About: Antimicrobial activity of bovine NK-lysin-derived peptides on bovine respiratory pathogen Histophilus somni

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About: Antimicrobial activity of bovine NK-lysin-derived peptides on bovine respiratory pathogen Histophilus somni Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Antimicrobial activity of bovine NK-lysin-derived peptides on bovine respiratory pathogen Histophilus somni
Creator	Falkenberg, Shollie Briggs, Robert Sacco, Randy Dassanayake, Rohana Tatum, Fred
Source	Medline; PMC
abstract	Bovine NK-lysins, which are functionally and structurally similar to human granulysin and porcine NK-lysin, are predominantly found in the granules of cytotoxic T-lymphocytes and NK-cells. Although antimicrobial activity of bovine NK-lysin has been assessed for several bacterial pathogens, not all the important bacterial pathogens that are involved in the bovine respiratory disease complex have been studied. Therefore the objective of the present study was to evaluate the antimicrobial activity of bovine NK-lysin-derived peptides on bovine respiratory pathogen Histophilus somni. Four, 30-mer peptides corresponding to the functional region of NK-lysin helices 2 and 3 were synthesized and assessed for antibacterial activity on four bovine pneumonic H. somni isolates. Although there were some differences in the efficiency of bactericidal activity among the NK-lysin peptides at lower concentrations (2–5 μM), all four peptides effectively killed most H. somni isolates at higher concentrations (10–30 μM) as determined by a bacterial killing assay. Confocal microscopic and flow cytometric analysis of Live/Dead Baclight stained H. somni (which were preincubated with NK-lysin peptides) were consistent with the killing assay findings and suggest NK-lysin peptides are bactericidal for H. somni. Among the four peptides, NK2A-derived peptide consistently showed the highest antimicrobial activity against all four H. somni isolates. Electron microscopic examination of H. somni following incubation with NK-lysin revealed extensive cell membrane damage, protrusions of outer membranes, and cytoplasmic content leakage. Taken together, the findings from this study clearly demonstrate the antimicrobial activity of all four bovine NK-lysin-derived peptides against bovine H. somni isolates.
has issue date	2017-08-21(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0183610
bibo:pmid	28827826
has license	cc0
sha1sum (hex)	e55df621c9df11f9127cdb8829686868bd2ec1cc
schema:url	https://doi.org/10.1371/journal.pone.0183610
resource representing a document's title	Antimicrobial activity of bovine NK-lysin-derived peptides on bovine respiratory pathogen Histophilus somni
has PubMed Central identifier	PMC5565109
has PubMed identifier	28827826
schema:publication	PLoS One
resource representing a document's body	covid:e55df621c9df11f9127cdb8829686868bd2ec1cc#body_text
is schema:about of	named entity 'RESPIRATORY' named entity 'NK-LYSIN' named entity 'assay' named entity 'activity' named entity 'content' named entity 'bactericidal' named entity 'Although' named entity 'peptide' named entity 'peptides' named entity 'functionally' named entity 'HAVE' named entity 'OBJECTIVE' named entity 'FOUND' named entity 'PROTRUSIONS' named entity 'CELL MEMBRANE DAMAGE' named entity 'HISTOPHILUS SOMNI' named entity 'PEPTIDES' named entity 'REGION' named entity 'MICROSCOPIC EXAMINATION' named entity 'PRESENT' named entity 'LOWER' named entity 'MEMBRANES' named entity 'HELICES' named entity 'CYTOTOXIC T-LYMPHOCYTES' named entity 'BOVINE RESPIRATORY DISEASE COMPLEX' named entity 'ELECTRON' named entity 'HUMAN' named entity 'DETERMINED BY' named entity 'LEAKAGE' named entity 'PATHOGEN' named entity 'BOVINE' named entity 'DERIVED' named entity 'LIVE' named entity 'ACTIVITY' named entity 'PATHOGEN' named entity 'ANTIMICROBIAL ACTIVITY' named entity 'INCUBATION' named entity 'BCM' named entity 'PORCINE' named entity 'CONSISTENT WITH' named entity 'IMPORTANT' named entity '282' named entity 'STAINED' named entity 'PNEUMONIC' named entity 'RESPIRATORY' named entity 'KILLING' named entity 'HIGHEST' named entity 'FLOW CYTOMETRIC ANALYSIS' named entity 'INVOLVED' named entity 'HIGHER' named entity 'CONTENT' named entity 'FUNCTIONAL' named entity 'NK-LYSIN' named entity 'EVALUATE' named entity 'SIMILAR' named entity 'ASSAY' named entity 'OUTER' named entity 'CYTOPLASMIC' named entity 'SUGGEST' named entity 'GRANULES' named entity 'STUDY' named entity 'MER' named entity 'EXTENSIVE' named entity 'BACTERICIDAL ACTIVITY' named entity 'TAKEN' named entity 'CONCENTRATIONS' named entity 'ISOLATES' named entity 'MICROSCOPIC' named entity 'PEPTIDE' named entity 'ASSESSED' named entity 'DERIVED' named entity 'REVEALED' named entity 'SYNTHESIZED' named entity 'ANTIMICROBIAL ACTIVITY' named entity 'HISTOPHILUS SOMNI' named entity 'BACTERIAL PATHOGENS' named entity 'FOLLOWING'

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