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An enterovirus-specific indirect ELISA, based on a single local isolate of coxsackie B5 as antigen, was used to study the IgA, IgG, and IgM responses in 19 patients with a recent or current enterovirus infection. Twelve different enterovirus serotypes were isolated from 15 patients. Paired serum samples were available from 10 and a single serum from 5 of these 15 patients. In addition, 4 patients diagnosed by a significant titer rise of complement fixing antibodies to enterovirus were included. A serological diagnosis, defined as an increase in titer of enterovirus IgG and/or presence of enterovirus IgM, were established in all 14 patients with paired sera. Enterovirus IgM was present in either a single serum or in both sera in 13 of them. Out of 5 patients with a single serum sample only, enterovirus IgA or enterovirus IgM was found in 4. Specific IgA was present in either a single serum or in both sera in 14 of the 19 patients. Seven of the 10 enterovirus isolate patients with paired sera had a significant titer rise of complement fixing antibodies; however, all 10 were diagnosed by ELISA. Among 64 healthy controls 2 had enterovirus IgA and none had enterovirus IgM. In conclusion, the use of a single antigen-based ELISA was found to be reliable for the diagnosis of recent and current enterovirus infections.

It has been suggested that the x2 glycosphingolipid (GSL) could offer a structural basis for a P-like antigen activity found in blood group p individuals [Kannagi R., Fukuda, M.N., Hakomori, S. (1982) J. Biol. Chem. 257, 4438]. The structures of the x2 and sialosyl-x2 GSLs have been confirmed unequivocally as shown below by +FAB-MS, methylation analysis by GC-MS, and 1H-NMR. We have established a [formula: see text] monoclonal antibody (TH2) specific for the GalNAc beta 1----3Gal beta 1----4GlcNAc epitope, the terminal trisaccharide of x2 GSL. Application of MAb TH2 on TLC immunoblotting together with chemical analysis indicates the following points of interest: (i) the existence of extended type GSLs having the same x2 terminal structure; (ii) the chemical quantities of x2, sialosyl-x2, and extended x2 found in blood cells and in various tissues including carcinomas being nearly the same; (iii) considerably larger quantities of x2 and x2-derived structures found in blood samples of rare blood group p individuals. The accumulation of x2 and its derivatives in blood cells of p individuals is in contrast to the occurrence of these GSLs as extreme minor components in normal human red blood cells and tissues, and they may be responsible for the reported P-like activity in blood group p individuals [Naiki, M., & Marcus, D. M. (1977) J. Immunol. 119, 537].

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