Abstract
Prokaryotic proteins with extended collagen domain are found in many bacterial species that are pathogenic to humans and animals. The collagen domain is often fused to additional ligand-binding domains and plays both structural and functional roles in modular “bacterial collagens.” Here, we describe the step-by-step expression and purification of the recombinant streptococcal collagen-like proteins, rScl, using the Strep-tag II system. The integrity and structural characterization of recombinant collagen-like proteins is very important for defining their function.
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Acknowledgments
We are grateful to all previous and current members of Lukomski’s laboratory for their contributions to the development of the methods and protocols presented here. We also thank our numerous collaborators, especially Doug Keene for performing rotary shadowing and EM imaging over the years. This work was supported by NIH grants AI50666 and AI083683, as well as West Virginia University HSC Bridge Grant Funding to S.L.
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Lukomski, S., McNitt, D.H. (2020). Expression and Purification of Collagen-Like Proteins of Group A Streptococcus. In: Proft, T., Loh, J. (eds) Group A Streptococcus. Methods in Molecular Biology, vol 2136. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0467-0_12
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DOI: https://doi.org/10.1007/978-1-0716-0467-0_12
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