Detection of abrin in food using enzyme-linked immunosorbent assay and electrochemiluminescence technologies

被引:42
作者
Garber, Eric A. E. [1 ]
Walker, Jennifer L. [2 ]
O'Brien, Thomas W. [2 ]
机构
[1] US FDA, Ctr Food Safety & Appl Nutr, Off Regulatory Sci, College Pk, MD 20740 USA
[2] Tetracore Inc, Rockville, MD 20850 USA
基金
美国国家卫生研究院;
关键词
D O I
10.4315/0362-028X-71.9.1868
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Abrin is a toxic ribosome-inactivating protein present in beans of Abrus precatorius, also known as rosary peas. The possibility that abrin could be used to adulterate food has made the development of assays for the detection of abrin a priority. Rabbit-derived polyclonal antibodies and mouse monoclonal antibodies were prepared against a mixture of abrin isozymes. The specificity and cross-reactivity of the antibodies were evaluated against a challenge library of 40 grains, nuts. legumes, and foods. An enzyme-linked immunosorbent assay (ELISA) and an electrochemiluminescence (ECL)-based assay were assembled and optimized. Polyclonal (capture) and polyclonal (detection) ELISAs, polyclonal and monoclonal ELISAs, and polyclonal and monoclonal ECL assays had limits of detection (LODs) of 0.1 to 0.5 ng/ml for abrin in buffer. The LOD for abrin dissolved into juices, dairy products, soda. chocolate drink, and condiments and analyzed with the ECL assay ranged from 0.1 to 0.5 ng/ml in the analytical sample. In contrast, the LODs for the ELISAs ranged from 0.5 to 10 ng/ml in the analytical sample.
引用
收藏
页码:1868 / 1874
页数:7
相关论文
共 26 条
[1]   Structure-function analysis and insights into the reduced toxicity of Abrus precatorius agglutinin I in relation to abrin [J].
Bagaria, Ashima ;
Surendranath, Kalpana ;
Ramagopal, Udupi A. ;
Ramakumar, Suryanarayanarao ;
Karande, Anjali A. .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (45) :34465-34474
[2]   Enzymatic activity of toxic and non-toxic type 2 ribosome-inactivating proteins [J].
Barbieri, L ;
Ciani, M ;
Girbés, T ;
Liu, WY ;
Van Damme, EJM ;
Peumans, WJ ;
Stirpe, F .
FEBS LETTERS, 2004, 563 (1-3) :219-222
[3]   DETECTION OF ABRIN [J].
CLARKE, EGC ;
HUMPHREYS, DJ .
JOURNAL OF THE FORENSIC SCIENCE SOCIETY, 1971, 11 (02) :109-+
[4]  
Dickers Kirsten J., 2003, Toxicological Reviews, V22, P137, DOI 10.2165/00139709-200322030-00002
[5]  
Ehrlich P., 1891, DMW-Deutsche Medizinische Wochenschrift, V17, P1218, DOI DOI 10.1089/bfm.2012.0025
[6]  
ENDO Y, 1987, J BIOL CHEM, V262, P5908
[7]  
GARBER EAE, 2005, 119 AOAC INT ANN M E
[8]  
Garber EAE, 2008, J AOAC INT, V91, P376
[9]   PROTECTION AGAINST INHALATION TOXICITY OF RICIN AND ABRIN BY IMMUNIZATION [J].
GRIFFITHS, GD ;
LINDSAY, CD ;
ALLENBY, AC ;
BAILEY, SC ;
SCAWIN, JW ;
RICE, P ;
UPSHALL, DG .
HUMAN & EXPERIMENTAL TOXICOLOGY, 1995, 14 (02) :155-164
[10]   EXAMINATION OF THE TOXICITY OF SEVERAL PROTEIN TOXINS OF PLANT-ORIGIN USING BOVINE PULMONARY ENDOTHELIAL-CELLS [J].
GRIFFITHS, GD ;
LINDSAY, CD ;
UPSHALL, DG .
TOXICOLOGY, 1994, 90 (1-2) :11-27