%0 Figure %A Dassanayake, Rohana P. %A Falkenberg, Shollie M. %A M. Nicholson, Eric %A E. Briggs, Robert %A Tatum, Fred M. %A K. Sharma, Vijay %A Reinhardt, Timothy A. %D 2019 %T Both original bNK2A-C10C20 and an analog bNK2A-S10S20 peptides displayed strong antimicrobial activities against Histophilus somni. %U 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 %R 10.1371/journal.pone.0218507.g003 %2 https://plos.figshare.com/ndownloader/files/15546581 %K well-conserved cysteine residues %K bNK 2A antimicrobial activity %K 30- mer bNK 2A peptides %K intra-chain disulfide bonds %K bNK 2A peptide %K Mature NK-lysin protein %K bactericidal activity Bovine NK-lysins %K disulfide bonds %K bNK 2A forms disulfide bonds %K α- helical structures %K NK-lysin-derived peptides show antimicrobial activity %K NK-lysin-derived peptide %K cationic antimicrobial proteins %X

(A). Two bovine H. somni 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% CO2 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 H. somni (91 and 2336). Results shown are the means and SD of three independent experiments.

%I PLOS ONE