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Structure and function of the Ts2631 endolysin of Thermus scotoductus phage vB_Tsc2631 with unique N-terminal extension used for peptidoglycan binding. | LitMetric

AI Article Synopsis

  • Bacteriophages use endolysins like Ts2631 to break down bacterial peptidoglycan for escape after their life cycle, with a focus on thermophilic phages which are less understood.
  • Ts2631, a zinc-dependent amidase, has an active site critical for lysis but not for binding to peptidoglycan; key residues identified include Tyr60 and Lys70 for binding, while His31 and others are essential for enzyme activity.
  • The enzyme features a charged N-terminal extension vital for binding peptidoglycan, with its deletion resulting in a loss of bacteriolytic function, highlighting its potential in developing heat-stable antimicrobial agents.

Article Abstract

To escape from hosts after completing their life cycle, bacteriophages often use endolysins, which degrade bacterial peptidoglycan. While mesophilic phages have been extensively studied, their thermophilic counterparts are not well characterized. Here, we present a detailed analysis of the structure and function of Ts2631 endolysin from thermophilic phage vB_Tsc2631, which is a zinc-dependent amidase. The active site of Ts2631 consists of His30, Tyr58, His131 and Cys139, which are involved in Zn coordination and catalysis. We found that the active site residues are necessary for lysis yet not crucial for peptidoglycan binding. To elucidate residues involved in the enzyme interaction with peptidoglycan, we tested single-residue substitution variants and identified Tyr60 and Lys70 as essential residues. Moreover, substitution of Cys80, abrogating disulfide bridge formation, inactivates Ts2631, as do substitutions of His31, Thr32 and Asn85 residues. The endolysin contains a positively charged N-terminal extension of 20 residues that can protrude from the remainder of the enzyme and is crucial for peptidoglycan binding. We show that the deletion of 20 residues from the N-terminus abolished the bacteriolytic activity of the enzyme. Because Ts2631 exhibits intrinsic antibacterial activity and unusual thermal stability, it is perfectly suited as a scaffold for the development of antimicrobial agents.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6361986PMC
http://dx.doi.org/10.1038/s41598-018-37417-6DOI Listing

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