Construction of Aeromonas salmonicida subsp. achromogenes AsaP1‐toxoid strains and study of their ability to induce immunity in Arctic char, Salvelinus alpinus L. Issue 10 (1st October 2014)
- Record Type:
- Journal Article
- Title:
- Construction of Aeromonas salmonicida subsp. achromogenes AsaP1‐toxoid strains and study of their ability to induce immunity in Arctic char, Salvelinus alpinus L. Issue 10 (1st October 2014)
- Main Title:
- Construction of Aeromonas salmonicida subsp. achromogenes AsaP1‐toxoid strains and study of their ability to induce immunity in Arctic char, Salvelinus alpinus L.
- Authors:
- Schwenteit, J M
Weber, B
Milton, D L
Bornscheuer, U T
Gudmundsdottir, B K - Abstract:
- <abstract abstract-type="main" id="jfd12303-abs-0001"> <title>Abstract</title> <p>The metalloendopeptidase AsaP1 is one of the major extracellular virulence factors of <italic>A. salmonicida</italic> subsp. <italic>achromogenes</italic>, expressed as a 37‐kDa pre‐pro‐peptide and processed to a 19‐kDa active peptide. The aim of this study was to construct mutant strains secreting an AsaP1‐toxoid instead of AsaP1‐wt, to study virulence of these strains and to test the potency of the AsaP1‐toxoid bacterin and the recombinant AsaP1‐toxoids to induce protective immunity in Arctic char. Two <italic>A. salmonicida</italic> mutants were constructed that secrete either AsaP1<sub>E294A</sub> or AsaP1<sub>Y309F</sub>. The secreted AsaP1<sub>Y309F</sub>‐toxoid had weak caseinolytic activity and was processed to the 19‐kDa peptide, whereas the AsaP1<sub>E294A</sub>‐toxoid was found as a 37‐kDa pre‐pro‐peptide suggesting that AsaP1 is auto‐catalytically processed. The LD<sub>50</sub> of the AsaP1<sub>Y309F</sub>‐toxoid mutant in Arctic char was significantly higher than that of the corresponding wt strain, and LD<sub>50</sub> of the AsaP1<sub>E294A</sub>‐toxoid mutant was comparable with that of an AsaP1‐deficient strain. Bacterin based on AsaP1<sub>Y309F</sub>‐toxoid mutant provided significant protection, comparable with that induced by a commercial polyvalent furunculosis vaccine. Detoxification of AsaP1 is very hard, expensive and time consuming. Therefore, an AsaP1‐toxoid‐secreting<abstract abstract-type="main" id="jfd12303-abs-0001"> <title>Abstract</title> <p>The metalloendopeptidase AsaP1 is one of the major extracellular virulence factors of <italic>A. salmonicida</italic> subsp. <italic>achromogenes</italic>, expressed as a 37‐kDa pre‐pro‐peptide and processed to a 19‐kDa active peptide. The aim of this study was to construct mutant strains secreting an AsaP1‐toxoid instead of AsaP1‐wt, to study virulence of these strains and to test the potency of the AsaP1‐toxoid bacterin and the recombinant AsaP1‐toxoids to induce protective immunity in Arctic char. Two <italic>A. salmonicida</italic> mutants were constructed that secrete either AsaP1<sub>E294A</sub> or AsaP1<sub>Y309F</sub>. The secreted AsaP1<sub>Y309F</sub>‐toxoid had weak caseinolytic activity and was processed to the 19‐kDa peptide, whereas the AsaP1<sub>E294A</sub>‐toxoid was found as a 37‐kDa pre‐pro‐peptide suggesting that AsaP1 is auto‐catalytically processed. The LD<sub>50</sub> of the AsaP1<sub>Y309F</sub>‐toxoid mutant in Arctic char was significantly higher than that of the corresponding wt strain, and LD<sub>50</sub> of the AsaP1<sub>E294A</sub>‐toxoid mutant was comparable with that of an AsaP1‐deficient strain. Bacterin based on AsaP1<sub>Y309F</sub>‐toxoid mutant provided significant protection, comparable with that induced by a commercial polyvalent furunculosis vaccine. Detoxification of AsaP1 is very hard, expensive and time consuming. Therefore, an AsaP1‐toxoid‐secreting mutant is more suitable than the respective wt strain for production of fish bacterins aimed to protect against atypical furunculosis.</p> </abstract> … (more)
- Is Part Of:
- Journal of fish diseases. Volume 38:Issue 10(2015:Oct.)
- Journal:
- Journal of fish diseases
- Issue:
- Volume 38:Issue 10(2015:Oct.)
- Issue Display:
- Volume 38, Issue 10 (2015)
- Year:
- 2015
- Volume:
- 38
- Issue:
- 10
- Issue Sort Value:
- 2015-0038-0010-0000
- Page Start:
- 891
- Page End:
- 900
- Publication Date:
- 2014-10-01
- Subjects:
- Fishes -- Diseases -- Periodicals
639.3 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2761 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/jfd.12303 ↗
- Languages:
- English
- ISSNs:
- 0140-7775
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4984.285000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3276.xml