Spider silk Escherichia coli

A particularly well studied example of functional amyloid is provided by Curli assembly (53). Curli amyloids are assembled by bacteria such as Escherichia coli and Salmonella. Once assembled on the extracellular surface, Curli amyloid fibers function as natural ceU adhesion molecules that link together bacterial cells into robust cellular networks of biofilms. Other examples of functional amyloids include the silk fibers observed commonly in spider webs the Chorion proteins of egg shells Factor XII, which is an activator of the hemostatic system and other naturally produced adhesives and materials (54). 

Xia, X.-X. et al (2010) Native-sized recombinant spider silk protein produced in metabolically engineered Escherichia coli results in a strong fiber. Proc. Nad. Acad. Sci. U.S.A., 107, 14059-14063. 

Arcidiacono, S. Mello, C. Kaplan, D.L. Cheley, S. Bayley, H. Purification and characterization of recombinant spider silk expressed in Escherichia coli. Appl Microbiol Biot. 49 31-38 (1998). 

The expression of silk proteins in heterologous hosts will ultimately enable the large-scale production of silk protein, and application-spedfic variants thereof. To date, there have been many attempts to aeate recombinant systems that express silk proteins using hosts, such as Escherichia coli, yeast, insect cells, mammalian cells, plants, and even the expression of spider silk-like proteins in silkworm glands. Most efforts have been toward the expression of silk-like fragments or attempts to stitch together consensus... 

Arcidiacono S, et al. (1998) Purification and Characterization of Recombinant Spider Silk Expressed in Escherichia coli. Appl. microbiol. biotechnol. 49 p. 31-8. 

Fahnestock, S.R., Irwin, S.L., 1997. Synthetic spider dragline silk proteins and their production in Escherichia coli. Appl. Microbiol. Biotechnol. 47, 23—32. 

The potential use of spider silk as a new biomaterial has led to the evaluation of various heterologous expression systems for the production of recombinant spider silk-like proteins [65]. Partial cDNA constructs of dragline silk protein were cloned and expressed in Escherichia coli [66], mammalian cell lines (MAC-T/bovine and BHK (baby hamster kidney)/hamster) [67], insect-cell lines [68, 69], and transgenic silkworm larvae [69]. Designer synthetic genes based on Nephila clavipes spider dragline and fiagdliform protein sequences have also been expressed in E. coli... 

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