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J Gen Virol 75 (1994), 889-893; DOI 10.1099/0022-1317-75-4-889
© 1994 Society for General Microbiology
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Monoclonal antibodies to immunodominant and neutralizing domains of the envelope surface protein of feline immunodeficiency virus

Herman Egberink1, Lian Keldermans1, Nancy Schuurman1, Jeanette Stam1, Wim Hesselink2, Arno van Vliet1, Ernst Verschoor1, Marian Horzinek1 and Anthony de Ronde1

1 Virology Division, Department of Infectious Diseases and Immunology, Veterinary Faculty, Utrecht University, Yalelaan 1, 3584 CL Utrecht
and2 Intervet International BV, Boxmeer, The Netherlands

Hybridomas secreting monoclonal antibodies (MAbs) specific for the surface protein (SU) of feline immunodeficiency virus were generated. Four MAbs were obtained which could be assigned to two groups based on their neutralization and competition behaviour. Using SU protein fragments expressed in Escherichia coli the antigenic site recognized by one of the MAbs (2H11) could be mapped to the c terminus. The neutralizing MAb 1E1 did not bind to any of the SU protein fragments and was directed to a conformational epitope. Binding of the MAb 1E1 to native SU protein could be blocked with a rabbit serum raised against the SU3 fragment (amino acids 361 to 445). These data indicate that at least part of the epitope is located on this SU3 domain. In competition experiments most sera of naturally infected cats were able to inhibit binding of the MAbs. This shows the conserved and immunodominant nature of the epitopes involved.

Received 12 August 1993; accepted 22 November 1993.


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Copyright © 1994 by the Society for General Microbiology.