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.
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http://dx.doi.org/10.1002/pro.3363 | DOI Listing |
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 PDFInt 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 PDFMol 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:
Curr Pharm Biotechnol
August 2024
Department of Medical Biotechnology, School of Advanced Technologies in Medicine, Tehran University of Medical Sciences, Tehran, Iran.
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 PDFProc Natl Acad Sci U S A
August 2024
Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720.
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.
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