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The War on Heterophilic Antibody Interference

Central Laboratory, Norwegian Radium Hospital, Montebello, N-0310 Oslo, Norway

^aAuthor for correspondence. Fax 47-22-730725; e-mail johan.bjerner@klinmed.uio.no.

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Human heterophilic antibodies may bind the animal antibodies used in an immunoassay and thus produce erroneous results. Such interference has been increasingly recognized as a diagnostic problem (1)(2). In this issue of Clinical Chemistry, Adel Ismail (3) discusses the two main issues of heterophilic antibody interference in immunometric assays: how to detect it and how to avoid it. This is an important discussion to which all clinical chemists should feel invited. This field requires not only a profound understanding of heterophilic antibody interference but also hands-on experience with immunoassays.

To detect heterophilic antibody interference in the sample, the first critical step is to suspect it. The starting point is often a clinician contacting the laboratory about a mismatch between the clinical information and laboratory results. Once there is suspicion of such interference, a classic approach has been to make serial dilutions of the sample. As Ismail (3) points out, most samples with heterophilic antibody interference will then display nonlinearity. The author does not explain this nonlinearity but draws attention to the polyclonality of interfering antibodies, with affinities ranging from high to low, and he points out that with human antibodies more than one functional binding site is often involved. Human antibodies with high affinities for animal antibodies are specific for one or more animal species and do not bind human immunoglobulins. High-affinity human anti-human immunoglobulins would instantly form larger complexes, either to be removed from circulation or to cause serious disease. In our experience before the surge in therapeutic use of murine or humanized murine monoclonal antibodies, we found little evidence of interfering immunoglobulins from the immunoglobulin classes that normally exhibit higher affinities, i.e., IgA or IgG (personal observation). Low-affinity human antibodies often bind to both animal and human immunoglobulins, making . . . [Full Text of this Article]

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