Antibody Testing for COVID-19


The orthopedic community has seen the COVID-19 pandemic decimate elective surgical volumes in most geographies. Patients and essential workers, such as health care providers, remain rightfully concerned about how to appropriately begin to return to work and community activity in a safe and responsible manner. Many believe that testing for the presence of antibodies on a widespread scale could help drive evidence-based decision-making, both on an individual and societal scale. Much information, and an equal amount of misinformation, has been produced on antibody testing. Education about the role and science of such testing is critically important for programs to be effectively understood and managed.

Antibody Function

An antibody, also called an immunoglobulin, is a protective protein produced by the immune system in response to the presence of a foreign substance (antigen), such as a pathogen. Antibodies recognize and latch onto antigens to remove them from the body. Antibodies are proteins produced and secreted by B cells (lymphocytes).

Because a principal function of B lymphocytes is antibody production, it is important to understand the salient features of these defense molecules and describe their different isotypes or classes. Antibodies are glycosylated protein molecules present on the surface of B cells (surface immunoglobulins) serving as antigen receptors or are secreted into the extracellular space where they can bind and neutralize their target antigens. A single antibody molecule consists of 4 protein chains: 2 “heavy” (H chains) and 2 “light” (L chains) linked to each other by disulfide bonds. The N-terminus regions of the heavy and light chains, which collectively make up the antigen-binding site, are where the variability between one antibody molecule and another resides, hence determining specificity. An important feature is that each antibody recognizes a specific antigen, a phenomenon called “antibody specificity.” For example, an antibody that recognizes the mumps virus cannot recognize the measles virus and can only recognize one particular binding site on the mumps virus. There will likely be multiple antibodies to multiple different binding sites on an antigen such as a virus. For example, some antibodies to COVID-19 will target binding sites on proteins in the outer shell while some may target nucleic acid binding sites, but each will be specific and unique. Only when 2 different, but similar, viruses have identical structures will cross-reactivity occur. For example, if multiple strains of a coronavirus have maintained regions of nucleic acid that have not undergone mutation, an antibody that targets that region in one may target the identical region in another. Conversely, an antibody that recognizes the measles virus generally cannot recognize the mumps virus.

Journal of Orthopedic Oncology offers information in all aspects of primary, malignant tumors. Osteosarcoma, Ewing's sarcoma, chondrosarcoma, chordoma, and soft tissue sarcomas etc., it also deals with diagnostic methods, therapeutic approaches, clinical, laboratory research and reconstructive techniques.

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Editorial Team

Journal of Orthopedic Oncology

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