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Journal of Clinical Microbiology, December 2008, p. 3971-3979, Vol. 46, No. 12
0095-1137/08/$08.00+0     doi:10.1128/JCM.01204-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Self-Assembly of the Recombinant Capsid Protein of a Swine Norovirus into Virus-Like Particles and Evaluation of Monoclonal Antibodies Cross-Reactive with a Human Strain from Genogroup II{triangledown}

Horacio Almanza,1 Carolina Cubillos,1 Iván Angulo,1,{dagger} Francisco Mateos,1 José R. Castón,2 Wim H. M. van der Poel,3,{ddagger} Jan Vinje,4,§ Juan Bárcena,1 and Ignacio Mena1*

Centro de Investigación en Sanidad Animal (CISA-INIA), Valdeolmos, 28130 Madrid, Spain,1 Centro Nacional de Biotecnología (CNB-CSIC), Campus UAM, 28049 Madrid, Spain,2 Microbiological Laboratory for Health Protection, National Institute for Public Health and the Environment, Bilthoven, The Netherlands,3 Department of Environmental Sciences and Engineering, University of North Carolina, Chapel Hill, North Carolina4

Received 25 June 2008/ Returned for modification 5 August 2008/ Accepted 29 September 2008

Noroviruses (NoVs) are responsible for the majority of gastroenteritis outbreaks in humans. Recently, NoV strains which are genetically closely related to human genogroup II (GII) NoVs have been detected in fecal specimens from swine. These findings have raised concern about the possible role of pigs as reservoirs for NoVs that could infect humans. To better understand the epidemiology of swine NoVs in both the swine and the human populations, rapid immunoassays are needed. In this study, baculovirus recombinants were generated to express the capsid gene of a swine NoV GII genotype 11 (GII.11) strain which self-assembled into virus-like particles (VLPs). Subsequently, the purified VLPs were used to evoke monoclonal antibodies (MAbs) in mice. A panel of eight promising MAbs was obtained and evaluated for their ability to bind to heterologous VLPs, denaturated antigens, and truncated capsid proteins. The MAbs could be classified into two groups: two MAbs that recognized linear epitopes located at the amino-terminal half (shell domain) of the swine NoV GII.11 VLPs and that cross-reacted with human GII.4 NoV VLPs. The other six MAbs bound to conformational epitopes and did not cross-react with the human GII.4 VLPs. To our knowledge, this is the first report on the characterization of MAbs against swine NoVs. The swine NoV VLPs and the MAbs described here may be further used for the design of diagnostic reagents that could help increase our knowledge of the prevalence of NoV infections in pigs and the possible role of pigs as reservoirs for NoVs.

* Corresponding author. Mailing address: Centro de Investigación en Sanidad Animal (CISA-INIA), Carretera de Algete a El Casar, Valdeolmos, Madrid 28130, Spain. Phone: 34 91 620 2300. Fax: 34 91 620 2247. E-mail: gmena{at}inia.es

{triangledown} Published ahead of print on 8 October 2008.

{dagger} Present address: The Scripps Research Institute, Scripps Florida, Jupiter, FL.

{ddagger} Present address: Central Veterinary Institute, Wageningen University Research, Wageningen, The Netherlands.

§ Present address: Division of Viral Diseases, Centers for Disease Control and Prevention, Atlanta, GA.

Journal of Clinical Microbiology, December 2008, p. 3971-3979, Vol. 46, No. 12
0095-1137/08/$08.00+0     doi:10.1128/JCM.01204-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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