Discovery and Biochemical Characterization of PlyP56, PlyN74, and PlyTB40—Bacillus Specific Endolysins

dc.contributor.authorEtobayeva, Irina
dc.contributor.authorLinden, Sara B.
dc.contributor.authorAlem, Farhang
dc.contributor.authorHarb, Laith
dc.contributor.authorRizkalla, Lucas
dc.contributor.authorMosier, Philip D.
dc.contributor.authorJohnson, Allison A.
dc.contributor.authorTemple, Louise
dc.contributor.authorHakami, Ramin M.
dc.contributor.authorNelson, Daniel C.
dc.date.accessioned2023-11-20T20:43:47Z
dc.date.available2023-11-20T20:43:47Z
dc.date.issued2018-05-21
dc.description.abstractThree Bacillus bacteriophage-derived endolysins, designated PlyP56, PlyN74, and PlyTB40, were identified, cloned, purified, and characterized for their antimicrobial properties. Sequence alignment reveals these endolysins have an N-terminal enzymatically active domain (EAD) linked to a C-terminal cell wall binding domain (CBD). PlyP56 has a Peptidase_M15_4/VanY superfamily EAD with a conserved metal binding motif and displays biological dependence on divalent ions for activity. In contrast, PlyN74 and PlyTB40 have T7 lysozyme-type Amidase_2 and carboxypeptidase T-type Amidase_3 EADs, respectively, which are members of the MurNAc-LAA superfamily, but are not homologs and thus do not have a shared protein fold. All three endolysins contain similar SH3-family CBDs. Although minor host range differences were noted, all three endolysins show relatively broad antimicrobial activity against members of the Bacillus cereus sensu lato group with the highest lytic activity against B. cereus ATCC 4342. Characterization studies determined the optimal lytic activity for these enzymes was at physiological pH (pH 7.0–8.0), over a broad temperature range (4–55 °C), and at low concentrations of NaCl (<50 mM). Direct comparison of lytic activity shows the PlyP56 enzyme to be twice as effective at lysing the cell wall peptidoglycan as PlyN74 or PlyTB40, suggesting PlyP56 is a good candidate for further antimicrobial development as well as bioengineering studies.
dc.description.urihttps://doi.org/10.3390/v10050276
dc.identifierhttps://doi.org/10.13016/dspace/zjwd-hrys
dc.identifier.citationEtobayeva, I.; Linden, S.B.; Alem, F.; Harb, L.; Rizkalla, L.; Mosier, P.D.; Johnson, A.A.; Temple, L.; Hakami, R.M.; Nelson, D.C. Discovery and Biochemical Characterization of PlyP56, PlyN74, and PlyTB40—Bacillus Specific Endolysins. Viruses 2018, 10, 276.
dc.identifier.urihttp://hdl.handle.net/1903/31462
dc.language.isoen_US
dc.publisherMDPI
dc.relation.isAvailableAtCollege of Agriculture & Natural Resourcesen_us
dc.relation.isAvailableAtDepartment of Veterinary Medicineen_us
dc.relation.isAvailableAtDigital Repository at the University of Marylanden_us
dc.relation.isAvailableAtUniversity of Maryland (College Park, MD)en_us
dc.subjectendolysin
dc.subjectbacteriophage
dc.subjectBacillus cereus sensu lato
dc.subjectpeptidoglycan hydrolase
dc.titleDiscovery and Biochemical Characterization of PlyP56, PlyN74, and PlyTB40—Bacillus Specific Endolysins
dc.typeArticle
local.equitableAccessSubmissionNo

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