Dassanayake, Rohana P. Falkenberg, Shollie M. M. Nicholson, Eric E. Briggs, Robert Tatum, Fred M. K. Sharma, Vijay Reinhardt, Timothy A. Both original bNK2A-C10C20 and an analog bNK2A-S10S20 peptides displayed strong antimicrobial activities against <i>Histophilus somni</i>. <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> 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
    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
10.1371/journal.pone.0218507.g003