Moonlighting Functions of Bacterial Fructose 1,6-Bisphosphate Aldolases

Oldfield, Neil J.; Shams, Fariza; Wooldridge, Karl G.; Turner, David P.J.

Abstract

© 2017 John Wiley & Sons, Inc. Moonlighting proteins are multifunctional proteins which perform two or more biochemical functions using a single polypeptide chain. Moonlighting proteins have been documented in diverse organisms, including archaea, bacteria, yeasts, eukaryotic parasites, plants, and vertebrates. Early reports describing the unexpected presence of Fructose 1,6-bisphosphate aldolase (FBA) on the bacterial cell surface resulted from the separation of surface or secreted fractions by gel electrophoresis, and the subsequent identification of proteins by mass spectroscopy or amino-terminal amino acid sequencing. Meningococcal FBA can be found in the cytoplasm and also in the outer membrane. The latter is surface accessible to anti-FBA antibodies in flow cytometry experiments, even in the presence of the meningococcal polysaccharide capsule. Flow cytometry and enzymatic activity measurements revealed that FBA-tb was exported to the cell surface and produced under various axenic growth conditions, including oxygen depletion, and hence by non-replicating bacilli.

Citation

Oldfield, N. J., Shams, F., Wooldridge, K. G., & Turner, D. P. (2017). Moonlighting Functions of Bacterial Fructose 1,6-Bisphosphate Aldolases. In B. Henderson (Ed.), Moonlighting Proteins: Novel Virulence Factors in Bacterial Infections (321-331). Wiley

• Publication Date: 2017-04
• Deposit Date: Aug 2, 2022
• Journal: Moonlighting Proteins: Novel Virulence Factors in Bacterial Infections
• Publisher: Wiley
• Pages: 321-331
• Book Title: Moonlighting Proteins: Novel Virulence Factors in Bacterial Infections
• ISBN: 9781118951118
• Public URL: https://nottingham-repository.worktribe.com/output/3129742
• Related Public URLs: https://www.wiley.com/en-us/Moonlighting+Proteins%3A+Novel+Virulence+Factors+in+Bacterial+Infections-p-9781118951118