Novel monoclonal antibodies broadly reactive to human recombinant sapovirus-like particles
Article first published online: 23 OCT 2012
© 2012 The Societies and Wiley Publishing Asia Pty Ltd
Microbiology and Immunology
Volume 56, Issue 11, pages 760–770, November 2012
How to Cite
Kitamoto, N., Oka, T., Katayama, K., Li, T.-C., Takeda, N., Kato, Y., Miyoshi, T. and Tanaka, T. (2012), Novel monoclonal antibodies broadly reactive to human recombinant sapovirus-like particles. Microbiology and Immunology, 56: 760–770. doi: 10.1111/j.1348-0421.2012.00499.x
- Issue published online: 23 OCT 2012
- Article first published online: 23 OCT 2012
- Accepted manuscript online: 25 AUG 2012 02:35AM EST
- Received 4 July 2012; revised 2 August 2012; accepted 3 August 2012.
- monoclonal antibody;
Sapovirus (SaV), a member of the family Caliciviridae, is an important cause of acute epidemic gastroenteritis in humans. Human SaV is genetically and antigenically diverse and can be classified into four genogroups (GI, GII, GIV, and GV) and 16 genotypes (7 GI [GI.1–7], 7 GII, [GII.1–7], 1 GIV and 1 GV), based on capsid sequence similarities. Monoclonal antibodies (MAbs) are powerful tools for examining viruses and proteins. PAI myeloma cells were fused with spleen cells from mice immunized with a single type of recombinant human SaV virus-like particles (VLPs) (GI.1, GI.5, GI.6, GII.3, GIV, or GV). Sixty-five hybrid clones producing MAbs were obtained. Twenty-four MAbs were characterized by ELISA, according to their cross-reactivity to each VLP (GI.1, GI.5, GI.6, GII.2, GII.3, GII.4, GII.7, GIV, and GV). The MAbs were classified by this method into: (i) MAbs broadly cross-reactive to all GI, GII, GIV and GV strains; (ii) those reactive in a genogroup-specific; and (iii) those reactive in a genotype-specific manner. Further analysis of three broadly cross-reactive MAbs with a competitive ELISA demonstrated that at least two different common epitopes are located on the capsid protein of human SaVs in the four genogroups. The MAbs generated and characterized in this study will be useful tools for further study of the antigenic and structural topography of the human SaV virion and for developing new diagnostic assays for human SaV.