Immunizing mice using different combination antigens of the PI-2a fimbria subunit of Streptococcus agalactiae

Document Type : Full paper (Original article)

Authors

1 Key Laboratory of Preventive Veterinary Medicine and Animal Biotechnology, Shandong Binzhou Animal Science and Veterinary Medicine Academy, Binzhou, 256600, China

2 Inner Mongolia Autonomous Region Engineering Technology Research Center of Prevention and Control the Pathogenic Bacteria in Milk, Tongliao 028043, China

3 Shandong Lvdu Bio-Sciences and Technology Co., Ltd., Binzhou, 256600, China

Abstract

Background: Streptococcus agalactiae is the main causal pathogen of bovine mastitis (BM), causing considerable economic loss to the dairy industry worldwide. Vaccines against S. agalactiae play an important role in preventing disease. Aims: The aim of this study was to evaluate the immunoprotection of S. agalactiae pilus island fusion proteins, ancillary protein 1-ancillary protein 2 (AP1-AP2), ancillary protein 1-bone protein (AP1-BP), bone protein-ancillary protein 2 (BP-AP2), and ancillary protein 1-bone protein-ancillary protein 2 (AP1-BP-AP2) in Balb/c mice. Methods: Four kinds of fusion antigens and the same volume of Freund’s complete adjuvant were mixed vigorously to prepare fusion antigen immuno-samples. The mice were immunized 4 times (on the 0th, 7th, 14th, and 28th days) with these samples with an immunizing dose of 50 mg/mouse. After the 4th immunization, serology tests were used to evaluate the antibody. The antibody titre produced by AP1-BP-AP2 fusion antigen was the highest, at up to 1:25600. The mice were then injected with 0.5 ml of 2 × 104 CFU/ml clinically isolated S. agalactiae at day 50 and observed daily for the following 7 days. Results: Statistical analyses showed that these 4 kinds of fusion antigens had good protective immunity. Among them, AP1-BP-AP2 fusion antigen had the best protective immunity in Balb/c mice, with an immune protection index (PI) of 80%. Conclusion: This research provides a reliable theoretical basis for screening candidate antigens of the subunit vaccine and detecting antigen preparations of S. agalactiae.

Keywords

References

Brochet, M; Couvé, E; Glaser, P; Guédon, G and Payot, S (2008). Integrative conjugative elements and related elements are major contributors to the genome diversity of Streptococcus agalactiae. J. Bacteriol., 190: 6913-6917.
Brodeur, BR; Boyer, M; Charlebois, I; Hamel, J; Couture, F; Rioux, CR and Martin, D (2000). Identification of group B streptococcal Sip protein, which elicits cross-protective immunity. Infect. Immun., 68: 5610-5618.
Du, L and Hao, YQ (2016). Drug resistance and tetracycline resistance gene identification of Streptococcus agalactiae isolates from bovine in Inner Mongolia. J. Huazhong Agr. Univ., 01: 114-119.
Fan, WH; Zhao, MC and Liu, J (2014). Antimicrobial resistance in 42 cases of neonate septicemia caused by Streptococcus agalactiae infection. Int. J. Lab. Med., 17: 2309-2310.
Herrera Ramírez, JC; De la Mora, A; De la Mora Valle, A; Lopez-Valencia, G; Hurtado, RM; Rentería Evangelista, TB; Rodríguez Castillo, JL; Rodríguez Gardea, A; Gómez Gómez, SD and Medina-Basulto, GE (2017). Immunopathological evaluation of recombinant mycobacterial antigen Hsp65 expressed in Lactococcus lactis as a novel vaccine candidate. Iran. J. Vet. Res., 18: 197-202.
Khara, B and Narayana, VL (2017). Pilus biogenesis of Gram-positive bacteria: roles of sortase and implication for assembly. Protein Sci., 26: 1458-1473.
Khare, B; Krishnan, V and Rajashankar, KR (2011). Structural differences between the Streptococcus agalactiae housekeeping and pilus-specific sortases: SrtA and SrtC1. PLoS One. 6: e22995.
Khodaei, F; Najafi, M and Hasni, A (2018). Pilus-encoding islets in S. agalactiae and its association with antibacterial resistance and serotype distribution. Microb. Pathog., 116: 189-194.
Konto-Ghiorghi, Y; Mairey, E and Mallet, A (2009). Dual role for pilus in adherence to epithelial cells and biofilm formation in Streptococcus agalactiae. PLoS Pathog. 5: e1000422.
Li, HS; Yu, J and Luo, JY (2012). Serotype distribution of bovine Streptococcus agalactiae and its drug resistance to antibiotics in China. Chin. Anim. Husb. & Vet. Med., 01: 164-167.
Mandlik, A; Swierczynski, A; Das, A and Ton-That, H (2008). Pili in Gram-positive bacteria: assembly, involvement in colonization and biofilm development. Trends Microbiol., 16: 33-40.
Martins, ER; Andreu, A; Melo-Cristino, J and Ramirez, M (2013). Distribution of pilus islands in Streptococcus agalactiae that cause human infections: insights into evolution and implication for vaccine development. Clin. Vaccine Immunol., 20: 313-316.
Mukherjee, F; Prasad, A; Bahekar, VS; Rana, SK; Rajendra, L; Sharma, GK and Srinivasan, VA (2017). Evaluation of immunogenicity and protective efficacy of a liposome containing Brucella abortus S19 outer membrane protein in BALB/c mice. Iran. J. Vet. Res., 17: 1-7.
Rosini, R; Rinaudo, CD and Soriani, M (2006). Identification of novel genomic islands coding for antigenic pilus-like structures in Streptococcus agalactiae. Mol. Microbiol., 61: 126-141.
Sharma, P; Lata, H and Arya, DK (2013). Role of pilus proteins in adherence and invasion of Streptococcus agalactiae to the lung and cervical epithelial cells. J. Biol. Chem., 288: 4023-4034.
Xicohtencatl-Cortés, J; Lyons, S; Chaparro, AP; Hernández, DR; Saldaña, Z; Ledesma, MA; Rendón, MA; Gewirtz, AT; Klose, KE and Girón, JA (2006). Identification of proinflammatory flagellin proteins in supernatants of Vibrio cholerae O1 by proteomics analysis. Mol. Cell Proteomics. 5: 2374-2383.
Yang, HH and Li, J (2016). Clinical and prognostic analysis of sepsis caused by Streptococcus agalactiae combined with purulent meningitis in 12 neonates. J. Clin. Pedia., 03: 181-184.

Files

Share

How to cite

Statistics