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Identification of immunogenic proteins of the bacterium Acinetobacter baumannii using a proteomic approach
Version of Record online: 28 AUG 2014
© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
PROTEOMICS - Clinical Applications
Special Issue: Focus on Proteomics in Paediatrics
Volume 8, Issue 11-12, pages 916–923, December 2014
How to Cite
Fajardo Bonin, R., Chapeaurouge, A., Perales, J., da Silva, J. G., do Nascimento, H. J., D'Alincourt Carvalho Assef, A. P. and Moreno Senna, J. P. (2014), Identification of immunogenic proteins of the bacterium Acinetobacter baumannii using a proteomic approach. Prot. Clin. Appl., 8: 916–923. doi: 10.1002/prca.201300133
- Issue online: 2 DEC 2014
- Version of Record online: 28 AUG 2014
- Accepted manuscript online: 4 JUN 2014 06:05PM EST
- Manuscript Accepted: 28 MAY 2014
- Manuscript Revised: 8 APR 2014
- Manuscript Received: 26 DEC 2013
- Fundação de Amparo à Pesquisa do Estado do Rio de Janeiro
- Conselho Nacional de Desenvolvimento Científico e Tecnológico
- Acinetobacter baumannii;
- Hospital infection;
Acinetobacter baumannii is an important opportunistic pathogen that causes pneumoniae, urinary tract infections, and/or septicemia in immunocompromised patients. This pathogen is frequently associated with nosocomial outbreaks worldwide and has become particularly problematic because of its prevalence and resistance patterns to several antibiotics. In the present study, we used an immunoproteome-based approach to identify immunogenic proteins located on the surface of A. baumannii for the development of a possible immunotherapy against this devastating bacterial infection.
Sera from patients with A. baumannii infections (n = 50) and from a control group of healthy individuals (n = 3) were analyzed for reactivity against A. baumannii outer membrane proteins (OMPs) using Western blot analysis. To identify potential immunogenic proteins in A. baumannii, OMPs were separated by 2DE, and reactive sera from infected patients were randomly selected and divided into two different pools, each containing 15 sera. Finally, MALDI-TOF/TOF mass spectrometric analysis was employed to identify the corresponding proteins.
This analysis identified six immunoreactive proteins: OmpA, Omp34kDa, OprC, OprB-like, OXA-23, and ferric siderophore receptor protein. Notably, these proteins are highly abundant on the bacterial surface and involved in virulence, antibiotic resistance, and growth.
Conclusions and clinical relevance
Our results support the notion that the proteins identified in the present immunoproteome study could serve as antigen candidates for the development of vaccines and passive immunotherapies against A. baumannii infections.