{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,8]],"date-time":"2026-01-08T21:28:53Z","timestamp":1767907733603,"version":"3.49.0"},"reference-count":53,"publisher":"American Society for Microbiology","issue":"19","license":[{"start":{"date-parts":[[2013,10,1]],"date-time":"2013-10-01T00:00:00Z","timestamp":1380585600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Appl Environ Microbiol"],"published-print":{"date-parts":[[2013,10]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            There continues to be a need for developing efficient and environmentally friendly treatments for\n            <jats:named-content content-type=\"genus-species\">Bacillus anthracis<\/jats:named-content>\n            , the causative agent of anthrax. One emerging approach for inactivation of vegetative\n            <jats:named-content content-type=\"genus-species\">B. anthracis<\/jats:named-content>\n            is the use of bacteriophage endolysins or lytic enzymes encoded by bacterial genomes (autolysins) with highly evolved specificity toward bacterium-specific peptidoglycan cell walls. In this work, we performed\n            <jats:italic>in silico<\/jats:italic>\n            analysis of the genome of\n            <jats:named-content content-type=\"genus-species\">Bacillus anthracis<\/jats:named-content>\n            strain Ames, using a consensus binding domain amino acid sequence as a probe, and identified a novel lytic enzyme that we termed AmiBA2446. This enzyme exists as a homodimer, as determined by size exclusion studies. It possesses\n            <jats:italic>N<\/jats:italic>\n            -acetylmuramoyl-\n            <jats:sc>l<\/jats:sc>\n            -alanine amidase activity, as determined from liquid chromatography-mass spectrometry (LC-MS) analysis of muropeptides released due to the enzymatic digestion of peptidoglycan. Phylogenetic analysis suggested that AmiBA2446 was an autolysin of bacterial origin. We characterized the effects of enzyme concentration and phase of bacterial growth on bactericidal activity and observed close to a 5-log reduction in the viability of cells of\n            <jats:named-content content-type=\"genus-species\">Bacillus cereus<\/jats:named-content>\n            4342, a surrogate for\n            <jats:named-content content-type=\"genus-species\">B. anthracis<\/jats:named-content>\n            . We further tested the bactericidal activity of AmiBA2446 against various\n            <jats:named-content content-type=\"genus-species\">Bacillus<\/jats:named-content>\n            species and demonstrated significant activity against\n            <jats:named-content content-type=\"genus-species\">B. anthracis<\/jats:named-content>\n            and\n            <jats:named-content content-type=\"genus-species\">B. cereus<\/jats:named-content>\n            strains. We also demonstrated activity against\n            <jats:named-content content-type=\"genus-species\">B. anthracis<\/jats:named-content>\n            spores after pretreatment with germinants. AmiBA2446 enzyme was also stable in solution, retaining its activity after 4 months of storage at room temperature.\n          <\/jats:p>","DOI":"10.1128\/aem.02235-13","type":"journal-article","created":{"date-parts":[[2013,7,20]],"date-time":"2013-07-20T05:08:50Z","timestamp":1374296930000},"page":"5899-5906","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":28,"title":["Characterization of AmiBA2446, a Novel Bacteriolytic Enzyme Active against Bacillus Species"],"prefix":"10.1128","volume":"79","author":[{"given":"Krunal K.","family":"Mehta","sequence":"first","affiliation":[{"name":"Howard P. Isermann Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, New York, USA"},{"name":"Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Elena E.","family":"Paskaleva","sequence":"additional","affiliation":[{"name":"Howard P. Isermann Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, New York, USA"},{"name":"Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Saba","family":"Azizi-Ghannad","sequence":"additional","affiliation":[{"name":"Department of Biology, Rensselaer Polytechnic Institute, Troy, New York, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daniel J.","family":"Ley","sequence":"additional","affiliation":[{"name":"U.S. Army Corps of Engineers, Engineer Research and Development Center, Construction Engineering Research Laboratory, Champaign, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Martin A.","family":"Page","sequence":"additional","affiliation":[{"name":"U.S. Army Corps of Engineers, Engineer Research and Development Center, Construction Engineering Research Laboratory, Champaign, Illinois, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jonathan S.","family":"Dordick","sequence":"additional","affiliation":[{"name":"Howard P. Isermann Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, New York, USA"},{"name":"Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York, USA"},{"name":"Department of Materials Science and Engineering, Rensselaer Polytechnic Institute, Troy, New York, USA"},{"name":"Department of Biology, Rensselaer Polytechnic Institute, Troy, New York, USA"},{"name":"Department of Biomedical Engineering, Rensselaer Polytechnic Institute, Troy, New York, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ravi S.","family":"Kane","sequence":"additional","affiliation":[{"name":"Howard P. 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