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The antibacterial activity of individual domains of endolysins from anti-\n                      <jats:italic toggle=\"yes\">Cutibacterium acnes<\/jats:italic>\n                      phages remains unexplored. In this study, a recombinant endolysin from\n                      <jats:italic toggle=\"yes\">C. acnes<\/jats:italic>\n                      phage CAP 10-3 and its N-terminal and C-terminal domains were tested against\n                      <jats:italic toggle=\"yes\">C. acnes<\/jats:italic>\n                      KCTC 3314 and KCTC 3320 using turbidity reduction and live cell count methods. Starting with an initial OD\n                      <jats:sub>600<\/jats:sub>\n                      <jats:bold>\u2248<\/jats:bold>\n                      1, a 3 h treatment with 50 \u00b5g\/mL of the N-terminal domain (N1) reduced OD\n                      <jats:sub>600<\/jats:sub>\n                      to 0.395 (KCTC 3314) and 0.324 (KCTC 3320), while that of full-length (FL) reduced OD\n                      <jats:sub>600<\/jats:sub>\n                      to 0.547 and 0.474, respectively. Correspondingly, N1 reduced viable counts by 1.13\u20131.35 log, whereas FL showed 0.94\u20130.95 log reduction, confirming N1\u2019s stronger bactericidal effect. C-terminal domain exhibited minimal changes in both OD\n                      <jats:sub>600<\/jats:sub>\n                      and cell count values. N1\u2019s lytic effect was further confirmed by morphology analysis. Therefore, the N-terminal domain was further characterized for its activity and specificity. It showed dose-dependent activity against both\n                      <jats:italic toggle=\"yes\">C. acnes<\/jats:italic>\n                      strains, but it had no significant effect on\n                      <jats:italic toggle=\"yes\">Staphylococcus aureus<\/jats:italic>\n                      KCTC 3881 and only weak activity against\n                      <jats:italic toggle=\"yes\">Staphylococcus epidermidis<\/jats:italic>\n                      CJNU 0702 at high concentrations (100 \u00b5g\/mL). These findings highlight the N-terminal domain\u2019s potential as a selective anti-\n                      <jats:italic toggle=\"yes\">C<\/jats:italic>\n                      .\n                      <jats:italic toggle=\"yes\">acnes<\/jats:italic>\n                      agent with minimal impact on skin flora, supporting its suitability for protein-based antimicrobial therapeutics and cosmetic applications.\n                    <\/jats:p>\n                    <jats:sec>\n                      <jats:title>IMPORTANCE<\/jats:title>\n                      <jats:p>\n                        <jats:italic toggle=\"yes\">Cutibacterium acnes<\/jats:italic>\n                        is known to play a significant role in the pathology of acne vulgaris and several other disorders. Conventional methods of treating\n                        <jats:italic toggle=\"yes\">C. acnes<\/jats:italic>\n                        infections using antibiotics face an ever-aggravating antibiotic resistance challenge. Endolysins present a promising alternative with advantages such as specificity and low-to-no chances of resistance. The current study compares the antibacterial activity of the full length as well as its N- and C-terminal domains of an endolysin from phage CAP 10-3. In addition, the dose-dependent effect and specificity of the N-terminal domain (which showed the most significant anti-\n                        <jats:italic toggle=\"yes\">C<\/jats:italic>\n                        .\n                        <jats:italic toggle=\"yes\">acnes<\/jats:italic>\n                        activity) are also explained. These findings can pave the way for developing alternative peptide-based anti-\n                        <jats:italic toggle=\"yes\">C<\/jats:italic>\n                        .\n                        <jats:italic toggle=\"yes\">acnes<\/jats:italic>\n                        therapeutics.\n                      <\/jats:p>\n                    <\/jats:sec>\n                  <\/jats:sec>","DOI":"10.1128\/aem.01168-25","type":"journal-article","created":{"date-parts":[[2025,9,22]],"date-time":"2025-09-22T13:00:16Z","timestamp":1758546016000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":4,"title":["Comparative antibacterial activity of N-terminal and C-terminal domains of a recombinant endolysin against\n                    <i>Cutibacterium acnes<\/i>"],"prefix":"10.1128","volume":"91","author":[{"given":"Jae-Hyuk","family":"Lee","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03qqbe534","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biotechnology, Korea National University of Transportation","place":["Jeungpyeong, Republic of Korea"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0003-5702-9621","authenticated-orcid":false,"given":"Muhammad Adeel","family":"Hasnain","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03qqbe534","id-type":"ROR","asserted-by":"publisher"}],"name":"Major in IT\u00b7Biohealth Convergence, Department of IT\u00b7Energy Convergence, Graduate School, Korea National University of Transportation","place":["Chungju, Republic of 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