Successful refolding and NMR structure of rMagi3: A disulfide-rich insecticidal spider toxin.

Protein Sci

Departamento de Química de Biomacromoléculas, Instituto de Química, Universidad Nacional Autónoma de México, CU, Ciudad de México, 04510, México.

Published: March 2018

AI Article Synopsis

  • The search for targeted insecticides is turning to spider venoms, which contain toxins evolved to selectively target insects.
  • In 2003, researchers isolated a group of toxins from the spider Macrothele gigas and identified their amino acid sequences.
  • One purified toxin, rMagi3, has shown to effectively target insects without harming mice, indicating its potential as a specific insecticide.

Article Abstract

The need for molecules with high specificity against noxious insects leads the search towards spider venoms that have evolved highly selective toxins for insect preys. In this respect, spiders as a highly diversified group of almost exclusive insect predators appear to possess infinite potential for the discovery of novel insect-selective toxins. In 2003, a group of toxins was isolated from the spider Macrothele gigas and the amino acid sequence was reported. We obtained, by molecular biology techniques in a heterologous system, one of these toxins. Purification process was optimized by chromatographic methods to determine the three-dimensional structure by nuclear magnetic resonance in solution, and, finally, their biological activity was tested. rMagi3 resulted to be a specific insect toxin with no effect on mice.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5818767PMC
http://dx.doi.org/10.1002/pro.3363DOI Listing

Publication Analysis

Top Keywords

successful refolding
4
refolding nmr
4
nmr structure
4
structure rmagi3
4
rmagi3 disulfide-rich
4
disulfide-rich insecticidal
4
insecticidal spider
4
spider toxin
4
toxin molecules
4
molecules high
4

Similar Publications

Biophysical characterization and structural insights of leptospiral complement regulator-acquiring protein A.

Biochem Biophys Res Commun

December 2024

Laboratory of Structural Biology, Department of Biochemistry, School of Life Sciences, University of Hyderabad, Prof. CR Rao Road, Gachibowli, Hyderabad, Telangana, 500046, India. Electronic address:

Many pathogens establish a successful infection by evading the host complement system, an essential arm of innate immunity. Pathogenic Leptospira is reported to escape complement-mediated killing by recruiting the host complement regulators by lipoproteins or outer surface proteins. One of the outer surface proteins, Leptospiral complement regulator-acquiring protein A (LcpA), is known to recruit complement regulators, C4b-binding protein (C4BP), and Factor H (FH) on the bacterial surface.

View Article and Find Full Text PDF

Refolding dynamics and immunoinformatic insights into Vibrio cholerae OmpA, OmpK, and OmpV for vaccine applications.

Int J Biol Macromol

December 2024

Department of Biosciences and Biomedical Engineering, Indian Institute of Technology, Indore, Simrol, Khandwa Road, Indore 453552, India. Electronic address:

OmpA, OmpK, and OmpV are crucial for the pathogenesis of Vibrio cholerae, functioning within the bacterium's outer membrane; they present significant potential as candidates for vaccine development. Due to their intrinsic β-sheet richness, these OMPs tend to form inclusion bodies whenever overexpression is attempted. To achieve a native-like structure, detergents can be utilized during the refolding of OMPs from inclusion bodies.

View Article and Find Full Text PDF

Super Enhanced Purification of Denatured-Refolded Ubiquitinated Proteins by ThUBD Revealed Ubiquitinome Dysfunction in Liver Fibrosis.

Mol Cell Proteomics

November 2024

State Key Laboratory of Medical Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences Beijing, Research Unit of Proteomics & Research and Development of New Drug of Chinese Academy of Medical Sciences, Institute of Lifeomics, Beijing, PR China; School of Basic Medical, Anhui Medical University, Heifei, Anhui, PR China; College of Chemistry and Materials Science, Hebei University, Baoding, Hebei, PR China. Electronic address:

Article Synopsis
  • * The study introduces a new method called denatured-refolded ubiquitinated sample preparation (DRUSP) combined with a tandem hybrid ubiquitin-binding domain (UBD), resulting in nearly three times stronger ubiquitin signals and a 10-fold improvement in protein enrichment compared to standard methods.
  • * DRUSP enhances the stability and reproducibility of ubiquitinomics, successfully applied to analyze early liver fibrosis in mice, providing valuable insights into liver disease research.
View Article and Find Full Text PDF

Objective: The anticancer properties of recombinant α-luffin (LUF) are wellestablished. However, the cytotoxic effects of encapsulating LUF within niosomes on the SKBR3 breast cancer cell line have yet to be explored. Our study aimed to investigate whether this encapsulation strategy could improve cytotoxic effects.

View Article and Find Full Text PDF

Protein folding in the cell often begins during translation. Many proteins fold more efficiently cotranslationally than when refolding from a denatured state. Changing the vectorial synthesis of the polypeptide chain through circular permutation could impact functional, soluble protein expression and interactions with cellular proteostasis factors.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!