10.1371/journal.pone.0218507.g003 Rohana P. Dassanayake Rohana P. Dassanayake Shollie M. Falkenberg Shollie M. Falkenberg Eric M. Nicholson Eric M. Nicholson Robert E. Briggs Robert E. Briggs Fred M. Tatum Fred M. Tatum Vijay K. Sharma Vijay K. Sharma Timothy A. Reinhardt Timothy A. Reinhardt Both original bNK2A-C10C20 and an analog bNK2A-S10S20 peptides displayed strong antimicrobial activities against <i>Histophilus somni</i>. Public Library of Science 2019 well-conserved cysteine residues bNK 2A antimicrobial activity 30- mer bNK 2A peptides intra-chain disulfide bonds bNK 2A peptide Mature NK-lysin protein bactericidal activity Bovine NK-lysins disulfide bonds bNK 2A forms disulfide bonds α- helical structures NK-lysin-derived peptides show antimicrobial activity NK-lysin-derived peptide cationic antimicrobial proteins 2019-06-19 17:37:25 Figure https://plos.figshare.com/articles/figure/Both_original_bNK2A-C10C20_and_an_analog_bNK2A-S10S20_peptides_displayed_strong_antimicrobial_activities_against_i_Histophilus_somni_i_/8297246 <p>(A). Two bovine <i>H</i>. <i>somni</i> pneumonic isolates (91 and 2336) were incubated with indicated concentrations of peptides or PBS (control) and incubated at 37°C in a humidified atmosphere of 7.5% CO<sub>2</sub> for 60 min. (B). The original bNK2A-C10C20 peptide (20 μM) was pre-incubated with 0.2, 0.5, and 1.0 mM DTT for 20 min before incubation with <i>H</i>. <i>somni</i> (91 and 2336). Results shown are the means and SD of three independent experiments.</p>