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Microbiology 155 (2009), 1580-1587; DOI  10.1099/mic.0.026278-0
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Microbiology 155 (2009), 1580-1587; DOI  10.1099/mic.0.026278-0
© 2009 Society for General Microbiology

Protective capacities of cell surface-associated proteins of Streptococcus suis mutants deficient in divalent cation-uptake regulators

Jesús Aranda1, Maria Elena Garrido1,2, Nahuel Fittipaldi3, Pilar Cortés1,4, Montserrat Llagostera1,2, Marcelo Gottschalk3 and Jordi Barbé1,2

1 Department de Genètica i Microbiologia, Universitat Autònoma de Barcelona (UAB), Bellaterra, 08193 – Barcelona, Spain
2 Centre de Recerca en Sanitat Animal (CReSA), Bellaterra, 08193 – Barcelona, Spain
3 Groupe de Recherche sur les Maladies Infectieuses du Porc and Centre de Recherche en Infectiologie Porcine, Faculté de Médecine Vétérinaire, Université de Montréal, St-Hyacinthe, QC J2S 7C6, Canada
4 Servei d'Anàlisis i d'Aplicacions Microbiològiques, UAB, Bellaterra, 08193 – Barcelona, Spain

Many cell surface-associated, divalent cation-regulated proteins are immunogenic, and some of them confer protection against the bacterial species from which they are derived. In this work, two Streptococcus suis divalent cation uptake regulator genes controlling zinc/manganese and iron uptake (adcR and fur, respectively) were inactivated in order to study the protective capacities of their cell surface-associated proteins. The results obtained showed overexpression of a set of immunogenic proteins (including members of the pneumococcal histidine triad family previously reported to confer protection against streptococcal pathogens) in S. suis adcR mutant cell surface extracts. Likewise, genes encoding zinc transporters, putative virulence factors and a ribosomal protein paralogue related to zinc starvation appeared to be derepressed in this mutant strain. Moreover, protection assays in mice showed that although neither adcR- nor fur-regulated cell surface-associated proteins were sufficient to confer protection in mice, the combination of both adcR- and fur-regulated cell surface-associated proteins is able to confer significant protection (50 %, P=0.038) against a challenge to mice vaccinated with them.

Correspondence
Jordi Barbé
jordi.barbe{at}uab.cat

Abbreviations: ABC, ATP-binding cassette; EMSA, electrophoretic mobility shift assay

Two supplementary tables, listing bacterial strains and plasmids and oligonucleotide primers used in this work, are available with the online version of this paper.






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