Interaction of Brucella abortus Lipopolysaccharide with Major Histocompatibility Complex Class II Molecules in B Lymphocytes

Author:

Forestier Claire1,Moreno Edgardo2,Méresse Stéphane1,Phalipon Armelle3,Olive Daniel4,Sansonetti Philippe3,Gorvel Jean-Pierre1

Affiliation:

1. Centre d’Immunologie INSERM-CNRS de Marseille-Luminy, 13288 Marseille Cedex 9,1

2. Tropical Disease Research Program, School of Veterinary Medicine, Universidad Nacional, Heredia, Costa Rica2

3. Unité de Pathogénie Microbienne Moléculaire, INSERM U389, Institut Pasteur, 75724 Paris Cedex 15,3 France, and

4. INSERM U119, 13009 Marseille,4 and

Abstract

ABSTRACT Lipopolysaccharide (LPS), a major amphiphilic molecule located at the outer membrane of gram-negative bacteria, is a potent antigen known to induce specific humoral immune responses in infected mammals. LPS has been described as a polyclonal activator of B lymphocytes, triggering the secretion of antibodies directed against distinct sugar epitopes of the LPS chain. But, how LPS is handled by B cells remains to be fully understood. This task appears to be essential for a better knowledge of the anti-LPS humoral immune response. In this study, we examine the internalization of LPS and its interaction with antigen-presenting major histocompatibility complex (MHC) class II molecules in murine and human B-cell lines. By use of immunofluorescence, we observe that structurally different LPSs from Brucella and Shigella strains accumulate in an intracellular compartment enriched in MHC class II molecules. By use of immunoprecipitation, we illustrate that only Brucella abortus LPS associates with MHC class II molecules in a haplotype-independent manner. Taken together, these results raise the possibility that B. abortus LPS may play a role in T-cell activation.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Immunology,Microbiology,Parasitology

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