The Journal of Experimental Medicine
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Published online March 3, 2008
doi:10.1084/jem.20071734
The Journal of Experimental Medicine, Vol. 205, No. 3, 657-667
The Rockefeller University Press, 0022-1007 $30.00
© 2008 Rotta et al.
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ARTICLE

 Contrasting roles of SPARC-related granuloma in bacterial containment and in the induction of anti–Salmonella typhimurium immunity

Gianluca Rotta1, Gianluca Matteoli1, Elisa Mazzini1, Paolo Nuciforo1, Mario P. Colombo2, and Maria Rescigno1

1 Department of Experimental Oncology, European Institute of Oncology, 20141 Milan, Italy
2 Immunotherapy and Gene Therapy Unit, Istituto Nazionale per lo Studio e la Cura dei Tumori, 20133 Milan, Italy

CORRESPONDENCE Maria Rescigno: maria.rescigno{at}ifom-ieo-campus.it

The role of matricellular proteins in bacterial containment and in the induction of pathogen-specific adaptive immune responses is unknown. We studied the function of the matricellular protein secreted protein, acidic and rich in cysteine (SPARC/osteonectin) in the dissemination of locally injected Salmonella typhimurium and in the subsequent immune response. We show that SPARC was required for the development of organized acute inflammatory reactions with granuloma-like (GL) features and for the control of bacterial spreading to draining lymph nodes (DLNs). However, SPARC-related GL also inhibited dendritic cell (DC) migration to the DLNs and limited the development of adaptive immune response, thus conferring increased susceptibility to the pathogen. In SPARC-deficient mice, both DC migration and antigen-specific responses were restored against bacteria, leading to protective anti–S. typhimurium immunity. This highlights a new function of matricellular proteins in bacterial infection and suggests that initial containment of bacteria can have drawbacks.

Abbreviations used: DLN, draining LN; ECM, extracellular matrix; GL, granuloma-like; GLR, GL reaction; i.d., intradermal; LB, Luria broth; MMP, matrix metalloproteinase; OCT, optimal cutting compound; SPARC, secreted protein, acidic and rich in cysteine; TSP, thrombospondin.

G. Rotta and G. Matteoli contributed equally to this work.


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