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J Clin Microbiol. Jun 1995; 33(6): 1452–1455.
PMCID: PMC228194
Expression, self-assembly, and antigenicity of a snow mountain agent-like calicivirus capsid protein.
X Jiang, D O Matson, G M Ruiz-Palacios, J Hu, J Treanor, and L K Pickering
Center for Pediatric Research, Children's Hospital of The King's Daughters, Eastern Virginia Medical School, Norfolk 23510-1001, USA.
Abstract
Virus-like particles were produced in insect cells infected with a recombinant baculovirus containing the capsid gene of MX virus, a Mexican strain of human calicivirus. These recombinant MX (rMX) particles were morphologically similar to recombinant Norwalk virus (rNV) particles as observed under an electron microscope and contained a single capsid protein with a molecular weight of 57,000, which was slightly smaller than that of rNV. This protein was immunoprecipitated by sera from volunteers infected with the Snow Mountain agent, but it reacted weakly with sera from volunteers infected with NV. This protein did not react with hyperimmune antisera from animals immunized with rNV in the rNV antigen enzyme immunoassay (EIA). Seroresponses were detected from volunteers infected with Snow Mountain agent and Hawaii agent when the rMX particles were used as antigen in an EIA. This EIA also detected an immune response in the sera of child from whom the MX virus was isolated, and a high prevalence of antibody to MX virus was found in the sera of a cohort of Mexican children.
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