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Detection of parvovirus B19 NS1-specific antibodies by ELISA and western blotting employing recombinant NS1 protein as antigen.
J Med Virol. 2002 Jul; 67(3):375-83.JM

Abstract

Human parvovirus B19 (B19) encodes a number of nonstructural proteins, including the major protein, NS1, and two structural proteins, VP1 and VP2. The use of denatured NS1 in enzyme-linked immunosorbent assay (ELISA) and Western blot (WB) assay has provided an opportunity to study some of the immunologic properties of NS1, but the results have been equivocal and the diagnostic sensitivity poor, probably because of the absence of conformational epitopes. Various viral isolates and baculovirus vectors were employed to produce recombinant B19 NS1 under nondenaturing conditions for the first time. To assess the antigenicity of purified B19 NS1, the reaction patterns of 252 samples were compared by B19 NS1 and VP2 ELISA. In sera from individuals with past infection (VP2 IgG-positive), the use of this new antigen increased significantly the sensitivity of ELISA compared with WB (78% vs. 33%, P = 0.001), contradicting perpetuated claims that B19 NS1 IgG is detected primarily in patients with arthralgia or chronic infection. Previous reports of the absence of NS1 IgG during the initial phase of infection (< 6 weeks) were proved incorrect by the detection of NS1 IgG in 60% of samples from patients recently infected by B19. Including conformational epitopes in the ELISA increases the diagnostic sensitivity, although immunologically, a temporal (years) attenuation of NS1 antibodies appears to take place. This novel diagnostic tool may be useful as a supplement in case of borderline results by VP2 ELISA and for monitoring the efficacy of future capsid-based B19 vaccines.

Authors+Show Affiliations

Department of Clinical Microbiology, University State Hospital, Rigshospitalet, Copenhagen, Denmark. e.heegaard@immi.ku.dkNo affiliation info availableNo affiliation info available

Pub Type(s)

Evaluation Study
Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

12116031

Citation

Heegaard, Erik D., et al. "Detection of Parvovirus B19 NS1-specific Antibodies By ELISA and Western Blotting Employing Recombinant NS1 Protein as Antigen." Journal of Medical Virology, vol. 67, no. 3, 2002, pp. 375-83.
Heegaard ED, Rasksen CJ, Christensen J. Detection of parvovirus B19 NS1-specific antibodies by ELISA and western blotting employing recombinant NS1 protein as antigen. J Med Virol. 2002;67(3):375-83.
Heegaard, E. D., Rasksen, C. J., & Christensen, J. (2002). Detection of parvovirus B19 NS1-specific antibodies by ELISA and western blotting employing recombinant NS1 protein as antigen. Journal of Medical Virology, 67(3), 375-83.
Heegaard ED, Rasksen CJ, Christensen J. Detection of Parvovirus B19 NS1-specific Antibodies By ELISA and Western Blotting Employing Recombinant NS1 Protein as Antigen. J Med Virol. 2002;67(3):375-83. PubMed PMID: 12116031.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Detection of parvovirus B19 NS1-specific antibodies by ELISA and western blotting employing recombinant NS1 protein as antigen. AU - Heegaard,Erik D, AU - Rasksen,Cecilie J, AU - Christensen,Jesper, PY - 2002/7/13/pubmed PY - 2002/10/2/medline PY - 2002/7/13/entrez SP - 375 EP - 83 JF - Journal of medical virology JO - J Med Virol VL - 67 IS - 3 N2 - Human parvovirus B19 (B19) encodes a number of nonstructural proteins, including the major protein, NS1, and two structural proteins, VP1 and VP2. The use of denatured NS1 in enzyme-linked immunosorbent assay (ELISA) and Western blot (WB) assay has provided an opportunity to study some of the immunologic properties of NS1, but the results have been equivocal and the diagnostic sensitivity poor, probably because of the absence of conformational epitopes. Various viral isolates and baculovirus vectors were employed to produce recombinant B19 NS1 under nondenaturing conditions for the first time. To assess the antigenicity of purified B19 NS1, the reaction patterns of 252 samples were compared by B19 NS1 and VP2 ELISA. In sera from individuals with past infection (VP2 IgG-positive), the use of this new antigen increased significantly the sensitivity of ELISA compared with WB (78% vs. 33%, P = 0.001), contradicting perpetuated claims that B19 NS1 IgG is detected primarily in patients with arthralgia or chronic infection. Previous reports of the absence of NS1 IgG during the initial phase of infection (< 6 weeks) were proved incorrect by the detection of NS1 IgG in 60% of samples from patients recently infected by B19. Including conformational epitopes in the ELISA increases the diagnostic sensitivity, although immunologically, a temporal (years) attenuation of NS1 antibodies appears to take place. This novel diagnostic tool may be useful as a supplement in case of borderline results by VP2 ELISA and for monitoring the efficacy of future capsid-based B19 vaccines. SN - 0146-6615 UR - https://www.unboundmedicine.com/medline/citation/12116031/Detection_of_parvovirus_B19_NS1_specific_antibodies_by_ELISA_and_western_blotting_employing_recombinant_NS1_protein_as_antigen_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&amp;sid=nlm:pubmed&amp;issn=0146-6615&amp;date=2002&amp;volume=67&amp;issue=3&amp;spage=375 DB - PRIME DP - Unbound Medicine ER -