TLR-9 dependent dendritic cells activation by filamentous bacteriophage targeting DEC-205
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1
Institute of Protein Biochemistry-CNR, Italy
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2
TIGEM-Telethon Institute of Genetics and Medicine, Italy
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3
Institute of Genetics and Biophysics “Adriano Buzzati Traverso”-CNR, Italy
Based on a modification of the phage display technology, we developed and described an antigen delivery system based on the filamentous bacteriophage fd, able to elicit full-spectrum of antigen-specific immune responses. We improved this system by constructing phage particles displaying a single chain antibody fragment known to bind the mouse dendritic cells (DC) surface molecule DEC-205, and thus enabling direct delivery of phage particles to DC. We demonstrated that targeting DCs via DEC-205 delivers phage particles into late endosome/lysosome LAMP-1 positive compartments. Moreover we observed that DCs targeted by fd virions via DEC-205 upregulate accessory molecules, produce IFN-alpha and IL-6, and mediate an increased antigen presentation. We found that these activities of fd-antiDEC-205 phage particles were TLR-9 dependent. Since to become active TLR-9 translocate into LAMP-1 positive compartments, we suggest that phage particles, containing a single strand DNA genome reach in CpG motifs, are able to intercept and trigger the active TLR-9 innate immune receptor and thus to enhance the immunogenicity of the displayed antigenic determinants.
Keywords:
TLR-9,
innate immunity.,
Dendritic Cells,
DEC-205,
filamentous bacteriophage fd
Conference:
15th International Congress of Immunology (ICI), Milan, Italy, 22 Aug - 27 Aug, 2013.
Presentation Type:
Abstract
Topic:
Innate immunity
Citation:
Sartorius
R,
D'Apice
L,
Trovato
M,
De Leo
G,
De Matteis
A,
Barba
P and
De Berardinis
P
(2013). TLR-9 dependent dendritic cells activation by filamentous bacteriophage targeting DEC-205.
Front. Immunol.
Conference Abstract:
15th International Congress of Immunology (ICI).
doi: 10.3389/conf.fimmu.2013.02.00884
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Received:
21 Jun 2013;
Published Online:
22 Aug 2013.
*
Correspondence:
Dr. Rossella Sartorius, Institute of Protein Biochemistry-CNR, naples, Italy, rossella.sartorius@ibbc.cnr.it