{"doi":"10.1128/aem.00555-19","title":"Bacteriophage φEf11 ORF28 Endolysin, a Multifunctional Lytic Enzyme with Properties Distinct from All Other Identified Enterococcus faecalis Phage Endolysins","abstract":"<jats:p>\n            The emergence of multidrug-resistant pathogenic microorganisms has brought increasing attention to the urgent need for the development of alternative antimicrobial strategies. One such alternative to conventional antibiotics employs lytic enzymes (endolysins) that are produced by bacteriophages in the course of lytic infection. During lytic infection by a bacteriophage, these enzymes hydrolyze the cell wall peptidoglycan, resulting in the lysis of the host cell. However, external endolysin application can result in lysis from without. In this study, we have cloned, expressed, purified, and characterized an endolysin produced by a bacteriophage infecting strains of\n            <jats:named-content content-type=\"genus-species\">Enterococcus faecalis</jats:named-content>\n            . The lysin is broadly active against most of the tested\n            <jats:named-content content-type=\"genus-species\">E. faecalis</jats:named-content>\n            strains and exhibits multifunctional enzymatic specificities that differ from all other characterized endolysins produced by\n            <jats:named-content content-type=\"genus-species\">E. faecalis</jats:named-content>\n            bacteriophages.\n          </jats:p>","journal":"Applied and Environmental Microbiology","year":2019,"id":599403,"datarank":0.5676284450877392,"base_score":3.784189633918261,"endowment":3.784189633918261,"self_citation_contribution":0.5676284450877392,"citation_network_contribution":0.0,"self_endowment_contribution":0.5676284450877392,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":43,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":291655,"name":"Bettina A. Buttaro","orcid":"0000-0003-4770-864X","position":1,"is_corresponding":false},{"id":245707,"name":"Derrick E. Fouts","orcid":"0000-0003-4323-7668","position":2,"is_corresponding":false},{"id":1536186,"name":"Salar Sanjari","orcid":null,"position":3,"is_corresponding":false},{"id":545791,"name":"Bradley S. Evans","orcid":"0000-0002-1207-9006","position":4,"is_corresponding":false},{"id":1536187,"name":"Roy H. Stevens","orcid":null,"position":5,"is_corresponding":false},{"id":1536185,"name":"Hongming Zhang","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Bacteriophage φEf11 ORF28 Endolysin, a Multifunctional Lytic Enzyme with Properties Distinct from All Other Identified Enterococcus faecalis Phage Endolysins","abstract":"<jats:p>\n            The emergence of multidrug-resistant pathogenic microorganisms has brought increasing attention to the urgent need for the development of alternative antimicrobial strategies. One such alternative to conventional antibiotics employs lytic enzymes (endolysins) that are produced by bacteriophages in the course of lytic infection. During lytic infection by a bacteriophage, these enzymes hydrolyze the cell wall peptidoglycan, resulting in the lysis of the host cell. However, external endolysin application can result in lysis from without. In this study, we have cloned, expressed, purified, and characterized an endolysin produced by a bacteriophage infecting strains of\n            <jats:named-content content-type=\"genus-species\">Enterococcus faecalis</jats:named-content>\n            . The lysin is broadly active against most of the tested\n            <jats:named-content content-type=\"genus-species\">E. faecalis</jats:named-content>\n            strains and exhibits multifunctional enzymatic specificities that differ from all other characterized endolysins produced by\n            <jats:named-content content-type=\"genus-species\">E. faecalis</jats:named-content>\n            bacteriophages.\n          </jats:p>","is_dataset_classified":null,"base_score":3.784189633918261,"endowment":3.784189633918261,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"30979842","pmcid":"PMC6581165","openalex_id":"https://openalex.org/W2937089792","authors":[],"funders":[{"funder_name":"HHS | National Institutes of Health","grant_id":"R15 DE021016","title":null},{"funder_name":"J&amp;J | Janssen Research and Development","grant_id":"","title":null}],"total_grants":2,"fwci":3.8406,"citation_percentile":0.93352626,"influential_citations":0,"citation_trend":[{"year":2019,"count":1},{"year":2020,"count":6},{"year":2021,"count":13},{"year":2022,"count":3},{"year":2023,"count":4},{"year":2024,"count":3},{"year":2025,"count":11},{"year":2026,"count":2}],"oa_status":"bronze","license":"https://journals.asm.org/non-commercial-tdm-license","oa_locations":[{"url":"https://aem.asm.org/content/aem/85/13/e00555-19.full.pdf","host_type":"journal"},{"url":"https://aem.asm.org/content/aem/85/13/e00555-19.full.pdf","host_type":"publisher"},{"url":"https://journals.asm.org/doi/pdf/10.1128/AEM.00555-19","host_type":"publisher"},{"url":"https://doi.org/10.1128/aem.00555-19","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/30979842","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/6581165","host_type":"repository"}],"fields_of_study":["Bacteriophages and microbial interactions","Probiotics and Fermented Foods","Genomics and Phylogenetic Studies","Amino Acid Sequence","Base Sequence","Endopeptidases","Sequence Alignment","Siphoviridae","Viral Proteins"],"mesh_terms":["Amino Acid Sequence","Base Sequence","Endopeptidases","Viral Proteins","Sequence Alignment","Siphoviridae"],"keywords":["Lysin","Lytic cycle","Bacteriophage","Enterococcus faecalis","Microbiology","Biology","Lysis","Peptidoglycan","Enterococcus","Bacteria","Enzyme","Escherichia coli","Virology","Antibiotics","Biochemistry","Genetics","Virus","Staphylococcus aureus","Endolysin"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"gen"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-29T03:17:46.956635Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}