Human parvovirus B19 is the aetiological agent of the common childhood
disease erythema infectiosum (fifth disease). The infection is usuall
y benign and self-limiting, but in adults cases of severe arthritis wh
ich may persist for years have been reported. Neutralizing antibodies
directed against the structural proteins are usually produced shortly
after the infection. The immune response against the third major prote
in, the nonstructural protein NS-1, of parvovirus B19 has not been cha
racterized so far. We cloned and expressed the full-length NS-1 protei
n and fragments thereof in Escherichia coli. The purified recombinant
proteins were used to investigate the presence of antibodies to the NS
-1 protein in sera from patients with parvovirus B19 infection. Specif
ic antibodies could be detected in sera from patients suffering from s
evere parvovirus B19-associated arthritis using Western blot analysis
and an ELISA. Sera from patients with acute or past infection without
complications did not contain detectable levels of immunoglobulin to N
S-1. The use of subfragments of the NS-1 protein allowed localization
of the antigenic domains in the carboxy-terminal region of the protein
.