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Updated: Jul 15, 2026

Single-cell Screening Method for the Selection and Recovery of Antibodies with Desired Specificities from Enriched Human Memory B Cell Populations
Published on: August 22, 2019
Immunoglobulin crystals in reactive plasma cells in a dog
B Zimmerman1, M I Yamaguchi, L J Rush
1Department of Veterinary Biosciences, The Ohio State University, Columbus, OH 43210, USA.
Abstract:
Intracellular crystalline deposits of immunoglobulin are occasionally seen in human B-cell lymphoproliferative disorders such as multiple myeloma, chronic lymphocytic leukemia, and various forms of lymphoma. Even more uncommon is the occurrence of immunoglobulin crystals in benign plasma cells or reactive lymphocytes. Here we describe the histologic, immunohistochemical, and ultrastructural features of intracellular immunoglobulin crystals in nonneoplastic plasma cells in a chronic inflammatory lesion in a dog. Microscopically, the intracellular, nonbirefringent eosinophilic crystals were square to rectangular, 2-20 microm long, and caused nuclear displacement to the periphery. The crystal-containing cells, as well as some of the crystals themselves, were positive for lambda light chain. Ultrastructural findings were consistent with a lattice network of protein-molecule alignment. The cause and significance of the crystals is unknown.
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Antibody Structure
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
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The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
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