Fructose 1,6-Bisphosphate aldolase, a novel immunogenic surface protein on listeria species (original) (raw)

• Mercelo L. Mendonça, Universidade Federal Rural de Pernambuco
• Gustavo Marçal Schmidt Garcia Moreira, Technische Universitat Braunschweig, Department of Biotechnology, Braunschweig, Germany
• Fabrício Fabrício Conceição, Universidade Federal de Pelotas, Pelotas, Brazil
• Michael Hust, Technische Universitat Braunschweig, Department of Biotechnology, Braunschweig, Germany
• Karla Sequeira Mendonça, Universidade Federal de Pelotas, Departamento de Ciência e Tecnologia Agroindustrial, Pelotas, Brazil
• Ângela Nunes Moreira, Universidade Federal de Pelotas, Centro de Desenvolvimento Tecnológico, Pelotas, Brazil
• Rodrigo Correa Orrea França, Universidade Federal de Pelotas, Laboratório de Imunologia Aplicada, Pelotas, Brazil
• Wladimir Padilha Da Silva, Universidade Federal de Pelotas, Programa de Pós-Graduação em Biotecnologia (PPGB), Pelotas, Brazil
• Arun K. Bhunia, Purdue University, Department of Food Science, West Lafayette, United States
• José Antônio Guimarães Uimarães Aleixo, Laboratório de Imunologia Aplicada, Pelotas, BrazilFollow

Abstract

Listeria monocytogenes is a ubiquitous food-borne pathogen, and its presence in food or production facilities highlights the importance of surveillance. Increased understanding of the surface exposed antigens on Listeria would provide potential diagnostic and therapeutic targets. In the present work, using mass spectrometry and genetic cloning, we show that fructose-1,6-bisphosphate aldolase (FBA) class II in Listeria species is the antigen target of the previously described mAb-3F8. Western and dot blot assays confirmed that the mAb-3F8 could distinguish all tested Listeria species from close-related bacteria. Localization studies indicated that FBA is present in every fraction of Listeria cells, including supernatant and the cell wall, setting Listeria spp. as one of the few bacteria described to have this protein on their cell surface. Epitope mapping using ORFeome display and a peptide membrane revealed a 14-amino acid peptide as the potential mAb-3F8 epitope. The target epitope in FBA allowed distinguishing Listeria spp. from closely-related bacteria, and was identified as part of the active site in the dimeric enzyme. However, its function in cell surface seems not to be host cell adhesion-related. Western and dot blot assays further demonstrated that mAb-3F8 together with anti-InlA mAb-2D12 could differentiate pathogenic from non-pathogenic Listeria isolated from artificially contaminated cheese. In summary, we report FBA as a novel immunogenic surface target useful for the detection of Listeria genus. © 2016 Mendonça et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Date of this Version

8-2016

DOI

10.1371/journal.pone.0160544

Recommended Citation

Mendonça, M., Moreira, G.M.S.G., Conceição, F.R., Hust, M., Mendonça, K.S., Moreira, Â.N., França, R.C., Silva, W.P.D., Bhunia, A.K. , Aleixo, J.A.G. Fructose 1,6-Bisphosphate aldolase, a novel immunogenic surface protein on listeria species. PLoS ONE Volume 11, Issue 8, August 2016, Article number e0160544. http://dx.doi.org/10.1371/journal.pone.0160544

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