1887

Abstract

We have expressed a number of polypeptides derived from the capsid proteins of the human parvovirus B19 in . These include native VP1 (84K) and VP2 (58K) proteins and also fusions to β-galactosidase containing differing amounts of the amino terminus of the VP1/2 polypeptide. Although each of these was expressed at high levels and the majority were produced as full-length proteins, only one was soluble. This soluble polypeptide, p132, is a β-galactosidase fusion protein that includes 145 amino acids from B19 which are entirely derived from the region unique to VP1. Despite containing such a small portion of VP1, which itself constitutes only 4% of total capsid protein, p132 reacted with all our known anti-B19 IgM-positive human serum samples. We conclude that this region contains epitopes which must be prominently exposed on the intact virus. We have demonstrated the use of this recombinant antigen in a simple diagnostic assay for B19-specific antibodies which can be used for initial screening of human serum samples. In a survey of 103 serum specimens, our ELISA positively identified all samples (19/19) which were positive by IgM antibody capture radioimmunoassay. The recombinant p132 antigen is efficiently produced and readily purified from , and its use as a diagnostic antigen should increase the availability of routine clinical testing for human parvovirus infection.

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/content/journal/jgv/10.1099/0022-1317-71-11-2665
1990-11-01
2020-01-19
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http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-71-11-2665
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