Porcine antibody profiles of 33 Mycoplasma hyopneumoniae fusion proteins from M. hyopneumoniae natural infection but not vaccination.


Journal

Veterinary medicine and science
ISSN: 2053-1095
Titre abrégé: Vet Med Sci
Pays: England
ID NLM: 101678837

Informations de publication

Date de publication:
01 2023
Historique:
pubmed: 16 12 2022
medline: 25 1 2023
entrez: 15 12 2022
Statut: ppublish

Résumé

Mycoplasma hyopneumoniae, the primary pathogen responsible for porcine enzootic pneumonia, reduces average daily weight gain and causes substantial economic losses to the pig industry worldwide. Vaccination is the most common strategy to control this disease but offers partial protection. Therefore, developing next-generation vaccines by screening protective antigens is crucial. The aim of this study was to evaluate the antibody response to 33 recombinant proteins in pigs naturally infected with M. hyopneumoniae. The genes encoding 33 (hypothetical) membrane proteins or secretory proteins were ligated into pGEX-6P-1, pGEX-6P-2, pGEX-5X-3 or pGEX-4T-3 vectors and transformed into Escherichia coli BL21(DE3) or E. coli XL-1 Blue to construct recombinant bacteria and to express the recombinant proteins. The recombinant bacteria expressing the target proteins reacted with porcine convalescent sera and negative sera to screen immunodominant proteins by ELISA. Then, recombinant bacteria expressing immunodominant proteins were used to identify the discriminating immunodominant proteins that were recognised by convalescent sera nut not hyperimmune sera. All recombinant bacteria could express the target recombinant proteins in soluble form. Twenty-one proteins were shown to present immunodominant antigens, and four proteins were not recognised by convalescent sera. Moreover, six proteins were considered discriminating and reacted with convalescent sera but not with hyperimmune sera. The identified immunodominant proteins were antigenic and expressed during bacterial infection, suggesting that these proteins, especially those capable of discriminating between sera, can be used to identify protective antigens with the view to develop more effective vaccines against M. hyopneumoniae infection.

Sections du résumé

BACKGROUND
Mycoplasma hyopneumoniae, the primary pathogen responsible for porcine enzootic pneumonia, reduces average daily weight gain and causes substantial economic losses to the pig industry worldwide. Vaccination is the most common strategy to control this disease but offers partial protection. Therefore, developing next-generation vaccines by screening protective antigens is crucial.
OBJECTIVES
The aim of this study was to evaluate the antibody response to 33 recombinant proteins in pigs naturally infected with M. hyopneumoniae.
METHODS
The genes encoding 33 (hypothetical) membrane proteins or secretory proteins were ligated into pGEX-6P-1, pGEX-6P-2, pGEX-5X-3 or pGEX-4T-3 vectors and transformed into Escherichia coli BL21(DE3) or E. coli XL-1 Blue to construct recombinant bacteria and to express the recombinant proteins. The recombinant bacteria expressing the target proteins reacted with porcine convalescent sera and negative sera to screen immunodominant proteins by ELISA. Then, recombinant bacteria expressing immunodominant proteins were used to identify the discriminating immunodominant proteins that were recognised by convalescent sera nut not hyperimmune sera.
RESULTS
All recombinant bacteria could express the target recombinant proteins in soluble form. Twenty-one proteins were shown to present immunodominant antigens, and four proteins were not recognised by convalescent sera. Moreover, six proteins were considered discriminating and reacted with convalescent sera but not with hyperimmune sera.
CONCLUSIONS
The identified immunodominant proteins were antigenic and expressed during bacterial infection, suggesting that these proteins, especially those capable of discriminating between sera, can be used to identify protective antigens with the view to develop more effective vaccines against M. hyopneumoniae infection.

Identifiants

pubmed: 36520664
doi: 10.1002/vms3.1053
pmc: PMC9857121
doi:

Substances chimiques

Antigens, Bacterial 0
Recombinant Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

203-216

Informations de copyright

© 2022 The Authors. Veterinary Medicine and Science published by John Wiley & Sons Ltd.

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Auteurs

Yaru Ning (Y)

Laboratory of Veterinary Mycoplasmology, College of Veterinary Medicine, Southwest University, Chongqing, China.

Yujiao Yang (Y)

Laboratory of Veterinary Mycoplasmology, College of Veterinary Medicine, Southwest University, Chongqing, China.

Yaqin Tian (Y)

Laboratory of Veterinary Mycoplasmology, College of Veterinary Medicine, Southwest University, Chongqing, China.

Yun Zhang (Y)

Laboratory of Veterinary Mycoplasmology, College of Veterinary Medicine, Southwest University, Chongqing, China.

Wenyi Luo (W)

The 181st Group of the Tenth Division, Xinjiang Production and Construction Corps, Beitun, Xinjiang, China.

Yukang Wen (Y)

Laboratory of Veterinary Mycoplasmology, College of Veterinary Medicine, Southwest University, Chongqing, China.

Yaoqin Zhou (Y)

College of Optoelectronic Engineering, Chongqing University, Chongqing, China.

Honglei Ding (H)

Laboratory of Veterinary Mycoplasmology, College of Veterinary Medicine, Southwest University, Chongqing, China.

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Classifications MeSH