Abstract

Abrin, a highly toxic plant toxin, is a potential bioterror weapon. Work from our laboratory and others have shown that abrin is highly resistant to both thermal and pH inactivation methods. We sought to evaluate the effectiveness of selected food processing thermal inactivation conditions against abrin in economically important food matrices (whole milk, non-fat milk, liquid egg, and ground beef). The effectiveness of toxin inactivation was measured via three different assays: (1) In vitro cell free translation (CFT) assay, (2) Vero cell culture cytotoxicity; and the in vivo mouse intraperitoneal (ip) bioassay. For both whole and non-fat milk, complete inactivation was achieved at temperatures of 80 °C for 3 min or 134 °C for 60 s, which were higher than the normal vat/batch pasteurization or the high temperature short time pasteurization (HTST). Toxin inactivation in liquid egg required temperatures of 74 °C for 3 min higher than suggested temperatures for scrambled eggs (22% solids) and plain whole egg. Additionally, the ground beef (80:20%) matrix was found to be inhibitory for full toxin activity in the mouse bioassay while retaining some activity in both the cell free translation assay and Vero cell culture cytotoxicity assay.

Highlights

  • Members of the Type II family of ribosome-inactivating proteins (RIP), such as abrin and ricin, inhibit eukaryotic protein synthesis, thereby leading to apoptosis and cell death

  • We sought to evaluate the effectiveness of some common pasteurization conditions for dairy and their effect on the highly potent plant toxin, abrin

  • To mimic ultra-pasteurization, we inactivated the toxin at 134 ◦ C (273.2 ◦ F) for 2 s, 30 s, or 60 s using a heat-block

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Summary

Introduction

Members of the Type II family of ribosome-inactivating proteins (RIP), such as abrin and ricin, inhibit eukaryotic protein synthesis, thereby leading to apoptosis and cell death. Abrin is an A-B toxin with the A-chain having an N-glycosidase activity that cleaves the C–N bond of adenine at position. 4324 on the 28S rat ribosomal RNA [1,2] This cleavage prevents ribosomes from binding to elongation factors (EF) 1/2, which leads to eventual cell death [1,2,3,4,5,6,7]. The B-chain is important for binding to cell surface carbohydrate receptors facilitating receptor-mediated endocytosis of the toxin. Oral intoxication with abrin is treated with emesis induction, gastric lavage, activated charcoal, and whole bowel irrigation [5]

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