Serum‐derived bovine immunoglobulin/protein isolate binds to pathogen‐associated molecular patterns (836.6)

Abstract

A key feature of the innate immune system is the panoply of pattern recognition receptors which bind a wide array of highly conserved pathogen‐associated molecular patterns (PAMPs). Under normal conditions, PAMP binding initiates downstream signaling cascades culminating in pro‐inflammatory cytokine production, inflammation, and subsequent antigen elimination. Continual PAMP binding leads to a persistent state of inflammation associated with numerous chronic inflammatory disorders such as IBS, IBD, and HIV enteropathy. We hypothesize that immune exclusion of PAMPs through antigen/antibody interactions can reduce inflammatory signaling and lessen the gastrointestinal manifestations of these disorders.Serum‐derived bovine immunoglobulin/protein isolate (SBI) is comprised primarily of immunoglobulins (Ig) and is indicated for the clinical dietary management of gastrointestinal enteropathy under physician supervision. We investigated the binding of SBI’s Ig components (IgG, IgA, and IgM) to PAMPs associated with intestinal inflammatory disorders. Using a modified ELISA technique we have shown that IgG, IgA, and IgM contained in SBI bind to a wide array of bacterial, viral, and fungal PAMPs.Oral administration of SBI has been shown clinically to manage GI symptoms in patients with IBS‐D and HIV enteropathy; however, the mechanism of action is poorly understood. Here we show that SBI binds a wide variety of PAMPs. We propose that Ig‐PAMP binding may inhibit immune recognition and the chronic inflammation associated with persistent immune activation.