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Applied and Environmental Microbiology, December 2008, p. 7399-7409, Vol. 74, No. 23
0099-2240/08/$08.00+0     doi:10.1128/AEM.00594-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Comparative Analysis of Extracellular and Intracellular Proteomes of Listeria monocytogenes Strains Reveals a Correlation between Protein Expression and Serovar{triangledown} ,{dagger}

Emilie Dumas,1,{ddagger} Bruno Meunier,2 Jean-Louis Berdagué,3 Christophe Chambon,4 Mickaël Desvaux,1 and Michel Hébraud1,4*

UR454 Microbiologie Equipe Qualité et Sécurité des Aliments,1 UR1213 Herbivores Equipe Croissance et Métabolisme du Muscle,2 UR370 Qualité des Produits Animaux Equipe Typicité Aromatique et Authentification,3 Plate-Forme de Protéomique, INRA Centre de Clermont-Ferrand/Theix, F-63122 Saint-Genès Champanelle, France4

Received 12 March 2008/ Accepted 28 September 2008

Listeria monocytogenes, the etiologic agent of listeriosis, remains a serious public health concern, with its frequent occurrence in food environments coupled with a high mortality rate. Among the 13 serovars, human listeriosis is mostly associated with the serovar 4b, 1/2b, and 1/2a strains. To investigate the diversity of L. monocytogenes, the intracellular and extracellular proteins of 12 strains were analyzed by two-dimensional gel electrophoresis. These strains had different origins, belonged to different serovars (4b, 1/2a, and 1/2b), and presented with different levels of virulence in chicken embryos. The clustering of the strains in two groups based on proteomic patterns is in agreement with the L. monocytogenes phylogenetic lineages. Statistical analysis did not allow for identification of proteins specific to the isolate origin or the virulence level of the strains, but 26 and 21 protein spots were shown to be significantly overexpressed and underexpressed, respectively, in the six strains of serovar 1/2a (lineage II) compared to strains of serovar 1/2b or 4b. Moreover, a penicillin-binding protein was specific for serovar 1/2b and two protein spots identified as a serine protease were specific to serovar 4b. These protein spots, identified through peptide mass fingerprinting using matrix-assisted laser desorption ionization-time of flight mass spectrometry, were essentially found in the extracellular proteome and may have uses as potential markers for serotyping and risk analysis.

* Corresponding author. Mailing address: UR454 Microbiologie, Equipe Qualité et Sécurité des Aliments, INRA Centre de Clermont-Ferrand/Theix, F-63122 Saint-Genès Champanelle, France. Phone: (33) 473 62 46 70. Fax: (33) 473 62 45 81. E-mail: hebraud{at}clermont.inra.fr

{triangledown} Published ahead of print on 3 October 2008.

{dagger} Supplemental material for this article may be found at http://aem.asm.org/.

{ddagger} Present address: Génomique Intégrée des Interactions Microbiennes, Laboratoire Microorganismes: Génome et Environnement, UMR CNRS 6023, Université Blaise Pascal, 24 avenue des Landais, Campus des Cézeaux, 63177 Aubière Cedex, France.

Applied and Environmental Microbiology, December 2008, p. 7399-7409, Vol. 74, No. 23
0099-2240/08/$08.00+0     doi:10.1128/AEM.00594-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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