Safety and Efficacy Testing of a Novel Multivalent Bovine Bacterial Respiratory Vaccine Composed of Five Bacterins and Two Immunogens

Cho, Yun Sang; Lee, Hee Soo; Lim, Sook-Kyoung; Joo, Yi-Seok; Kim, Jong Man; Kim, Jae-Hoon

doi:10.1292/jvms.70.959

Cited by 7 publications

(3 citation statements)

References 18 publications

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“…T. pyogenes vaccines have been developed since the 1950s [2]. T. pyogenes bacterin toxoid and genetic toxoid were widely tested for their potency against T. pyogenes infections or challenge in experimental animals and livestock [6][7][8][9][10]. Inactivated whole T. pyogenes culture was also used as vaccine antigen [11,12].…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2020

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Trueperella pyogenes (T. pyogenes) is an important opportunistic pathogen in livestock and wild animals. However, only one commercial T. pyogenes vaccine is currently available, and its immunoprotective effect is not ideal. Pyolysin (PLO) is one of the important virulence factors expressed by T. pyogenes and one of the targets for the development of new T. pyogenes vaccines. In this study, we constructed two recombinant antigens, tPLOA1 (contains amino acids 1–110 and domain 4 of the PLO molecule) and tPLOA2 (contains amino acids 190–296 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 T. pyogenes. 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 T. pyogenes vaccines.

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Section: Introductionmentioning

confidence: 99%

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

et al. 2020

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“…Commercial vaccines against BRD are monovalent or divalent, limiting their efficacy. Recent studies have focused on multivalent vaccines containing antigenic proteins to simplify the vaccination schedule and increase the protection range (Cho et al, 2008) as well as genetic fusions to deliver diverse antigens to the immune system (Ayalew et al, 2008). On the other hand, a proper adjuvant plays an important role in the success of the vaccine formulations containing recombinant proteins (Buchman et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Immunogenicity and protective efficacy of the recombinant Pasteurella lipoprotein E and outer membrane protein H from Pasteurella multocida A:3 in mice

Okay

Özcengīz

Gürsel

et al. 2012

Research in Veterinary Science

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Pasteurella multocida serotype A:3 is a Gram-negative bacterial pathogen, one of the causative agents of shipping fever of cattle. In this study, outer membrane protein H (ompH) and Pasteurella lipoprotein E (plpE) genes were cloned and plpEC-ompH fusion was constructed and expressed in Escherichia coli. Recombinant PlpE, OmpH and PlpEC-OmpH fusion proteins were purified and formulated with oil-based and oil-based CpG ODN adjuvants. Antibody responses in mice vaccinated with recombinant PlpE and PlpEC-OmpH proteins formulated with both adjuvants were significantly (p<0.05) increased. However, a significant (p<0.05) increment in serum IFN-γ level was only observed upon immunization with oil-based CpG formulations. Protectivity of the vaccines were evaluated via intraperitoneal challenge of mice with 10 LD50 of P. multocida A:3. The recombinant proteins PlpE and PlpEC-OmpH fusion conferred 100% protection when formulated with oil-based CpG ODN while the protectivity was found to be 80% and 60%, respectively when only oil-based adjuvant was used in respective formulations. These findings indicated that the recombinant PlpE or PlpEC-OmpH fusion proteins formulated with oil-based CpG ODN adjuvant are possible acellular vaccine candidates against shipping fever.

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“…A multivalent vaccine for bovine bacterial respiratory disease was developed to simplify the vaccination schedule and increase the range of protection, composed of two immunogens and five bacterins (including attenuated H. somni) (5). However, similarly developed commercial vaccines produce diverse secondary effects due to the high lipooligosaccharide content of the cell walls of Gram-negative bacteria.…”

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confidence: 99%

Two Outer Membrane Lipoproteins from Histophilus somni Are Immunogenic in Rabbits and Sheep and Induce Protection against Bacterial Challenge in Mice

Guzmán-Brambila¹,

Rojas-Mayorquín²,

Flores-Samaniego³

et al. 2012

Clin. Vaccine Immunol.

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dHistophilus somni is an economically important pathogen of cattle and other ruminants and is considered one of the key components of the bovine respiratory disease (BRD) complex, the leading cause of economic loss in the livestock industry. BRD is a multifactorial syndrome, in which a triad of agents, including bacteria, viruses, and predisposing factors or "stressors," combines to induce disease. Although vaccines against H. somni have been used for many decades, traditional bacterins have failed to demonstrate effective protection in vaccinated animals. Hence, the BRD complex continues to produce strong adverse effects on the health and well-being of stock and feeder cattle. The generation of recombinant proteins may facilitate the development of more effective vaccines against H. somni, which could confer better protection against BRD. In the present study, primers were designed to amplify, clone, express, and purify two recombinant lipoproteins from H. somni, p31 (Plp4) and p40 (LppB), which are structural proteins of the outer bacterial membrane. The results presented here demonstrate, to our knowledge for the first time, that when formulated, an experimental vaccine enriched with these two recombinant lipoproteins generates high antibody titers in rabbits and sheep and exerts a protective effect in mice against septicemia induced by H. somni bacterial challenge.

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Safety and Efficacy Testing of a Novel Multivalent Bovine Bacterial Respiratory Vaccine Composed of Five Bacterins and Two Immunogens

Cited by 7 publications

References 18 publications

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

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

Immunogenicity and protective efficacy of the recombinant Pasteurella lipoprotein E and outer membrane protein H from Pasteurella multocida A:3 in mice

Two Outer Membrane Lipoproteins from Histophilus somni Are Immunogenic in Rabbits and Sheep and Induce Protection against Bacterial Challenge in Mice

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