The use of poly- and monoclonal antibodies to assess the state of the immune system

Abstract

The function of the immune system of animals is influenced by a fairly large number of external (environmental, anthropogenic, infectious) and internal (mutations, impaired protein synthesis) factors. The result of their exposure is either the activation of the entire system or its individual links, or its suppression, causing the development of an immunodeficiency state. The quantitative determination of proteins of the immunoglobulin superfamily, namely, natural antibodies and cell receptors, provides valuable clinical information for clarifying the pathogenesis of the disease and differential diagnosis. The immunoglobulin profile of the body determines the functional ability of the immune system to recognize foreign agents. B-cell membrane immunoglobulins are the receptor for the antigen and are identical to its secreted form - the antibody. The modulation of their number reflects the processes of activation and inhibition of cellular reactions. The cell is constantly recycling membrane proteins. Similar processes occur with immunoglobulins, some of which are immersed in the cell, while others, on the contrary, are built into the membrane or secreted into the extracellular space in soluble form. Immunodiagnostics based on the determination of the immunoglobulins that make up the membrane and soluble pools makes it possible to assess the functional state of not only B cells, but also the immunoreactivity of the body as a whole. This paper presents a quantitative assessment of the soluble and membrane forms of clinically healthy cattle immunoglobulins using poly- and monoclonal antibodies.

Roughness of Production Conditions: Does It Really Affect Stability of IgG-Based Antivenoms?

“…Namely, increased temperatures partially unfold proteins, disclosing the hydrophobic amino acids that are usually hidden within their core and that represent “hot spots“ for aggregation. After being exposed to the solvent, such sequences tend to form strong irreversible bonds, which are particularly common between the β-folded structures [ 25 , 26 ] that are highly represented in immunoglobulins [ 27 ].…”