New Insights on the Feature and Function of Tail Tubular Protein B and Tail Fiber Protein of the Lytic Bacteriophage φYeO3-12 Specific for Yersinia enterocolitica Serotype O:3

Abstract

For the first time, we are introducing TTPBgp12 and TFPgp17 as new members of the tail tubular proteins B (TTPB) and tail fiber proteins (TFP) family, respectively. These proteins originate from Yersinia enterocolitica phage φYeO3-12. It was originally thought that these were structural proteins. However, our results show that they also inhibit bacterial growth and biofilm formation. According to the bioinformatic analysis, TTPBgp12 is functionally and structurally similar to the TTP of Enterobacteria phage T7 and adopts a β-structure. TFPgp17 contains an intramolecular chaperone domain at its C-terminal end. The N-terminus of TFPgp17 is similar to other representatives of the TFP family. Interestingly, the predicted 3D structure of TFPgp17 is similar to other bacterial S-layer proteins. Based on the thermal unfolding experiment, TTPBgp12 seems to be a two-domain protein that aggregates in the presence of sugars such as maltose and N-acetylglucosamine (GlcNAc). These sugars cause two unfolding events to transition into one global event. TFPgp17 is a one-domain protein. Maltose and GlcNAc decrease the aggregation temperature of TFPgp17, while the presence of N-acetylgalactosamine (GalNAc) increases the temperature of its aggregation. The thermal unfolding analysis of the concentration gradient of TTPBgp12 and TFPgp17 indicates that with decreasing concentrations, both proteins increase in stability. However, a decrease in the protein concentration also causes an increase in its aggregation, for both TTPBgp12 and TFPgp17.

φYeO3-12 phage tail fiber Gp17 as a promising high specific tool for recognition of Yersinia enterocolitica pathogenic serotype O:3

“…Their combined mass of 113.088 kDa corresponds to the predicted mass of H/MTFP-Gp17 before autoproteolysis (Additional file 1 : Figures S1 and S2). The autoproteolysis indicates that the C-terminal fragment of TFP-Gp17 is cleaved, supporting our previous observation that TFP-Gp17 contains an S74 peptidase domain, which is responsible for protein autolysis (Pyra et al, 2020 ). Importantly, the results also demonstrated that there are no sterical obstacles for the autoproteolysis in the H/MTFP-Gp17 construct where the His-MBP is fused to the N-terminal end of TFP-Gp17.…”

“…In our previous report, we indicated that two amino sugars GalNAc and GlcNAc stabilize the phage adhesin having impact on increase of its thermal stability (Pyra et al, 2020 ). Initially we thought that this could be due to interaction with the aminosugar moieties presented in the outer core (OC) of YeO:3 (Al-Hendy et al, 1992 ).…”

“…Our previous results suggested that tail fiber protein TFP-Gp17 belonging to φYeO3-12 phage tail fiber contained a chaperone domain on the C-terminus of its polypeptide chain and the adhesion domain on its N-terminus end. The 3D structure of this protein was predicted using the Swiss-Model server suggesting to adopt the tertiary structure as adhesin A (PDB code: 3d9x) (Pyra et al, 2020 ). That might suggest the adhesive feature for this protein.…”

A Lytic Yersina pestis Bacteriophage Obtained From the Bone Marrow of Marmota himalayana in a Plague-Focus Area in China

“…It forms an attachment for tail spikes to mediate infection through sensing the deflection of side fibers upon cell-wall binding. During infection by bacteria, TPPA can bind with bacterial receptors to mediate bacteriophage adsorption and subsequent bacterial lysis ( Hu et al., 2020 ; Pyra et al., 2020a ; Pyra et al., 2020b ). If differences occur specifically in the genes encoding the tail fibers, then recognition of the cell target will change ( Vacheron et al., 2021 ).…”

Recent Advances in the Application of Bacteriophages against Common Foodborne Pathogens

“…Combating yersinosis is a great challenge since numerous representatives of this species have developed resistance to many frontline antibiotics such as penicillin, ampicillin, cephalosporine and macrolides [ 84 ]. Clearance of Yersinia contamination in food and food processing equipment is also difficult due to the ability of this pathogen to form biofilm structures [ 85 ].…”