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Molecular assessment of the role of envelope-associated structural proteins in cross neutralization among different PRRS viruses

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Abstract

To assess the role of each envelope-associated protein (i.e., ORFs 2–6 products) of type 2 PRRSV in cross neutralization mediated by antibody, chimeric mutants were generated by replacing ORFs of a VR2332-based infectious clone with those of JA142, SDSU73, PRRS124, or 2M11715 that are genetically and antigenically distinct from VR2332 and two-way neutralization assays were performed on those mutants using VR2332, JA142, SDSU73, or PRRS124 antisera. All ORF 5-replaced mutants showed increased susceptibility or resistance against homologous or heterologous antisera, respectively, in comparison to that of the donor strains, but failed to achieve a complete reversion of cross neutralization. In contrast, substitution of ORFs 3–6 completely reversed the susceptibility of the virus to neutralization by antibody. Changes in ORFs 3, 5, and 6 were additively responsible for reversion of the susceptibility, suggesting that the genetic similarity of these ORFs should be considered for better cross neutralization between two different type 2 PRRS viruses.

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Acknowledgments

The authors wish to thank Ms. Christine Meraz for excellent assistance in manuscript preparation. Dr. Fernando Osorio at the University of Nebraska (Lincoln, NE) and Dr. Kay Faaberg at the University of Minnesota (St. Paul, MN) are acknowledged for providing antisera and the VR2332 infectious clone, respectively, which were extremely valuable to this study. The study was supported in part by funding from the United States Department of Agriculture Formula Grant, Iowa Livestock Health Advisory Council, and the Iowa Pork Producers Association.

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  1. Department of Veterinary Diagnostic and Production Animal Medicine, College of Veterinary Medicine, Iowa State University, 1600 South 16th Street, Ames, IA, 50011, USA

    Won-Il Kim & Kyoung-Jin Yoon

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Kim, WI., Yoon, KJ. Molecular assessment of the role of envelope-associated structural proteins in cross neutralization among different PRRS viruses. Virus Genes 37, 380–391 (2008). https://doi.org/10.1007/s11262-008-0278-1

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