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>