Assessment of prokaryotic collagen-like sequences derived from streptococcal Scl1 and Scl2 proteins as a source of recombinant GXY polymers

Runlin Han, Antoni Zwiefka, Clayton C. Caswell, Yi Xu, Douglas R. Keene, Ewa Lukomska, Zhihong Zhao, Magnus Höök, Slawomir Lukomski

Research output: Contribution to journalArticle

62 Scopus citations

Abstract

Collagen triple helix, composed of the repeating Gly-Xaa-Yaa (GXY) sequence, is a structural element found in all multicellular animals and also in some prokaryotes. Long GXY polymers are highly regarded components used in food, cosmetic, biomedical, and pharmaceutical industries. In this study, we explore a new concept for the production of recombinant GXY polymers which are based on the sequence of "prokaryotic collagens", the streptococcal collagen-like proteins Scl1 and Scl2. Analysis of 50 Scl variants identified the amino acid distribution and GXY-repeat usage that are involved in the stabilization of the triple helix in Scls. Using circular dichroism spectroscopy and electron microscopy, we show that significantly different recombinant rScl polypeptides form stable, unhydroxylated homotrimeric triple helices that can be produced both intra- and extracellularly in the Escherichia coli. These rScl constructs containing 20 to 129 GXY repeats had mid-point melting temperatures between 32 and 39°C. Altogether, Scl-derived collagens, which are different from the mammalian collagens, can form stable triple helices under physiological conditions and can be used for the production of recombinant GXY polymers with a wide variety of potential applications.

Original languageEnglish (US)
Pages (from-to)109-115
Number of pages7
JournalApplied Microbiology and Biotechnology
Volume72
Issue number1
DOIs
StatePublished - Aug 2006

ASJC Scopus subject areas

  • Biotechnology
  • Applied Microbiology and Biotechnology

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