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Key Projects of Alternatives to Antibiotics for Animal Usages","award":["22322906D"],"award-info":[{"award-number":["22322906D"]}]},{"name":"The Key Projects of Alternatives to Antibiotics for Animal Usages","award":["CAASASTIP-2013-FRI-02"],"award-info":[{"award-number":["CAASASTIP-2013-FRI-02"]}]},{"name":"The Key Projects of Alternatives to Antibiotics for Animal Usages","award":["CAAS-ZDRW202111"],"award-info":[{"award-number":["CAAS-ZDRW202111"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Marine Drugs"],"abstract":"<jats:p>The marine peptide, American oyster defensin (AOD), is derived from Crassostrea virginica and exhibits a potent bactericidal effect. However, recombinant preparation has not been achieved due to the high charge and hydrophobicity. Although the traditional fusion tags such as Trx and SUMO shield the effects of target peptides on the host, their large molecular weight (12\u201320 kDa) leads to the yields lower than 20% of the fusion protein. In this study, a short and acidic fusion tag was employed with a compact structure of only 1 kDa. Following 72 h of induction in a 5 L fermenter, the supernatant exhibited a total protein concentration of 587 mg\/L. The recombinant AOD was subsequently purified through affinity chromatography and enterokinase cleavage, resulting in the final yield of 216 mg\/L and a purity exceeding 93%. The minimum inhibitory concentrations (MICs) of AOD against Staphylococcus aureus, Staphylococcus epidermidis, and Streptococcus galactis ranged from 4 to 8 \u03bcg\/mL. Moreover, time-killing curves indicated that AOD achieved a bactericidal rate of 99.9% against the clinical strain S. epidermidis G-81 within 0.5 h at concentrations of 2\u00d7 and 4\u00d7 MIC. Additionally, the activity of AOD was unchanged after treatment with artificial gastric fluid and intestinal fluid for 4 h. Biocompatibility testing demonstrated that AOD, at a concentration of 128 \u03bcg\/mL, exhibited a hemolysis rate of less than 0.5% and a cell survival rate of over 83%. Furthermore, AOD\u2019s in vivo therapeutic efficacy against mouse subcutaneous abscess revealed its capability to restrain bacterial proliferation and reduce bacterial load, surpassing that of antibiotic lincomycin. These findings indicate AOD\u2019s potential for clinical usage.<\/jats:p>","DOI":"10.3390\/md22010008","type":"journal-article","created":{"date-parts":[[2023,12,20]],"date-time":"2023-12-20T11:24:33Z","timestamp":1703071473000},"page":"8","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["High-Yield Preparation of American Oyster Defensin (AOD) via a Small and Acidic Fusion Tag and Its Functional Characterization"],"prefix":"10.3390","volume":"22","author":[{"given":"Qingyi","family":"Zhao","sequence":"first","affiliation":[{"name":"Gene Engineering Laboratory, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China"},{"name":"Innovative Team of Antimicrobial Peptides and Alternatives to Antibiotics, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China"},{"name":"Key Laboratory of Feed Biotechnology, Ministry of Agriculture and Rural Affairs, Beijing 100081, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Na","family":"Yang","sequence":"additional","affiliation":[{"name":"Gene Engineering Laboratory, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China"},{"name":"Innovative Team of Antimicrobial Peptides and Alternatives to Antibiotics, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China"},{"name":"Key Laboratory of Feed Biotechnology, Ministry of Agriculture and Rural Affairs, Beijing 100081, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xinxi","family":"Gu","sequence":"additional","affiliation":[{"name":"Enzyme Engineering Laboratory, College of Food Science and Technology, Hebei Agricultural University, Baoding 071001, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuanyuan","family":"Li","sequence":"additional","affiliation":[{"name":"Gene Engineering Laboratory, Feed Research 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China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ya","family":"Hao","sequence":"additional","affiliation":[{"name":"Gene Engineering Laboratory, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China"},{"name":"Innovative Team of Antimicrobial Peptides and Alternatives to Antibiotics, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China"},{"name":"Key Laboratory of Feed Biotechnology, Ministry of Agriculture and Rural Affairs, Beijing 100081, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Haiqiang","family":"Lu","sequence":"additional","affiliation":[{"name":"Enzyme Engineering Laboratory, College of Food Science and Technology, Hebei Agricultural University, Baoding 071001, 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Res."},{"key":"ref_2","doi-asserted-by":"crossref","unstructured":"Figueroa, D., Perez, C., and Elmore, D.E. (2016). The Role of Arginine and Lysine in Histone Derived Antimicrobial Peptides. Biophys. J., 110.","DOI":"10.1016\/j.bpj.2015.11.2249"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"e5480","DOI":"10.1126\/science.aau5480","article-title":"Antimicrobial Peptides: Application Informed by Evolution","volume":"368","author":"Lazzaro","year":"2020","journal-title":"Science"},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Pen, G., Yang, N., Teng, D., Mao, R., Hao, Y., and Wang, J. (2020). A Review on the Use of Antimicrobial Peptides to Combat Porcine Viruses. Antibiotics, 9.","DOI":"10.3390\/antibiotics9110801"},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Coleman, P.C., Bale, J.S., and Hayward, S.A. (2015). Meat Feeding Restricts Rapid Cold Hardening Response and Increases Thermal Activity Thresholds of Adult Blow Flies, Calliphora vicina (Diptera: Calliphoridae). PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0131301"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1998","DOI":"10.1016\/j.bbrc.2005.11.013","article-title":"Purification of a Novel Arthropod Defensin from the American Oyster, Crassostrea virginica","volume":"338","author":"Seo","year":"2005","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Seo, J.-K., Kim, D.-G., Lee, J.-E., Park, K.-S., Lee, I.-A., Lee, K.-Y., Kim, Y.-O., and Nam, B.-H. (2021). Antimicrobial Activity and Action Mechanisms of Arg-Rich Short Analog Peptides Designed from the C-terminal Loop Region of American Oyster Defensin (AOD). Mar. Drugs, 19.","DOI":"10.3390\/md19080451"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1016\/S0165-022X(01)00213-5","article-title":"The FLAG\u2122 peptide, a Versatile Fusion Tag for the Purification of Recombinant Proteins","volume":"49","author":"Einhauer","year":"2001","journal-title":"J. Biochem. Biophys. Methods"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/S0021-9673(00)93969-4","article-title":"New Metal Chelate Adsorbent Selective for Proteins and Peptides Containing Neighbouring Histidine Residues","volume":"411","author":"Hochuli","year":"1987","journal-title":"J. Chromatogr. A"},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Kim, D.S., Kim, S.W., Song, J.M., Kim, S.Y., and Kwon, K.-C. (2019). A New Prokaryotic Expression Vector for the Expression of Antimicrobial Peptide Abaecin Using SUMO Fusion Tag. BMC Biotechnol., 19.","DOI":"10.1186\/s12896-019-0506-x"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1204","DOI":"10.1038\/nbt1088-1204","article-title":"A Short Polypeptide Marker Sequence Useful for Recombinant Protein Identification and Purification","volume":"6","author":"Hopp","year":"1988","journal-title":"Biol. Technol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"5031","DOI":"10.1016\/S0021-9258(18)61965-9","article-title":"Purification and Specificity of Porcine Enterokinase","volume":"246","author":"Maroux","year":"1971","journal-title":"J. Biol. Chem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1002\/yea.3226","article-title":"N-ICE Plasmids for Generating N-terminal 3\u00d7 FLAG Tagged Genes that Allow Inducible, Constitutive or Endogenous Expression in Saccharomyces cerevisiae","volume":"34","author":"Zhang","year":"2017","journal-title":"Yeast"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.idc.2008.10.001","article-title":"Coagulase-negative Staphylococcal Infections","volume":"23","author":"Rogers","year":"2009","journal-title":"Infect. Dis. Clin. N. Am."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1111\/jdv.15183","article-title":"Biofilm Production and Antibiotic Susceptibility of Staphylococcus epidermidis strains from Hidradenitis Suppurativa lesions","volume":"33","author":"Ardon","year":"2019","journal-title":"J. Eur. Acad. Dermatol. Venereol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1927","DOI":"10.1007\/s00253-016-7960-3","article-title":"Optimization of the Fermentation and Downstream Processes for Human Enterokinase Production in Pichia pastoris","volume":"101","author":"Krahulec","year":"2017","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/S0958-1669(02)00330-0","article-title":"Production of Recombinant Proteins in Fermenter Cultures of the Yeast Pichia pastoris","volume":"13","author":"Cereghino","year":"2002","journal-title":"Curr. Opin. Biotechnol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"5193","DOI":"10.1007\/s00253-019-09785-0","article-title":"A Recombinant Fungal Defensin-like Peptide-P2 Combats Multidrug-resistant Staphylococcus aureus and biofilms","volume":"103","author":"Yang","year":"2019","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/j.pep.2011.04.014","article-title":"Expression of Plectasin in Pichia pastoris and Its Characterization as a New Antimicrobial Peptide against Staphyloccocus and Streptococcus","volume":"78","author":"Zhang","year":"2011","journal-title":"Protein Expr. Purif."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1093\/jac\/48.suppl_1.5","article-title":"Determination of Minimum Inhibitory Concentrations","volume":"48","author":"Andrews","year":"2001","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Hao, Y., Teng, D., Mao, R., Yang, N., and Wang, J. (2023). Site Mutation Improves the Expression and Antimicrobial Properties of Fungal Defense. Antibiotics, 12.","DOI":"10.3390\/antibiotics12081283"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"637","DOI":"10.3389\/fmicb.2021.637662","article-title":"Design and High Expression of Non-glycosylated Lysostaphins in Pichia pastoris and their pharmacodynamic study","volume":"12","author":"Shen","year":"2021","journal-title":"Front. Microbiol."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Jin, Y., Yang, N., Teng, D., Hao, Y., Mao, R., and Wang, J. (2023). Molecular Modification of Kex2 P1\u2019Site Enhances Expression and Druggability of Fungal Defensin. Antibiotics, 12.","DOI":"10.3390\/antibiotics12040786"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.tifs.2021.01.005","article-title":"The Structure-mechanism Relationship and Mode of Actions of Antimicrobial Peptides: A Review","volume":"109","author":"Li","year":"2021","journal-title":"Trends Food Sci. Technol."},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Ambrosio, R.L., Rossell\u00f3, C.A., Casares, D., Palmieri, G., Anastasio, A., and Escrib\u00e1, P.V. (2022). The Antimicrobial Peptide 1018-K6 Interacts Distinctly with Eukaryotic and Bacterial Membranes, the Basis of Its Specificity and Bactericidal Activity. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms232012392"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"3977","DOI":"10.1128\/AAC.00575-06","article-title":"Treatment and Prevention of Staphylococcus epidermidis Experimental Biomaterial-associated Infection by Bactericidal Peptide 2","volume":"50","author":"Kwakman","year":"2006","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Ma, X., Yang, N., Mao, R., Hao, Y., Yan, X., Teng, D., and Wang, J. (2021). The Pharmacodynamics Study of Insect Defensin DLP4 against Toxigenic Staphylococcus hyicus ACCC 61734 in Vitro and Vivo. Front. Cell Infect. Microbiol., 11.","DOI":"10.3389\/fcimb.2021.638598"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1555","DOI":"10.1007\/s00253-019-10313-3","article-title":"A New High-yielding Antimicrobial Peptide NZX and Its Antibacterial Activity against Staphylococcus hyicus in Vitro\/Vivo","volume":"104","author":"Liu","year":"2020","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"6255","DOI":"10.1007\/s00253-015-6394-7","article-title":"In Vitro and in Vivo Characterization of a New Recombinant Antimicrobial Peptide, MP1102, against Methicillin-resistant Staphylococcus aureus","volume":"99","author":"Zhang","year":"2015","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1038\/nprot.2007.521","article-title":"Agar and Broth Dilution Methods to Determine the Minimal Inhibitory Concentration (MIC) of Antimicrobial Substances","volume":"3","author":"Wiegand","year":"2008","journal-title":"Nat. Protoc."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1128\/AAC.02549-18","article-title":"Evaluation of the Bactericidal Activity of Fosfomycin in Combination with Selected Antimicrobial Comparison Agents Tested against Gram-Negative Bacterial Strains by Using Time-Kill Curves","volume":"63","author":"Flamm","year":"2019","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"3392","DOI":"10.1038\/s41598-017-03664-2","article-title":"Antibacterial and Detoxifying Activity of NZ17074 Analogues with Multi-layers of Selective Antimicrobial Actions against Escherichia coli and Salmonella enteritidis","volume":"7","author":"Yang","year":"2017","journal-title":"Sci. Rep."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"e01056-16","DOI":"10.1128\/AAC.01056-16","article-title":"Combined Systems Approaches Reveal a Multistage Mode of Action of a Marine Antimicrobial Peptide against Pathogenic Escherichia coli and its Protective Effect against Bacterial Peritonitis and Endotoxemia","volume":"61","author":"Wang","year":"2017","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1146\/annurev-pathol-011110-130327","article-title":"The Pathogenesis of Sepsis","volume":"6","author":"Osuchowski","year":"2011","journal-title":"Annu. Rev. Pathol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1206","DOI":"10.1016\/j.ajpath.2012.07.005","article-title":"A Novel Mouse Model of Staphylococcus aureus Chronic Osteomyelitis that Closely Mimics the Human Infection: An Integrated View of Disease Pathogenesis","volume":"181","author":"Horst","year":"2012","journal-title":"Am. J. Pathol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.rvsc.2018.01.016","article-title":"Activation of Mast Cells in Skin Abscess Induced by Staphylococcus aureus (S. aureus) Infection in Mice","volume":"118","author":"Lei","year":"2018","journal-title":"Res. Vet. Sci."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1093\/jac\/dkx432","article-title":"Effect of Staphylococcus aureus Tet38 Native Efflux Pump on in Vivo Response to Tetracycline in a Murine Subcutaneous Abscess Model","volume":"73","author":"Chen","year":"2018","journal-title":"J. Antimicrob. Chemother."}],"container-title":["Marine Drugs"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1660-3397\/22\/1\/8\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T21:39:09Z","timestamp":1760132349000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1660-3397\/22\/1\/8"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,12,20]]},"references-count":37,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2024,1]]}},"alternative-id":["md22010008"],"URL":"https:\/\/doi.org\/10.3390\/md22010008","relation":{},"ISSN":["1660-3397"],"issn-type":[{"value":"1660-3397","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,12,20]]}}}