulin subclass, virus-neutralizing activity, and immunoreactivity with a large collection of bvdv isolates. The MAb were found to be specific for 1 of 3 sets of related viral-induced proteins found in cells infected with the Singer strain of bvdv. Group-1 MAb were specific for the 80- and 118-kilodalton (kD) proteins of bvdv. Group-2 MAb recognized 3 proteins with molecular sizes of 54, 56, and 58 kD. Group-3 MAb recognized a 43- and a 65-kD protein. The MAb belonged to either the IgGl, IgG2a, IgG2b, IgG3 subclasses or the IgE class of mouse immunoglobulin. All MAb in group 2 were able to neutralize bvdv and had neutralization titers that ranged from 24 to 1,600,000. The reactivity of the MAb with numerous field isolates of bvdv was highly variable. Both cytopathic and noncytopathic biotypes of bvdv were examined and had the same degree of antigenic variation. The greatest degree of variation was detected with group-2 MAb. The data demonstrate that bvdv isolates have a high degree of antigenic variation that is largely confined to the envelope glycoproteins associated with virus neutralization. The results also suggest that antigenic variability of this virus is important in the development and severity of the disease it causes.

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