Tail Fiber Research Articles

Wavelength modulation‐based active laser heterodyne spectroscopy for standoff gas detection

AbstractThe wavelength modulation‐active laser heterodyne spectroscopy (WM‐ALHS), which introduces wavelength modulation technique into active laser heterodyne spectroscopy, is reported to enhance the gas standoff detection capability of weak return optical power. The ALHS gas standoff detection system is developed using a 1.65 μm butterfly packaged distributed feedback laser with tail fiber and an all‐fiber structure, which successfully detects methane concentrations at a distance of 35 cm using an aluminum plate as the reflective surface. Allan variance analysis shows that the system has good stability, and the detection limit at 29.2 s integration time is 0.84 ppm m. Standoff detection experiments with direct absorption‐active laser heterodyne spectroscopy (DA‐ALHS) and wavelength modulation spectroscopy (WMS) are carried out on the basis of the WM‐ALHS system and the detection limits of 4.49 and 1.64 ppm m were achieved within integration times of 18.6 and 29 s for DA‐ALHS and WMS, respectively. The superiority of the WM‐ALHS method compared to these two spectral detection methods is demonstrated. Furthermore, the feasibility of applying WM‐ALHS to gas standoff detection has been verified, laying the foundation for the development of this spectroscopic technology.

Bioinformatic Analysis of a Set of 14 Temperate Bacteriophages Isolated from Staphylococcus aureus Strains Highlights Their Massive Genetic Diversity.

ABSTRACTEpidemiology and virulence studies of Staphylococcus aureus showed that temperate bacteriophages are one of the most powerful drivers for its evolution not only because of their abundance but also because of the richness of their genetic payload. Here, we report the isolation, genome sequencing, and bioinformatic analysis of 14 bacteriophages induced from lysogenic S. aureus strains from human or veterinary (cattle) origin. The bacteriophages belonged to the Siphoviridae family; were of similar genome size (40 to 45 kbp); and fell into clusters B2, B3, B5, and B7 according to a recent clustering proposal. One of the phages, namely, vB_SauS_308, was the most unusual one, belonging to the sparsely populated subcluster B7 but showing differences in protein family contents compared with the rest of the members. This phage contains a type I endolysin (one catalytic domain and noncanonical cell wall domain [CBD]) and a host recognition module lacking receptor binding protein, cell wall hydrolase, and tail fiber proteins. This phage also lacked virulence genes, which is opposite to what has been reported for subcluster B6 and B7 members. None of six phages, taken as representatives of each of the four subclusters, showed activity on coagulase-negative staphylococci (excepted for two Staphylococcus hominis strains in which propagation and a very slow adsorption rate were observed) nor transducing ability. Immunity tests on S. aureus RN4220 lysogens with each of these phages showed no cross immunity.IMPORTANCE To the best of our knowledge, this set of sequenced bacteriophages is the largest one in South America. Our report describes for the first time the utilization of MultiTwin software to analyze the relationship between phage protein families. Notwithstanding the fact that most of the genetic information obtained correlated with recently published information, due to their geographical origin, the reported analysis adds up to and confirms currently available knowledge of Staphylococcus aureus temperate bacteriophages in terms of phylogeny and role in host evolution.

Morphological and Genetic Characterization of Eggerthella lenta Bacteriophage PMBT5.

Eggerthella lenta is a common member of the human gut microbiome. We here describe the isolation and characterization of a putative virulent bacteriophage having E. lenta as host. The double-layer agar method for isolating phages was adapted to anaerobic conditions for isolating bacteriophage PMBT5 from sewage on a strictly anaerobic E. lenta strain of intestinal origin. For this, anaerobically grown E. lenta cells were concentrated by centrifugation and used for a 24 h phage enrichment step. Subsequently, this suspension was added to anaerobically prepared top (soft) agar in Hungate tubes and further used in the double-layer agar method. Based on morphological characteristics observed by transmission electron microscopy, phage PMBT5 could be assigned to the Siphoviridae phage family. It showed an isometric head with a flexible, noncontractile tail and a distinct single 45 nm tail fiber under the baseplate. Genome sequencing and assembly resulted in one contig of 30,930 bp and a mol% GC content of 51.3, consisting of 44 predicted protein-encoding genes. Phage-related proteins could be largely identified based on their amino acid sequence, and a comparison with metagenomes in the human virome database showed that the phage genome exhibits similarity to two distantly related phages.

Isolation and characterization of two homolog phages infecting Pseudomonas aeruginosa

Bacteriophages (phages) are capable of infecting specific bacteria, and therefore can be used as a biological control agent to control bacteria-induced animal, plant, and human diseases. In this study, two homolog phages (named PPAY and PPAT) that infect Pseudomonas aeruginosa PAO1 were isolated and characterized. The results of the phage plaque assay showed that PPAT plaques were transparent dots, while the PPAY plaques were translucent dots with a halo. Transmission electron microscopy results showed that PPAT (65 nm) and PPAY (60 nm) strains are similar in size and have an icosahedral head and a short tail. Therefore, these belong to the short-tailed phage family Podoviridae. One-step growth curves revealed the latent period of 20 min and burst time of 30 min for PPAT and PPAY. The burst size of PPAT (953 PFUs/infected cell) was higher than that of PPAY (457 PFUs/infected cell). Also, the adsorption rate constant of PPAT (5.97 × 10−7 ml/min) was higher than that of PPAY (1.32 × 10−7 ml/min) at 5 min. Whole-genome sequencing of phages was carried out using the Illumina HiSeq platform. The genomes of PPAT and PPAY have 54,888 and 50,154 bp, respectively. Only 17 of the 352 predicted ORFs of PPAT could be matched to homologous genes of known function. Likewise, among the 351 predicted ORFs of PPAY, only 18 ORFs could be matched to genes of established functions. Homology and evolutionary analysis indicated that PPAT and PPAY are closely related to PA11. The presence of tail fiber proteins in PPAY but not in PPAT may have contributed to the halo effect of its plaque spots. In all, PPAT and PPAY, newly discovered P. aeruginosa phages, showed growth inhibitory effects on bacteria and can be used for research and clinical purposes.

Engineering Phage Tail Fiber Protein as a Wide-Spectrum Probe for Acinetobacter baumannii Strains with a Recognition Rate of 100.

As a multidrug-resistant pathogen, Acinetobacter baumannii has long been identified as one of the most common nosocomial bacteria. High-performance recognition probes for wide-spectrum detection of A. baumannii are highly desired to achieve efficient diagnosis and timely treatment of infectious diseases induced by this pathogen. An engineering tail fiber protein (ETFP) named as Gp50 encoded by lytic phage Abp9 was expressed in Escherichia coli and identified as a binding protein for A. baumannii. According to the results of genome sequencing of an A. baumannii wild strain and phage-resistant strains, the binding receptor of ETFP Gp50 is inferred to be a lipopolysaccharide distributed on the bacterial surface. The engineering protein did not show lytic activity to A. baumannii, which facilitates the development of reliable diagnosis kits and biosensors with high flexibility and low false-negative rate. The results of specificity study show that ETFP Gp50 is a species-specific binding protein with a recognition rate of 100% for all tested 77 A. baumannii strains, while that of the natural phage Abp9 is only 27.3%. With the engineering protein, a fluorescence method was developed to detect A. baumannii with a detection range of 2.0 × 102 to 2.0 × 108 cfu mL-1. The method has been used for the quantification of A. baumannii in a diverse sample matrix with acceptable reliability. The work demonstrates the application potential of ETFP Gp50 as an ideal recognition probe for rapid screening of A. baumannii strains in a complicated sample matrix.

Phage long tail fiber protein-immobilized magnetic nanoparticles for rapid and ultrasensitive detection of Salmonella

There is an urgent need to develop fast and sensitive detection methods for foodborne pathogens. But the conventional culture method that typically requires 2–3 days is not ideal for the rapid analysis. Food samples demonstrate a great challenge for direct detection due to the complex matrix. Hence, we present a new method based on the phage long-tail-fiber proteins (LTF4-a) immobilized magnetic nanoparticles (MNPs) for specific separation and concentration of Salmonella. The LTF4-a-MNP was prepared via the coupling of recombinant LTF4-a with MNPs and used to isolate and enrich Salmonella cells from contaminated food samples. The captured material was further integrated with the direct PCR program for accurate detection of Salmonella. Our study successfully established a new method for detecting contaminated food samples of Salmonella, the overall approach took no more than 3 h, which allowed a detection limit of 7 CFU/mL, demonstrating a promising alternative to the immunomagnetic separation method by replacing antibodies or aptamers, that is compatible with downstream analysis.

The Specific Capsule Depolymerase of Phage PMK34 Sensitizes Acinetobacter baumannii to Serum Killing.

The rising antimicrobial resistance is particularly alarming for Acinetobacter baumannii, calling for the discovery and evaluation of alternatives to treat A. baumannii infections. Some bacteriophages produce a structural protein that depolymerizes capsular exopolysaccharide. Such purified depolymerases are considered as novel antivirulence compounds. We identified and characterized a depolymerase (DpoMK34) from Acinetobacter phage vB_AbaP_PMK34 active against the clinical isolate A. baumannii MK34. In silico analysis reveals a modular protein displaying a conserved N-terminal domain for anchoring to the phage tail, and variable central and C-terminal domains for enzymatic activity and specificity. AlphaFold-Multimer predicts a trimeric protein adopting an elongated structure due to a long α-helix, an enzymatic β-helix domain and a hypervariable 4 amino acid hotspot in the most ultimate loop of the C-terminal domain. In contrast to the tail fiber of phage T3, this hypervariable hotspot appears unrelated with the primary receptor. The functional characterization of DpoMK34 revealed a mesophilic enzyme active up to 50 °C across a wide pH range (4 to 11) and specific for the capsule of A. baumannii MK34. Enzymatic degradation of the A. baumannii MK34 capsule causes a significant drop in phage adsorption from 95% to 9% after 5 min. Although lacking intrinsic antibacterial activity, DpoMK34 renders A. baumannii MK34 fully susceptible to serum killing in a serum concentration dependent manner. Unlike phage PMK34, DpoMK34 does not easily select for resistant mutants either against PMK34 or itself. In sum, DpoMK34 is a potential antivirulence compound that can be included in a depolymerase cocktail to control difficult to treat A. baumannii infections.

Characterization of Three Novel Virulent Aeromonas Phages Provides Insights into the Diversity of the Autographiviridae Family.

In this study, we isolated and characterized three novel virulent Autographiviridae bacteriophages, vB_AspA_Bolek, vB_AspA_Lolek, and vB_AspA_Tola, which infect different Aeromonas strains. These three host–pathogen pairs were derived from the same sampling location—the arsenic-containing microbial mats of the Zloty Stok gold mine. Functional analysis showed they are psychrotolerant (4–25 °C), albeit with a much wider temperature range of propagation for the hosts (≤37 °C). Comparative genomic analyses revealed a high nucleotide and amino acid sequence similarity of vB_AspA_Bolek and vB_AspA_Lolek, with significant differences exclusively in the C-terminal region of their tail fibers, which might explain their host range discrimination. The protein-based phage network, together with a phylogenetic analysis of the marker proteins, allowed us to assign vB_AspA_Bolek and vB_AspA_Lolek to the Beijerinckvirinae and vB_AspA_Tola to the Colwellvirinae subfamilies, but as three novel species, due to their low nucleotide sequence coverage and identity with other known phage genomes. Global comparative analysis showed that the studied phages are also markedly different from most of the 24 Aeromonas autographiviruses known so far. Finally, this study provides in-depth insight into the diversity of the Autographiviridae phages and reveals genomic similarities between selected groups of this family as well as between autographiviruses and their relatives of other Caudoviricetes families.

Identification of a phage-derived depolymerase specific for KL47 capsule of Klebsiella pneumoniae and its therapeutic potential in mice.

Klebsiella pneumoniae is one of the major pathogens causing global multidrug-resistant infections. Therefore, strategies for preventing and controlling the infections are urgently needed. Phage depolymerase, often found in the tail fiber protein or the tail spike protein, is reported to have antibiofilm activity. In this study, phage P560 isolated from sewage showed specific for capsule locus type KL47 K. pneumoniae, and the enlarged haloes around plaques indicated that P560 encoded a depolymerase. The capsule depolymerase, ORF43, named P560dep, derived from phage P560 was expressed, purified, characterized and evaluated for enzymatic activity as well as specificity. We reported that the capsule depolymerase P560dep, can digest the capsule polysaccharides on the surface of KL47 type K. pneumoniae, and the depolymerization spectrum of P560dep matched to the host range of phage P560, KL47 K. pneumoniae. Crystal violet staining assay showed that P560dep was able to significantly inhibit biofilm formation. Further, a single dose (50 μg/mouse) of depolymerase intraperitoneal injection protected 90%–100% of mice from lethal challenge before or after infection by KL47 carbapenem-resistant K. pneumoniae. And pathological changes were alleviated in lung and liver of mice infected by KL47 type K. pneumoniae. It is demonstrated that depolymerase P560dep as an attractive antivirulence agent represents a promising tool for antimicrobial therapy.

Broad host range bacteriophage, EscoHU1, infecting Escherichia coli O157:H7 and Salmonella enterica: Characterization, comparative genomics, and applications in food safety

Shiga toxin-producing Escherichia coli and Salmonella enterica are important pathogens worldwide. Bacteriophages can be effectively used to reduce the incidence of foodborne pathogens. The host recognition systems of phages are highly specific, with the host range of a common phage being limited to the species or strain level. Here, we characterized a novel broad-host-range phage, EscoHU1, that infects several bacterial species, including E. coli and S. enterica, and evaluated its antimicrobial potential to inhibit E. coli O157:H7 and S. Typhimurium growth in food systems. The adsorption of EscoHU1 on E. coli was faster than that on S. Typhimurium; however, the one-step growth curves of EscoHU1 in both species were similar. Genomic analysis of EscoHU1 revealed that this phage has long direct terminal repeats at both ends of the genome, and phylogenetic analysis of the terminase large subunit confirmed that EscoHU1 belongs to the genus Epseptimavirus. Comparative analysis of structural proteins indicated a diversity of proteins related to the host range (receptor-binding proteins and L-shaped tail fibers). Challenge tests using beef and milk demonstrated the antimicrobial effects of EscoHU1 in inhibiting the growth of E. coli O157:H7 and S. Typhimurium in the food system. However, the antimicrobial effect of EscoHU1 on S. Typhimurium was lower than that on E. coli O157:H7. These results suggest that the novel broad-host-range phage EscoHU1 may serve as an effective antimicrobial agent to reduce food poisoning caused by E. coli O157:H7 and S. Typhimurium.

Phenotypic characterization and genome analysis of a novel Salmonella Typhimurium phage having unique tail fiber genes

Salmonella enterica serovar Typhimurium is a foodborne pathogen causing occasional outbreaks of enteric infections in humans. Salmonella has one of the largest pools of temperate phages in its genome that possess evolutionary significance for pathogen. In this study, we characterized a novel temperate phage Salmonella phage BIS20 (BIS20) with unique tail fiber genes. It belongs to the subfamily Peduovirinae genus Eganvirus and infects Salmonella Typhimurium strain (SE-BS17; Acc. NO MZ503545) of poultry origin. Phage BIS20 was viable only at biological pH and temperature ranges (pH7 and 37 °C). Despite being temperate BIS20 significantly slowed down the growth of host strain for 24 h as compared to control (P < 0.009). Phage BIS20 features 29,477-base pair (bp) linear DNA genome with 53% GC content and encodes for 37 putative ORFs. These ORFs have mosaic arrangement as indicated by its ORF similarity to various phages and prophages in NCBI. Genome analysis indicates its similarity to Salmonella enterica serovar Senftenberg prophage (SEStP) sequence (Nucleotide similarity 87.7%) and Escherichia virus 186 (~ 82.4% nucleotide similarity). Capsid genes were conserved however those associated with tail fiber formation and assembly were unique to all members of genus Eganvirus. We found strong evidence of recombination hotspot in tail fiber gene. Our study identifies BIS20 as a new species of genus Eganvirus temperate phages as its maximum nucleotide similarity is 82.4% with any phage in NCBI. Our findings may contribute to understanding of origin of new temperate phages.

The Beauty of Bacteriophage T4 Research: Lindsay W. Black and the T4 Head Assembly.

Viruses are biochemically complex structures and mainly consist of folded proteins that contain nucleic acids. Bacteriophage T4 is one of most prominent examples, having a tail structure that contracts during the infection process. Intracellular phage multiplication leads to separate self-directed assembly reactions of proheads, tails and tail fibers. The proheads are packaged with concatemeric DNA produced by tandem replication reactions of the parental DNA molecule. Once DNA packaging is completed, the head is joined with the tail and six long fibers are attached. The mature particles are then released from the cell via lysis, another tightly regulated process. These processes have been studied in molecular detail leading to a fascinating view of the protein-folding dynamics that direct the structural interplay of assembled complexes. Lindsay W. Black dedicated his career to identifying and defining the molecular events required to form the T4 virion. He leaves us with rich insights into the astonishingly precise molecular clockwork that co-ordinates all of the players in T4 assembly, both viral and cellular. Here, we summarize Lindsay’s key research contributions that are certain to stimulate our future science for many years to come.

Structure of a thylakoid-anchored contractile injection system in multicellular cyanobacteria

Contractile injection systems (CISs) mediate cell–cell interactions by phage tail-like structures, using two distinct modes of action: extracellular CISs are released into the medium, while type 6 secretion systems (T6SSs) are attached to the cytoplasmic membrane and function upon cell–cell contact. Here, we characterized a CIS in the multicellular cyanobacterium Anabaena, with features distinct from extracellular CISs and T6SSs. Cryo-electron tomography of focused ion beam-milled cells revealed that CISs were anchored in thylakoid membrane stacks, facing the cell periphery. Single particle cryo-electron microscopy showed that this unique in situ localization was mediated by extensions of tail fibre and baseplate components. On stress, cyanobacteria induced the formation of ghost cells, presenting thylakoid-anchored CISs to the environment. Functional assays suggest that these CISs may mediate ghost cell formation and/or interactions of ghost cells with other organisms. Collectively, these data provide a framework for understanding the evolutionary re-engineering of CISs and potential roles of these CISs in cyanobacterial programmed cell death.

High-coupling efficiency and robust fusion splicing between fluorotellurite and chalcogenide fibers

We demonstrate a low-loss and high-robustness fusion splicing point between fluorotellurite fiber and arsenic sulfide-based chalcogenide fiber (As2S3) by using an asymmetric fiber splicing technology. The splicing loss of point is less than 0.55 dB at the wavelength of 1.55 μm, and the monitored tension is 129 g by tuning the distance of the fusion splicing head offset in the fusion splicing process. Using an all-fiber testing system, the fusion splicing point loss between the 1.55 μm testing light source tail fiber (silica fiber) and the fluorotellurite fiber is 0.503 dB. The output power from the As2S3 fiber is 0.91 W with a testing light source of 2 W, and the temperature of the splicing joint shows no evident increase. This finding indicates that the fusion splicing point offers excellent beam quality. This work lays a solid foundation for building an all-fiber cascaded system generating mid-infrared supercontinuum with high-coupling efficiency between mid-infrared soft-glass fibers.

Directed Evolution of Replication-Competent Double-Stranded DNA Bacteriophage toward New Host Specificity.

In the fight against antimicrobial resistance, bacteriophages are a promising alternative to antibiotics. However, due to their narrow spectra, phage therapy requires the careful matching between the host and bacteriophage to be effective. Despite our best efforts, nature remains as the only source of novel phage specificity. Directed evolution can potentially open an avenue for engineering phage specificity and improving qualities of phages that are not strongly selected for in their natural environments but are important for therapeutic applications. In this work, we present a strategy that generates large libraries of replication-competent phage variants directly from synthetic DNA fragments, with no restriction on their host specificity. Using the T7 bacteriophage as a proof-of-concept, we created a large library of tail fiber mutants with at least 107 unique variants. From this library, we identified mutants that have broadened specificity as evidenced by their novel lytic activity against Yersinia enterocolitica, a strain that the wild-type T7 was unable to lyse. Using the same concept, mutants with improved lytic efficiency and characteristics, such as lytic condition tolerance and resistance suppression, were also identified. However, the observed limitations in altering host specificity by tail fiber mutagenesis suggest that other bottlenecks could be of equal or even greater importance.

IN VITRO EFFECT OF NEWLY BACTERIOPHAGES ISOLATES AGAINST ESCHERICHIA COLI SEROGROUPS COLLECTED FROM THE LOCAL HOSPITAL LABORATORY; THEIR SPECIFIC CHARACTERIZATION AND IDENTIFICATION

The aim of this study is to isolate a new bacteriophage with lytic effect against several serogroups of Escherichia coli that were isolated from different samples submitted to the local hospital laboratory. These serogroups are the main causative agents of bloodstream and urinary tract infections (UTIs) among Gram-negative bacteria. Three isolates of E. coli were used as a host to isolate phages from a hospital wastewater treatment plant. Eight phages were isolated and only three of them (EC-BSR1, EC-BSR2, and EC-BSR3) were considered for further characterization and identification. The three phages appear to belong to Myoviridae characterized by icosahedral heads, necks and contractile tails with tail fibers. Phage EC-BSR1 and EC-BSR2 had genome sizes of 67.06 and 68.04 kb, respectively. All three phages were lysed 100% of E. coli serogroups that was tested in vitro and 42.7%, 61.7% and 44.7% in vitro lyses of ECOR collection reference. Phages were resistant to pH from 5 to 9, and phage EC-BSR3 appeared to be more resistant than the other two phages to an acidic and alkaline environment. These phages have the pattern of homologous DNA fragments after being digested with Acc1 and EcoR1 restriction enzymes. It was concluded that these phages are highly coli lytic for the E. coli serogroups isolates.

Targeting of Pseudomonas aeruginosa cell surface via GP12, an Escherichia coli specific bacteriophage protein

Bacteriophages are highly abundant molecular machines that have evolved proteins to target the surface of host bacterial cells. Given the ubiquity of lipopolysaccharides (LPS) on the outer membrane of Gram-negative bacteria, we reasoned that targeting proteins from bacteriophages could be leveraged to target the surface of Gram-negative pathogens for biotechnological applications. To this end, a short tail fiber (GP12) from the T4 bacteriophage, which infects Escherichia coli (E. coli), was isolated and tested for the ability to adhere to whole bacterial cells. We found that, surprisingly, GP12 effectively bound the surface of Pseudomonas aeruginosa cells despite the established preferred host of T4 for E. coli. In efforts to elucidate why this binding pattern was observed, it was determined that the absence of the O-antigen region of LPS on E. coli improved cell surface tagging. This indicated that O-antigens play a significant role in controlling cell adhesion by T4. Probing GP12 and LPS interactions further using deletions of the enzymes involved in the biosynthetic pathway of LPS revealed the inner core oligosaccharide as a possible main target of GP12. Finally, we demonstrated the potential utility of GP12 for biomedical applications by showing that GP12-modified agarose beads resulted in the depletion of pathogenic bacteria from solution.

Isolation, characterization, molecular analysis and application of bacteriophage DW-EC to control Enterotoxigenic Escherichia coli on various foods

Among food preservation methods, bacteriophage treatment can be a viable alternative method to overcome the drawbacks of traditional approaches. Bacteriophages are naturally occurring viruses that are highly specific to their hosts and have the capability to lyse bacterial cells, making them useful as biopreservation agents. This study aims to characterize and determine the application of bacteriophage isolated from Indonesian traditional Ready-to-Eat (RTE) food to control Enterotoxigenic Escherichia coli (ETEC) population in various foods. Phage DW-EC isolated from Indonesian traditional RTE food called dawet with ETEC as its host showed a positive result by the formation of plaques (clear zone) in the bacterial host lawn. Transmission electron microscopy (TEM) results also showed that DW-EC can be suspected to belong to the Myoviridae family. Molecular characterization and bioinformatic analysis showed that DW-EC exhibited characteristics as promising biocontrol agents in food samples. Genes related to the lytic cycle, such as lysozyme and tail fiber assembly protein, were annotated. There were also no signs of lysogenic genes among the annotation results. The resulting PHACTS data also indicated that DW-EC was leaning toward being exclusively lytic. DW-EC significantly reduced the ETEC population (P ≤ 0.05) in various food samples after two different incubation times (1 day and 6 days) in chicken meat (80.93%; 87.29%), fish meat (63.78%; 87.89%), cucumber (61.42%; 71.88%), tomato (56.24%; 74.51%), and lettuce (46.88%; 43.38%).

\u03c6YeO3-12 phage tail fiber Gp17 as a promising high specific tool for recognition of Yersinia enterocolitica pathogenic serotype O:3

Yersiniosis is an infectious zoonotic disease caused by two enteropathogenic species of Gram-negative genus Yersinia: Yersinia enterocolitica and Yersinia pseudotuberculosis. Pigs and other wild and domestic animals are reservoirs for these bacteria. Infection is usually spread to humans by ingestion of contaminated food. Yersiniosis is considered a rare disease, but recent studies indicate that it is overlooked in the diagnostic process therefore the infections with this bacterium are not often identified. Reliable diagnosis of Yersiniosis by culturing is difficult due to the slow growth of the bacteria easily overgrown by other more rapidly growing microbes unless selective growth media is used. Phage adhesins recognizing bacteria in a specific manner can be an excellent diagnostic tool, especially in the diagnosis of pathogens difficult for culturing. In this study, it was shown that Gp17, the tail fiber protein (TFP) of phage φYeO3-12, specifically recognizes only the pathogenic Yersinia enterocolitica serotype O:3 (YeO:3) bacteria. The ELISA test used in this work confirmed the specific interaction of this protein with YeO:3 and demonstrated a promising tool for developing the pathogen recognition method based on phage adhesins.

Ckp1 Bacteriophage, a S16-Like Broad-Host-Range Myovirus, Recognizes Citrobacter Koseri Lipopolysaccharide Through its Long Tail Fibers

Ckp1 Bacteriophage, a S16-Like Broad-Host-Range Myovirus, Recognizes Citrobacter Koseri Lipopolysaccharide Through its Long Tail Fibers