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Miyanaga, K.

Publications and source records attributed to Miyanaga, K..

5 recordsLinked to original sources

A Novel Metric for Quantifying the Sustainability of Phage-Mediated Bacterial Suppression

The global spread of antimicrobial-resistant (AMR) bacteria represents one of the greatest threats to modern medicine, making the development of novel therapeutic strategies increasingly urgent. Phage therapy, which exploits bacteriophages (phages, viruses that specifically infect and kill bacteria) has regained attention as a therapeutic approach for multidrug-resistant infections. One critical determinant of treatment outcome is the capacity of phages to sustain bacterial growth suppression; however, no metric has previously existed to directly quantify the duration of effective lytic activity. Here, we propose the Sustainability Index (SusI), a novel metric that quantifies both the duration and extent of phage-mediated bacterial growth suppression, which is restricted to the primary lysis period from lysis initiation to resistance emergence. Evaluation of individual phages and two-phage cocktails against both laboratory and clinical isolates of Escherichia coli demonstrated that SusI provides information independent of the Virulence Index, which primarily reflects bactericidal activity during the initial phase of infection, and serves as a complementary metric to the Suppression Index, which may incorporate behavior beyond primary lysis. Cocktails composed of phages targeting different receptors specificities consistently exhibited higher SusI values, consistent with the notion that multifaceted selective pressure delays resistance emergence. Furthermore, in a mouse model of systemic infection established by intraperitoneal administration, cocktails with higher SusI values demonstrated superior therapeutic efficacy. These results confirm SusI as a practical metric for rational phage cocktail design. As phage therapy advances toward clinical implementation, standardized quantitative metrics such as SusI are expected to facilitate evidence-based selection of therapeutic phages across diverse pathogens and infection conditions. ImportanceThe global spread of antimicrobial-resistant bacteria is making bacterial infections increasingly difficult to treat. Phage therapy, which uses bacteriophages (viruses that specifically infect bacteria), has re-emerged as a therapeutic alternative; however, reliable methods to determine in advance which phages will be therapeutically effective remain limited. Current evaluation metrics are well-suited for quantifying how rapidly phages kill bacteria but were not designed to directly measure how long lytic activity is sustained before resistant bacteria emerge. Here, we developed the Sustainability Index (SusI), a novel metric that specifically quantifies the duration of effective bacterial growth suppression. Evaluation of multiple phages and their combinations (cocktails) against both laboratory and clinical bacterial isolates demonstrated that SusI can distinguish phage combinations that existing metrics fail to differentiate. Moreover, in a mouse model of lethal bacterial infection, higher SusI values correlated with improved therapeutic outcomes. SusI has potential as a practical tool for selecting phages with greater likelihood of therapeutic success.

microbiology↗

Cell-autonomous thermogenesis of macrophage alters its antibacterial function

Dynamic temperature gradients exist across the bodies of endothermic animals, from the core to peripheral organ, resulting in the physiological cold environment in superficial regions. Consequently, macrophages distributed throughout the body must be able to adapt not only to thermoneutral conditions but also to colder environments. In fact, it is known that environmental temperature influences macrophage immune responses. However, the thermo-responsive mechanisms of macrophage have been largely unexplored. Here we show that macrophage themselves maintains intracellular temperature under physiological cold condition by increasing proton leak index (defined as mitochondrial proton leak per spare respiratory capacity). We further identified a contribution of ADP/ATP carrier (AAC) to this increase in proton leak index. This cell-autonomous thermogenesis pathway, which does not depend on neural or hormonal inputs, highlights the potential for local and organ-specific temperature regulation. Moreover, cold stress reduced mitochondrial membrane potential, which in turn suppressed the expression of the antimicrobial peptide Resistin-like molecule alpha (RETNLA) and diminished antibacterial properties. Together, these findings suggest that macrophages generate heat whereas compromising antibacterial properties, thereby increasing susceptibility to bacterial infection in physiological cold environment. This adaptation mechanism may underscore the important role of temperature homeostasis in non-adipocyte cells.

physiology↗

Selective bacteriophages reduce the emergence of resistant bacteria in the bacteriophage-antibiotic combination therapy

Escherichia coli O157:H7 is a globally important foodborne pathogen that affects food safety. Antibiotic administration against O157:H7 may contribute to the exacerbation of hemolytic uremic syndrome (HUS) and antibiotic-resistant strains increase; therefore, bacteriophage therapy (phage therapy) is considered a useful alternative. In the treatment of resistant bacterial infections, combination therapy with bacteriophages and antibiotics, taking advantage of the benefits of both agents, has been suggested to be effective in inhibiting the emergence of antimicrobial-resistant strains; however, its effectiveness against O157:H7 is not well understood. In this study, we isolated SP015, a phage that infects O157:H7, and compared the combined effect of the bacteriophage and fosfomycin (FOM) with that of the PP01 phage. Genomic analysis revealed that FOM exerts its antibacterial activity through glycerol-3-phosphate transporter (GlpT) and hexose phosphate transporter (UhpT) proteins, and the receptors of PP01 and SP015 phages are the outer membrane protein C (OmpC) and ferrichrome outer membrane transporter protein (FhuA), respectively. Experiments with knockout strains have suggested that FOM also uses OmpC, the receptor for PP01, as a transporter. This may explain why the combination treatment with PP01 resulted in a faster emergence of resistance than the combination treatment with SP015. We propose that phage-antibiotic combination therapy requires careful selection of the phage to be used.

microbiology↗

Analysis host-recognition mechanism of staphylococcal kayvirus phiSA039 reveals a novel strategy that protects Staphylococcus aureus against infection by Staphylococcus pseudintermedius Siphoviridae phages

Following the emergence of antibiotic resistant bacteria such as methicillin-resistant Staphylococcus aureus (MRSA) and methicillin-resistant Staphylococcus pseudintermedius (MRSP), phage therapy has attracted significant attention as an alternative to antibiotic treatment. Bacteriophages belonging to kayvirus (previously known as Twort-like phages) have broad host range and are strictly lytic in Staphylococcus spp. Previous work revealed that kayvirus {phi}SA039 has a host-recognition mechanism distinct from those of other known kayviruses: most of kayviruses use the backbone of wall teichoic acid (WTA) as their receptor; by contrast, {phi}SA039 uses the {beta}-N-acetylglucosamine ({beta}-GlcNAc) residue in WTA. In this study, we found that {phi}SA039 could switch its receptor to be able to infect S. aureus lacking the {beta}-GlcNAc residue by acquiring a spontaneous mutation in open reading frame (ORF) 100 and ORF102. Moreover, {phi}SA039 could infect S. pseudintermedius, which has a different WTA structure than S. aureus. By comparison with newly isolated S. pseudintermedius-specific phage (SP phages), we determined that glycosylation in WTA of S. pseudintermedius is essential for adsorption of SP phages, but not {phi}SA039. Finally, we describe a novel strategy of S. aureus which protects the bacteria from infection of SP phages. Notably, glycosylation of ribitol phosphate (RboP) WTA by TarM or/and TarS prevents infection of S. aureus by SP phages. These findings could help to establish a new strategy for treatment of S. aureus and S. pseudintermedius infection, as well as provide valuable insights into the biology of phage-host interactions.

microbiology↗

Analysis of phage-resistant mechanisms in Staphylococcus aureus SA003 reveals a different binding mechanism for the closely related Twort-like phages phiSA012 and phiSA039

We have previously generated strains of Staphylococcus aureus SA003 resistant to its specific phage {phi}SA012 through long-term coevolution experiment. However, the DNA mutations responsible for the phenotypic change of phage resistance are unknown. Whole-genome analysis revealed six genes that acquired unique point mutations: five missense mutations and one nonsense mutation. Moreover, one deletion, 1.779-bp, resulted in the deletion of the genes encoding glycosyltransferase, TarS, and iron-sulfure repair protein, ScdA. The deletion occurred from the second round of coculture (SA003R2) and remained through the last round. The {phi}SA012 infection toward SA003R2 had decreased to 79.77{+/-}7.50% according to plating efficiency. Complementation of the phage-resistant strain by the wild-type allele showed two mutated host genes were linked to the inhibition of post-adsorption, and five genes were linked to phage adsorption of {phi}SA012. Unlike {phi}SA012, infection by {phi}SA039, a close relative of {phi}SA012, onto SA003R2 was impaired drastically. Complementation of SA003R2 by wild-type tarS restores the infectivity of {phi}SA039. Thus, we concluded that {phi}SA039 requires {beta}-GlcNAc in Wall Teichoic Acid (WTA) for its binding. In silico analysis of the {phi}SA039 genome revealed that several proteins in the tail and baseplate region were different from {phi}SA012; notably the partial deletion of orf96 of {phi}SA039, a homolog of orf99 of {phi}SA012. Orf100 of {phi}SA039, a homolog of Orf103 of {phi}SA012, a previously reported receptor binding protein (RBP), had low similarity (86%) to that of {phi}SA012. The difference in tail and baseplate proteins might be the factor for specificity difference between {phi}SA012 and {phi}SA039.

microbiology↗