Evaluation of protein-denaturing immunoassays for avidity of immunoglobulin G to rubella virus.

Abstract

Immunoassays have been recently developed that measure the avidity of IgG antibodies to complex microbial antigens and are suitable for serologic diagnosis of infectious diseases. In these avidity ELISAs, protein-denaturing agents are applied either as diluents of patient sera to prevent the immune complexing of IgG (diluting principle), or the preformed complexes are treated with the protein denaturants (eluting principle). We compared four protein denaturants previously used in such assays, in a diagnostic avidity ELISA for rubella IgG. Diethylamine, guanidine, thiocyanate, or urea were applied, by either principle at various concentrations, and thiocyanate, or urea were applied, by either principle at various concentrations, and thiocyanate at an optimum pH. Patient sera obtained recently after primary infection were distinguished from sera representing past rubella immunity by any protein denaturant tested by the eluting principle, which was superior to the diluting principle.

• Authors: J Polanec, I Seppälä, S Rousseau, K Hedman
• Journal: Journal of clinical laboratory analysis (J Clin Lab Anal) Vol. 8 Issue 1 Pg. 16-21 ( 1994) ISSN: 0887-8013 [Print] United States
• PMID: 8164106 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Diethylamines
• Guanidines
• Immunoglobulin G
• Thiocyanates
• Urea
• diethylamine
• Guanidine
• thiocyanate

Topics

• Antibody Affinity
• Diethylamines (pharmacology)
• Enzyme-Linked Immunosorbent Assay (methods)
• Guanidine
• Guanidines (pharmacology)
• Humans
• Hydrogen-Ion Concentration
• Immunoglobulin G (immunology)
• Protein Denaturation
• Rubella (immunology)
• Rubella virus (immunology)
• Thiocyanates (pharmacology)
• Urea (pharmacology)