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ARS Home » Midwest Area » Ames, Iowa » National Animal Disease Center » Virus and Prion Research » Research » Publications at this Location » Publication #69610
Title: BACULOVIRUS EXPRESSION AND IMMUNOLOGICAL DETECTION OF THE MAJOR STRUCTURAL PROTEINS OF PORCINE REPRODUCTIVE AND RESPIRATORY SYNDROME VIRUS

Author
item KREUTZ, LUIZ - IOWA STATE UNIVERSITY
item Mengeling, William

Submitted to: Veterinary Microbiology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 6/19/1997
Publication Date: N/A
Citation: N/A

Interpretive Summary: Porcine reproductive and respiratory syndrome (PRRS) first appeared in the United States in 1987. It caused by a virus and, as the name implies, it affects both the reproductive and respiratory tracts of susceptible pigs. Since 1987 PRRS has spread nationally and internationally and it is now believed to be one of the most economically important diseases faced by the swine industries worldwide. In this study we developed a laboratory method to produce components of the causative virus that have potential to be used for improved diagnostic tests and vaccines. The ability to diagnose the disease and control it by vaccination will save the U.S. swine industry millions of dollars annually.

Technical Abstract: Each of the three major structural proteins (envelope glycoprotein E, non- glycosylated membrane protein M, and nucleoprotein N) of an American strain of porcine reproductive and respiratory syndrome virus (PRRSV) was expressed using a recombinant baculovirus expression system. Insect cells infected with the respective recombinant baculovirus synthesized five distinct forms of E glycoprotein with molecular mass (Mr) of 17, 20, 23, 25, and 26 K, and a single form of non-glycosylated protein M and nucleocapsid N with a Mr of approximately 21 and 15 K, respectively. Because the number of forms of the glycoprotein E was reduced from five to two (20 and 17 K) when infected cells were treated with tunicamycin, we speculate that they were different glycosylated forms of the same proteins, and the 20 and 17 K peptides represent non-glycosylated forms of E glycoprotein with and without, respectively, the N-terminal signal sequence. All the proteins were identified by immunoblot with convalescent sera from animals infected with an American strain of PRRSV, indicating that they were similar to the native proteins. The ability to produce each protein in the baculovirus system might provide an additional mean for their structural and functional characterization.