BacteriophagePub Date : 2013-07-01Epub Date: 2013-07-26DOI: 10.4161/bact.25697
Joelle Woolston, Adam R Parks, Tamar Abuladze, Bradley Anderson, Manrong Li, Chandi Carter, Leigh Farris Hanna, Serena Heyse, Duane Charbonneau, Alexander Sulakvelidze
{"title":"Bacteriophages lytic for <i><i>Salmonella</i></i> rapidly reduce <i><i>Salmonella</i></i> contamination on glass and stainless steel surfaces.","authors":"Joelle Woolston, Adam R Parks, Tamar Abuladze, Bradley Anderson, Manrong Li, Chandi Carter, Leigh Farris Hanna, Serena Heyse, Duane Charbonneau, Alexander Sulakvelidze","doi":"10.4161/bact.25697","DOIUrl":"https://doi.org/10.4161/bact.25697","url":null,"abstract":"A cocktail of six lytic bacteriophages, SalmoFresh™, significantly (p < 0.05) reduced the number of surface-applied Salmonella Kentucky and Brandenburg from stainless steel and glass surfaces by > 99% (2.1–4.3 log). Both strains were susceptible to SalmoFresh™ in the spot-test assay. Conversely, SalmoFresh™ was unable to reduce surface contamination with a Salmonella Paratyphi B strain that was not susceptible to the phage cocktail in the spot-test assay. However, by replacing two SalmoFresh™ component phages with two new phages capable of lysing the Paratyphi B strain in the spot-test assay, the target range of the cocktail was shifted to include the Salmonella Paratyphi B strain. The modified cocktail, SalmoLyse™, was able to significantly (p < 0.05) reduce surface contamination of the Paratyphi B strain by > 99% (2.1–4.1 log). The data show that both phage cocktails were effective in significantly reducing the levels of Salmonella on hard surfaces, provided the contaminating strains were susceptible in the spot-test (i.e., spot-test susceptibility was indicative of efficacy in subsequent surface decontamination studies). The data also support the concept that phage preparations can be customized to meet the desired antibacterial application.","PeriodicalId":8686,"journal":{"name":"Bacteriophage","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/bact.25697","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31862928","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BacteriophagePub Date : 2013-07-01Epub Date: 2013-07-29DOI: 10.4161/bact.25857
Jeremy J Barr, Merry Youle, Forest Rohwer
{"title":"Innate and acquired bacteriophage-mediated immunity.","authors":"Jeremy J Barr, Merry Youle, Forest Rohwer","doi":"10.4161/bact.25857","DOIUrl":"https://doi.org/10.4161/bact.25857","url":null,"abstract":"<p><p>We recently described a novel, non-host-derived, phage-mediated immunity active at mucosal surfaces, the main site of pathogen entry in metazoans. In that work, we showed that phage T4 adheres to mucus glycoproteins via immunoglobulin-like domains displayed on its capsid. This adherence positions the phage in mucus surfaces where they are more likely to encounter and kill bacteria, thereby benefiting both the phage and its metazoan host. We presented this phage-metazoan symbiosis based on an exclusively lytic model of phage infection. Here we extend our bacteriophage adherence to mucus (BAM) model to consider the undoubtedly more complex dynamics in vivo. We hypothesize how mucus-adherent phages, both lytic and temperate, might impact the commensal microbiota as well as protect the metazoan epithelium from bacterial invasion. We suggest that BAM may provide both an innate and an acquired antimicrobial immunity.</p>","PeriodicalId":8686,"journal":{"name":"Bacteriophage","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/bact.25857","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31862802","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Properties and mutation studies of a bacteriophage-derived chimeric recombinant staphylolytic protein P128: Comparison to recombinant lysostaphin.","authors":"Sanjeev Rajagopalan Saravanan, Vivek Daniel Paul, Shilpa George, Sudarson Sundarrajan, Nirmal Kumar, Madhavi Hebbur, Naveen Kumar, Ananda Veena, Uma Maheshwari, Chemira Biddappa Appaiah, Muralidharan Chidambaran, Anuradha Gopal Bhat, Sukumar Hariharan, Sriram Padmanabhan","doi":"10.4161/bact.26564","DOIUrl":"https://doi.org/10.4161/bact.26564","url":null,"abstract":"<p><p>P128 is a chimeric anti-staphylococcal protein having a catalytic domain from a <i>Staphylococcus</i> bacteriophage K tail associated structural protein and a cell wall targeting domain from the <i>Staphylococcus</i> bacteriocin-lysostaphin. In this study, we disclose additional properties of P128 and compared the same with lysostaphin. While lysostaphin was found to get inactivated by heat and was inactive on its parent strain <i>S. simulans</i> biovar <i>staphylolyticus</i>, P128 was thermostable and was lytic towards <i>S. simulans</i> biovar <i>staphylolyticus</i> demonstrating a difference in their mechanism of action. Selected mutation studies of the catalytic domain of P128 showed that arginine and cysteine, at 40th and 76th positions respectively, are critical for the staphylolytic activity of P128, although these amino acids are not conserved residues. In comparison to native P128, only the R40S mutant (P301) was catalytically active on zymogram gel and had a similar secondary structure, as assessed by circular dichroism analysis and in silico modeling with similar cell binding properties. Mutation of the arginine residue at 40th position of the P128 molecule caused dramatic reduction in the V<sub>max</sub> (∆OD<sub>600</sub> [mg/min]) value (nearly 270 fold) and the recombinant lysostaphin also showed lesser V<sub>max</sub> value (nearly 1.5 fold) in comparison to the unmodified P128 protein. The kinetic parameters such as apparent K<sub>m</sub> (K<sub>m</sub><sup>APP</sup>) and apparent K<sub>cat</sub> (K<sub>cat</sub><sup>APP</sup>) of the native P128 protein also showed significant differences in comparison to the values observed for P301 and lysostaphin.</p>","PeriodicalId":8686,"journal":{"name":"Bacteriophage","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/bact.26564","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31881535","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BacteriophagePub Date : 2013-07-01Epub Date: 2013-10-24DOI: 10.4161/bact.26861
Jochen Klumpp, Martin J Loessner
{"title":"<i>Listeria</i> phages: Genomes, evolution, and application.","authors":"Jochen Klumpp, Martin J Loessner","doi":"10.4161/bact.26861","DOIUrl":"10.4161/bact.26861","url":null,"abstract":"<p><p><i>Listeria</i> is an important foodborne pathogen and the causative agent of Listeriosis, a potentially fatal infection. Several hundred <i>Listeria</i> bacteriophages have been described over the past decades, but only few have actually been characterized in some detail, and genome sequences are available for less than twenty of them. We here present an overview of what is currently known about <i>Listeria</i> phage genomics, their role in host evolution and pathogenicity, and their various applications in biotechnology and diagnostics.</p>","PeriodicalId":8686,"journal":{"name":"Bacteriophage","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3827098/pdf/bact-3-e26861.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31881537","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BacteriophagePub Date : 2013-04-01DOI: 10.4161/bact.25516
Richard Calendar
{"title":"Life in Science: Richard Calendar.","authors":"Richard Calendar","doi":"10.4161/bact.25516","DOIUrl":"https://doi.org/10.4161/bact.25516","url":null,"abstract":"","PeriodicalId":8686,"journal":{"name":"Bacteriophage","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/bact.25516","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31862924","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BacteriophagePub Date : 2013-04-01DOI: 10.4161/bact.24872
Alexandra Henein
{"title":"What are the limitations on the wider therapeutic use of phage?","authors":"Alexandra Henein","doi":"10.4161/bact.24872","DOIUrl":"10.4161/bact.24872","url":null,"abstract":"<p><p>Bacterial resistance to antibiotics poses a serious health threat. Since research into new antibiotics is not progressing at the same rate as the development of bacterial resistance, widespread calls for alternatives to antibiotics have been made. Phage therapy is an ideal alternative candidate to be investigated. However the success of phage therapy may be hampered by a lack of investment support from large pharmaceutical companies, due to their narrow spectrum of activity in antibiotics, very large costs associated with clinical trials of the variety of phages needed, and regulatory requirements remaining unclear. Intellectual property is difficult to secure for therapeutic phage products for a variety of reasons, and patenting procedures vary widely between the US and the EU. Consequently, companies are more likely to invest in phage products for decontamination or veterinary use, rather than clinical use in humans. Some still raise questions as to the safety of phage therapy overall, suggesting the possibility of cytotoxicity and immunogenicity, depending on the phage preparation and route. On the other hand, with patients dying because of infections untreatable with conventional antibiotics, the question arises as to whether it is ethical not to pursue phage therapy more diligently. A paradigm shift about how phage therapy is perceived is required, as well as more rigorous proof of efficacy in the form of clinical trials of existing medicinal phage products. Phage therapy potential may be fulfilled in the meantime by allowing individual preparations to be used on a named-patient basis, with extensive monitoring and multidisciplinary team input. The National Health Service and academia have a role in carrying out clinical phage research, which would be beneficial to public health, but not necessarily financially rewarding.</p>","PeriodicalId":8686,"journal":{"name":"Bacteriophage","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/02/c2/bact-3-e24872.PMC3821673.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31862922","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BacteriophagePub Date : 2013-04-01DOI: 10.4161/bact.25518
Manan Sharma
{"title":"Lytic bacteriophages: Potential interventions against enteric bacterial pathogens on produce.","authors":"Manan Sharma","doi":"10.4161/bact.25518","DOIUrl":"10.4161/bact.25518","url":null,"abstract":"<p><p>Foodborne illnesses resulting from the consumption of produce commodities contaminated with enteric pathogens continue to be a significant public health issue. Lytic bacteriophages may provide an effective and natural intervention to reduce bacterial pathogens on fresh and fresh-cut produce commodities. The use of multi-phage cocktails specific for a single pathogen has been most frequently assessed on produce commodities to minimize the development of bacteriophage insensitive mutants (BIM) in target pathogen populations. Regulatory approval for the use of several lytic phage products specific for bacterial pathogens such as <i>Escherichia coli</i> O157:H7, <i>Salmonella</i> spp. and <i>Listeria monocytogenes</i> in foods and on food processing surfaces has been granted by various agencies in the US and other countries, possibly allowing for the more widespread use of bacteriophages in the decontamination of fresh and minimally processed produce. Research studies have shown lytic bacteriophages specific for <i>E. coli</i> O157:H7, <i>Salmonella</i> spp. and <i>Listeria monocytogenes</i> have been effective in reducing pathogen populations on leafy greens, sprouts and tomatoes.</p>","PeriodicalId":8686,"journal":{"name":"Bacteriophage","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/81/06/bact-3-e25518.PMC3821672.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31862925","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BacteriophagePub Date : 2013-04-01DOI: 10.4161/bact.25449
Diana A Tafoya, Zacariah L Hildenbrand, Nadia Herrera, Sudheer K Molugu, Vadim V Mesyanzhinov, Konstantin A Miroshnikov, Ricardo A Bernal
{"title":"Enzymatic characterization of a lysin encoded by bacteriophage EL.","authors":"Diana A Tafoya, Zacariah L Hildenbrand, Nadia Herrera, Sudheer K Molugu, Vadim V Mesyanzhinov, Konstantin A Miroshnikov, Ricardo A Bernal","doi":"10.4161/bact.25449","DOIUrl":"https://doi.org/10.4161/bact.25449","url":null,"abstract":"<p><p>The bacteriophage EL is a virus that specifically attacks the human pathogen <i>Pseudomonas aeruginosa</i>. This phage carries a large genome that encodes for its own chaperonin which presumably facilitates the proper folding of phage proteins independently of the host chaperonin system. EL also encodes a lysin enzyme, a critical component of the lytic cycle that is responsible for digesting the peptidoglycan layer of the host cell wall. Previously, this lysin was believed to be a substrate of the chaperonin encoded by phage EL. In order to characterize the activity of the EL lysin, and to determine whether lysin activity is contingent on chaperonin-mediated folding, a series of peptidoglycan hydrolysis activity assays were performed. Results indicate that the EL-encoded lysin has similar enzymatic activity to that of the <i>Gallus gallus lysozyme</i> and that the EL lysin folds into a functional enzyme in the absence of phage chaperonin and should not be considered a substrate.</p>","PeriodicalId":8686,"journal":{"name":"Bacteriophage","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2013-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/bact.25449","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"31862923","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}