Open AccessAntibody‐ and TRIM 21‐dependent intracellular restriction of Salmonella enterica
Author(s) -
Rakebrandt Nikolas,
Lentes Sabine,
Neumann Heinz,
James Leo C.,
NeumannStaubitz Petra
Publication year - 2014
Publication title -
pathogens and disease
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.983
H-Index - 105
ISSN - 2049-632X
DOI - 10.1111/2049-632x.12192
Subject(s) - intracellular , salmonella enterica , antibody , salmonella , immunity , biology , microbiology and biotechnology , intracellular parasite , virology , cytosol , pathogen , bacteria , immune system , immunology , genetics , biochemistry , enzyme
TRIM 21 (‘tripartite motif‐containing protein 21’, Ro52) is a ubiquitously expressed cytosolic Fc receptor, which has a potent role in protective immunity against nonenveloped viruses. TRIM 21 mediates intracellular neutralisation of antibody‐coated viruses, a process called ADIN (antibody‐dependent intracellular neutralisation). Our results reveal a similar mechanism to fight bacterial infections. TRIM 21 is recruited to the intracellular pathogen Salmonella enterica in epithelial cells early in infection. TRIM 21 does not bind directly to S. enterica , but to antibodies opsonising it. Most importantly, bacterial restriction is dependent on TRIM 21 as well as on the opsonisation state of the bacteria. Finally, Salmonella and TRIM 21 colocalise with the autophagosomal marker LC 3, and intracellular defence is enhanced in starved cells suggesting an involvement of the autophagocytic pathway. Our data extend the protective role of TRIM 21 from viruses to bacteria and thereby strengthening the general role of ADIN in cellular immunity.