Evaluation of the Potency of Two Pyolysin-Derived Recombinant Proteins as Vaccine Candidates of <i>Trueperella Pyogenes</i> in a Mouse Model: Pyolysin Oligomerization and Structural Change Affect the Efficacy of Pyolysin-Based Vaccines

<i>Trueperella pyogenes </i>(<i>T. pyogenes</i>)<i> </i>is an important opportunistic pathogen in livestock and wild animals. However, only one commercial<i> T. pyogenes </i>vaccine is currently available, and its immunoprotective effect is not ideal....

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Main Authors: Lingxiao Yang, Hongmin Liang, Bing Wang, Bo Ma, Junwei Wang, Wenlong Zhang
Format: Article
Language:English
Published: MDPI AG 2020-02-01
Series:Vaccines
Subjects:
Online Access:https://www.mdpi.com/2076-393X/8/1/79
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author Lingxiao Yang
Hongmin Liang
Bing Wang
Bo Ma
Junwei Wang
Wenlong Zhang
author_facet Lingxiao Yang
Hongmin Liang
Bing Wang
Bo Ma
Junwei Wang
Wenlong Zhang
author_sort Lingxiao Yang
collection DOAJ
description <i>Trueperella pyogenes </i>(<i>T. pyogenes</i>)<i> </i>is an important opportunistic pathogen in livestock and wild animals. However, only one commercial<i> T. pyogenes </i>vaccine is currently available, and its immunoprotective effect is not ideal. Pyolysin (PLO) is one of the important virulence factors expressed by<i> T. pyogenes </i>and one of the targets for the development of new <i>T. pyogenes</i> vaccines. In this study, we constructed two recombinant antigens, tPLOA1 (contains amino acids 1&#8722;110 and domain 4 of the PLO molecule) and tPLOA2 (contains amino acids 190&#8722;296 and domain 4 of the PLO molecule). Vaccines were prepared by mixing the two recombinant antigens with incomplete Freund's adjuvant or sheep red blood cell membrane and provided partial immune protection to immunized mice against the lethal challenge of<i> T. pyogenes. </i>Analysis of the PLO-specific IgG levels of immunized mice indicated that the antibody-inducing potency and immunoprotective efficacy of PLO-based vaccines are affected by the oligomerization and structural changes of PLO after binding to a cholesterol-containing membrane. In addition, the titer of anti-hemolysis antibodies is not a suitable indicator of the immunoprotective effect of these vaccines in PLO-based vaccine-immunized animals. The results provide new insights into the development of <i>T. pyogenes </i>vaccines.
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spelling doaj.art-6ae97f5164254232bb2adc27cc6a24e72022-12-22T04:09:48ZengMDPI AGVaccines2076-393X2020-02-01817910.3390/vaccines8010079vaccines8010079Evaluation of the Potency of Two Pyolysin-Derived Recombinant Proteins as Vaccine Candidates of <i>Trueperella Pyogenes</i> in a Mouse Model: Pyolysin Oligomerization and Structural Change Affect the Efficacy of Pyolysin-Based VaccinesLingxiao Yang0Hongmin Liang1Bing Wang2Bo Ma3Junwei Wang4Wenlong Zhang5Heilongjiang Key Laboratory for Animal Disease Control and Pharmaceutical Development, College of Veterinary Medicine, Northeast Agricultural University, Harbin 150030, ChinaHeilongjiang Key Laboratory for Animal Disease Control and Pharmaceutical Development, College of Veterinary Medicine, Northeast Agricultural University, Harbin 150030, ChinaHeilongjiang Key Laboratory for Animal Disease Control and Pharmaceutical Development, College of Veterinary Medicine, Northeast Agricultural University, Harbin 150030, ChinaHeilongjiang Key Laboratory for Animal Disease Control and Pharmaceutical Development, College of Veterinary Medicine, Northeast Agricultural University, Harbin 150030, ChinaHeilongjiang Key Laboratory for Animal Disease Control and Pharmaceutical Development, College of Veterinary Medicine, Northeast Agricultural University, Harbin 150030, ChinaHeilongjiang Key Laboratory for Animal Disease Control and Pharmaceutical Development, College of Veterinary Medicine, Northeast Agricultural University, Harbin 150030, China<i>Trueperella pyogenes </i>(<i>T. pyogenes</i>)<i> </i>is an important opportunistic pathogen in livestock and wild animals. However, only one commercial<i> T. pyogenes </i>vaccine is currently available, and its immunoprotective effect is not ideal. Pyolysin (PLO) is one of the important virulence factors expressed by<i> T. pyogenes </i>and one of the targets for the development of new <i>T. pyogenes</i> vaccines. In this study, we constructed two recombinant antigens, tPLOA1 (contains amino acids 1&#8722;110 and domain 4 of the PLO molecule) and tPLOA2 (contains amino acids 190&#8722;296 and domain 4 of the PLO molecule). Vaccines were prepared by mixing the two recombinant antigens with incomplete Freund's adjuvant or sheep red blood cell membrane and provided partial immune protection to immunized mice against the lethal challenge of<i> T. pyogenes. </i>Analysis of the PLO-specific IgG levels of immunized mice indicated that the antibody-inducing potency and immunoprotective efficacy of PLO-based vaccines are affected by the oligomerization and structural changes of PLO after binding to a cholesterol-containing membrane. In addition, the titer of anti-hemolysis antibodies is not a suitable indicator of the immunoprotective effect of these vaccines in PLO-based vaccine-immunized animals. The results provide new insights into the development of <i>T. pyogenes </i>vaccines.https://www.mdpi.com/2076-393X/8/1/79<i>trueperella pyogenes</i>pyolysinrecombinant antigensvaccine efficacyoligomerization and structural changes
spellingShingle Lingxiao Yang
Hongmin Liang
Bing Wang
Bo Ma
Junwei Wang
Wenlong Zhang
Evaluation of the Potency of Two Pyolysin-Derived Recombinant Proteins as Vaccine Candidates of <i>Trueperella Pyogenes</i> in a Mouse Model: Pyolysin Oligomerization and Structural Change Affect the Efficacy of Pyolysin-Based Vaccines
Vaccines
<i>trueperella pyogenes</i>
pyolysin
recombinant antigens
vaccine efficacy
oligomerization and structural changes
title Evaluation of the Potency of Two Pyolysin-Derived Recombinant Proteins as Vaccine Candidates of <i>Trueperella Pyogenes</i> in a Mouse Model: Pyolysin Oligomerization and Structural Change Affect the Efficacy of Pyolysin-Based Vaccines
title_full Evaluation of the Potency of Two Pyolysin-Derived Recombinant Proteins as Vaccine Candidates of <i>Trueperella Pyogenes</i> in a Mouse Model: Pyolysin Oligomerization and Structural Change Affect the Efficacy of Pyolysin-Based Vaccines
title_fullStr Evaluation of the Potency of Two Pyolysin-Derived Recombinant Proteins as Vaccine Candidates of <i>Trueperella Pyogenes</i> in a Mouse Model: Pyolysin Oligomerization and Structural Change Affect the Efficacy of Pyolysin-Based Vaccines
title_full_unstemmed Evaluation of the Potency of Two Pyolysin-Derived Recombinant Proteins as Vaccine Candidates of <i>Trueperella Pyogenes</i> in a Mouse Model: Pyolysin Oligomerization and Structural Change Affect the Efficacy of Pyolysin-Based Vaccines
title_short Evaluation of the Potency of Two Pyolysin-Derived Recombinant Proteins as Vaccine Candidates of <i>Trueperella Pyogenes</i> in a Mouse Model: Pyolysin Oligomerization and Structural Change Affect the Efficacy of Pyolysin-Based Vaccines
title_sort evaluation of the potency of two pyolysin derived recombinant proteins as vaccine candidates of i trueperella pyogenes i in a mouse model pyolysin oligomerization and structural change affect the efficacy of pyolysin based vaccines
topic <i>trueperella pyogenes</i>
pyolysin
recombinant antigens
vaccine efficacy
oligomerization and structural changes
url https://www.mdpi.com/2076-393X/8/1/79
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AT hongminliang evaluationofthepotencyoftwopyolysinderivedrecombinantproteinsasvaccinecandidatesofitrueperellapyogenesiinamousemodelpyolysinoligomerizationandstructuralchangeaffecttheefficacyofpyolysinbasedvaccines
AT bingwang evaluationofthepotencyoftwopyolysinderivedrecombinantproteinsasvaccinecandidatesofitrueperellapyogenesiinamousemodelpyolysinoligomerizationandstructuralchangeaffecttheefficacyofpyolysinbasedvaccines
AT boma evaluationofthepotencyoftwopyolysinderivedrecombinantproteinsasvaccinecandidatesofitrueperellapyogenesiinamousemodelpyolysinoligomerizationandstructuralchangeaffecttheefficacyofpyolysinbasedvaccines
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