Real-Time, label-free monitoring of tumor antigen and serum antibody interactions Journal Article


Authors: Campagnolo, C.; Meyers, K. J.; Ryan, T.; Atkinson, R. C.; Chen, Y. T.; Scanlan, M. J.; Ritter, G.; Old, L. J.; Batt, C. A.
Article Title: Real-Time, label-free monitoring of tumor antigen and serum antibody interactions
Abstract: Conventional techniques for the detection of biomolecular interactions can be limited by the need for exogenous labels, time- and labor-intensive protocols, as well as by poor sensitivity levels. A refractometer instrument has been reconfigured to detect biomolecular interactions through changes in surface plasmon resonance (SPR). The binding kinetics and affinity values of anti-NY-ESO-1 monoclonal antibody, ES121, to the cancer-testis antigen NY-ESO-1 were determined according to the surface heterogeneity model and resulted in K D values of 1.3×10 -9 and 2.1×10 -10 M. The reconfigured instrument was then used to measure the interaction between tumor antigens and serum antibodies against these antigens in preselected cancer patient sera samples. The tumor antigens assayed included NY-ESO-1, SSX2 and p53, all used as recombinant proteins containing polyhistidine tags. These results demonstrated that the instrument is capable of detecting the binding of serum antibodies from cancer patient sera to immobilized tumor antigens, consistent with those observed previously in ELISA-based experiments. These results demonstrate the potential of SPR technology for the rapid diagnosis and monitoring immune responses. © 2004 Elsevier B.V. All rights reserved.
Keywords: cancer patient; binding affinity; blood chemical analysis; membrane proteins; tumor antigen; enzyme linked immunosorbent assay; antibodies, monoclonal; immune response; antigens, neoplasm; cancer testis antigen; antigen detection; testicular neoplasms; immunoassay; molecular interaction; enzyme-linked immunosorbent assay; elisa; surface plasmon resonance; staining and labeling; antigen-antibody reactions; computer systems; antibody blood level; protein-protein interactions; biosensor; humans; human; male; priority journal; article; biomolecular interactions; ni-nta; nickel-nitrilotriacetic acid; spr; x-ray photoelectron spectroscopy; xps; refractometer; refractometry
Journal Title: Journal of Biochemical and Biophysical Methods
Volume: 61
Issue: 3
ISSN: 0165-022X
Publisher: Elsevier Science, Inc.  
Date Published: 2004-11-30
Start Page: 283
End Page: 298
Language: English
DOI: 10.1016/j.jbbm.2004.05.006
PROVIDER: scopus
PUBMED: 15571777
DOI/URL:
Notes: J. Biochem. Biophys. Methods -- Cited By (since 1996):57 -- Export Date: 16 June 2014 -- CODEN: JBBMD -- Source: Scopus
Altmetric
Citation Impact
MSK Authors
  1. Matthew J Scanlan
    49 Scanlan
  2. Gerd Ritter
    166 Ritter
  3. Lloyd J Old
    519 Old