Isolation of four isotoxic proteins and one agglutinin from jequiriti bean (Abrus precatorius)

Lin, Jung‐Yaw; Lee, Te‐Chang; Hu, Su-Tieng; Tung, Ta‐Cheng

doi:10.1016/0041-0101(81)90116-1

Cited by 86 publications

(22 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…AAG was isolated from the kernels of Abrus precatorius seeds by chromatographies on a Sepharose 6B column and a Sephadex G-100 column as described previously [12]. The flow rate of chromatography was 20 ml/hr and protein concentration was determined by the bicinchonic acid method [27].…”

Section: Methodsmentioning

confidence: 99%

“…Most commonly RIPs are type I RIPs, only single polypeptide chain proteins composed of the toxophoric A subunit with a molecular mass around 30 kDa [5-8] such as curcin [9] and trichomislin [10]. Some are type II RIPs consisting of two types of polypeptide subunits, A chain of homologous and functionally similar to type I RIPs and B chain with a galactose-specific lectin domain that binds to cell surfaces, such as ricin [11] abrin and abrus agglutinin (AAG) [12]. A chain and B chain are from one gene and link through disulfide bond after post-translation modification [13].…”

Section: Introductionmentioning

confidence: 99%

“…They can be classified as abrins and AAG by oligomerization. Abrins are potent toxic heterodimeric glycoproteins with an LD50 of 20 μg/kg body weight; while AAG is a relatively less toxic heterotetrameric glycoprotein of which the LD50 is 5 mg/kg body weight [12]. But their therapeutics indexes are similar [18].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

A biophysical elucidation for less toxicity of Agglutinin than Abrin-a from the Seeds of Abrus Precatorius in consequence of crystal structure

Cheng

Liu

et al. 2010

J Biomed Sci

View full text Add to dashboard Cite

X-ray crystal structure determination of agglutinin from abrus precatorius in Taiwan is presented. The crystal structure of agglutinin, a type II ribosome-inactivating protein (RIP) from the seeds of Abrus precatorius in Taiwan, has been determined from a novel crystalline form by the molecular replacement method using the coordinates of abrin-a as the template. The structure has space group P41212 with Z = 8, and been refined at 2.6 Å to R-factor of 20.4%. The root-mean-square deviations of bond lengths and angles from the standard values are 0.009 Å and 1.3°. Primary, secondary, tertiary and quaternary structures of agglutinin have been described and compared with those of abrin-a to a certain extent. In subsequent docking research, we found that Asn200 of abrin-a may form a critical hydrogen bond with G4323 of 28SRNA, while corresponding Pro199 of agglutinin is a kink hydrophobic residue bound with the cleft in a more compact complementary relationship. This may explain the lower toxicity of agglutinin than abrin-a, despite of similarity in secondary structure and the activity cleft of two RIPs.

show abstract

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

A biophysical elucidation for less toxicity of Agglutinin than Abrin-a from the Seeds of Abrus Precatorius in consequence of crystal structure

Cheng

Liu

et al. 2010

J Biomed Sci

View full text Add to dashboard Cite

show abstract

“…Abrin isolated from Abrus precatorius seeds has many different potential isoforms [ 7 , 8 , 9 ]. Three to four isoforms have been isolated by different laboratories and reported to have different toxin activities or median lethal doses (LD 50 ) [ 7 , 9 , 10 , 11 , 12 , 13 , 14 ]. Our abrin toxin preparations also contained a 120 kDa heterotetrameric species, agglutinin (APA-1).…”

Section: Introductionmentioning

confidence: 99%

Abrin Toxicity and Bioavailability after Temperature and pH Treatment

Tam

Henderson

Stanker

et al. 2017

Toxins

View full text Add to dashboard Cite

Abrin, one of most potent toxins known to man, is derived from the rosary pea (jequirity pea), Abrus precatorius and is a potential bioterror weapon. The temperature and pH stability of abrin was evaluated with an in vitro cell free translation (CFT) assay, a Vero cell culture cytotoxicity assay, and an in vivo mouse bioassay. pH treatment of abrin had no detrimental effect on its stability and toxicity as seen either in vitro or in vivo. Abrin exposure to increasing temperatures did not completely abrogate protein translation. In both the cell culture cytotoxicity model and the mouse bioassay, abrin’s toxic effects were completely abrogated if the toxin was exposed to temperatures of 74 °C or higher. In the cell culture model, 63 °C-treated abrin had a 30% reduction in cytotoxicity which was validated in the in vivo mouse bioassay with all mice dying but with a slight time-to-death delay as compared to the non-treated abrin control. Since temperature inactivation did not affect abrin’s ability to inhibit protein synthesis (A-chain), we hypothesize that high temperature treatment affected abrin’s ability to bind to cellular receptors (affecting B-chain). Our results confirm the absolute need to validate in vitro cytotoxicity assays with in vivo mouse bioassays.

show abstract

“…Furthermore, agglutinin, an evolutionary variant of pulchellin and abrin, has been shown to be less toxic due to the lack of a critical hydrogen bond that causes a lower binding in between Abrin and 28S RNA [9]. From Abrus precatorius, the chemical isolation and initial cell toxicity testing of four distinct protein isoforms of abrin (abrin-a, -b, -c, and -d) and agglutinin was first published in the late 1970s and early 1980s [10,11]. The first successful cDNA conversion and cloning of these multiple sequences was carried out between 1991 and 1992 [12,13], providing the first genetic sequencing information on the coding of these toxin producing genes.…”

Section: Introductionmentioning

confidence: 99%

Detection of Abrin-Like and Prepropulchellin-Like Toxin Genes and Transcripts Using Whole Genome Sequencing and Full-Length Transcript Sequencing of Abrus precatorius

Hovde

Daligault

Hanschen

et al. 2019

Toxins

View full text Add to dashboard Cite

The sequenced genome and the leaf transcriptome of a near relative of Abrus pulchellus and Abrus precatorius was analyzed to characterize the genetic basis of toxin gene expression. From the high-quality genome assembly, a total of 26 potential coding regions were identified that contain genes with abrin-like, pulchellin-like, and agglutinin-like homology, with full-length transcripts detected in leaf tissue for 9 of the 26 coding regions. All of the toxin-like genes were identified within only five isolated regions of the genome, with each region containing 1 to 16 gene variants within each genomic region (<1 Mbp). The Abrus precatorius cultivar sequenced here contains genes which encode for proteins that are homologous to certain abrin and prepropulchellin genes previously identified, and we observed substantial diversity of genes and predicted gene products in Abrus precatorius and previously characterized toxins. This suggests diverse toxin repertoires within Abrus, potentially the results of rapid toxin evolution.

show abstract

Isolation of four isotoxic proteins and one agglutinin from jequiriti bean (Abrus precatorius)

Cited by 86 publications

References 13 publications

A biophysical elucidation for less toxicity of Agglutinin than Abrin-a from the Seeds of Abrus Precatorius in consequence of crystal structure

A biophysical elucidation for less toxicity of Agglutinin than Abrin-a from the Seeds of Abrus Precatorius in consequence of crystal structure

Abrin Toxicity and Bioavailability after Temperature and pH Treatment

Detection of Abrin-Like and Prepropulchellin-Like Toxin Genes and Transcripts Using Whole Genome Sequencing and Full-Length Transcript Sequencing of Abrus precatorius

Contact Info

Product

Resources

About