An ester bond underlies the mechanical strength of a pathogen surface protein

Hai Lei, Quan Ma, Wenfei Li, Jing Wen, Haibo Ma, Meng Qin, Wei Wang and Yi Cao ()
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Hai Lei: Nanjing University
Quan Ma: Nanjing University
Wenfei Li: Nanjing University
Jing Wen: Nanjing University
Haibo Ma: Nanjing University
Meng Qin: Nanjing University
Wei Wang: Nanjing University
Yi Cao: Nanjing University

Nature Communications, 2021, vol. 12, issue 1, 1-12

Abstract: Abstract Gram-positive bacteria can resist large mechanical perturbations during their invasion and colonization by secreting various surface proteins with intramolecular isopeptide or ester bonds. Compared to isopeptide bonds, ester bonds are prone to hydrolysis. It remains elusive whether ester bonds can completely block mechanical extension similarly to isopeptide bonds, or whether ester bonds dissipate mechanical energy by bond rupture. Here, we show that an ester-bond containing stalk domain of Cpe0147 is inextensible even at forces > 2 nN. The ester bond locks the structure to a partially unfolded conformation, in which the ester bond remains largely water inaccessible. This allows the ester bond to withstand considerable mechanical forces and in turn prevent complete protein unfolding. However, the protecting effect might be reduced at non-physiological basic pHs or low calcium concentrations due to destabilizing the protein structures. Inspired by this design principle, we engineer a disulfide mutant resistant to mechanical unfolding under reducing conditions.

Date: 2021
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DOI: 10.1038/s41467-021-25425-6

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