Bacteria-induced neo-biosynthesis, stabilization, and surface expression of functional class I molecules in mouse dendritic cells - PubMed
- ️Thu Jan 01 1998
Bacteria-induced neo-biosynthesis, stabilization, and surface expression of functional class I molecules in mouse dendritic cells
M Rescigno et al. Proc Natl Acad Sci U S A. 1998.
Erratum in
- Proc Natl Acad Sci U S A 1999 Aug 17;96(17):9666
Abstract
Here, we show that bacteria induce de novo synthesis of both major histocompatability complex (MHC) class I and II molecules in a mouse dendritic cell culture system. The neo-biosynthesis of MHC class I molecules is delayed as compared with that of MHC class II. Furthermore, bacteria stabilize MHC class I molecules by a 3-fold increase of their half-life. This has important consequences for the capacity of dendritic cells to present bacterial antigens in the draining lymph nodes. In addition, a model antigen, ovalbumin, expressed on the surface of recombinant Streptococcus gordonii is processed and presented on MHC class I molecules. This presentation is 10(6) times more efficient than that of soluble OVA protein. This exogenous pathway of MHC class I presentation is transporter associated with antigen processing (TAP)-dependent, indicating that there is a transport from phagolysosome to cytosol in dendritic cells. Thus, bacteria are shown to be a potentially useful mean for the correct delivery of exogenous antigens to be presented efficiently on MHC class I molecules.
Figures
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DC internalize S. gordonii via conventional phagocytosis. DC were incubated with bacteria for different time periods at a ratio of 10 bacteria to 1 DC, then washed and processed for transmission electron microscopy. (A) Thirty minutes after infection, bacteria were contacting the cell membrane and inducing local thickening of plasma membrane (arrows) (magnification, ×39,000; bar represents 3.9 μm). (B) Four hours after infection, bacteria were found in phagolysosomes in a partially degraded form (arrow) at a magnification of ×28,700; bar = 2.9 μm.

Phenotypical maturation of D1 cells. FACS profiles of surface markers after incubation with S. gordonii at a ratio of 10 bacteria to 1 DC (Left) or latex beads at a ratio of 100 beads to 1 DC (Right). Histograms represent the following: filled, cells after treatment; open, untreated cells; dashed, isotype controls.

S. gordonii-treated DC secrete large amounts of inflammatory cytokines. Culture supernatants from untreated cells (hatched bars), S. gordonii-treated D1 (black bars), or R1 culture medium (white bars) were tested for cytokine release by ELISA. Recombinant cytokines were used as standards in each ELISA.
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Bacterial infection induces de novo synthesis and stabilization of MHC class I molecules. (A) DC were metabolically labeled before (t = 0) or at different times (t = 1–36 h) after bacterial infection. HCm, heavy chain mature form; HCi, heavy chain immature form; a, actin; β2 m, β2 microglobulin. The graph shows the quantification by Phosphorimager of the radioactivity associated with MHC I heavy chain. A.U., arbitrary units. (B) Stability of MHC I molecules synthesized by untreated cells (Top) or by cells treated for 18 h with bacteria (Bottom). Cells were biosynthetically labeled and chased for 0–48 h in an excess of cold methionine. Abbreviations are as in A. The graph represents the quantification by
bio-1dsoftware of the radioactivity associated with MHC I molecules in treated and untreated DC chased in the absence of bacteria.

Bacterial infection induces de novo synthesis and stabilization of MHC class II molecules. (A) DC were metabolically labeled before (t = 0) or at different times (t = 1–36 h) after bacterial infection. α + Ii, alpha chain + invariant chain; β, beta chain. The graph shows the quantification by Phosphorimager of the radioactivity associated with the α-chains. (B) Stability of mature MHC class II molecules synthesized by untreated cells (Top) or cells treated for 18 h with bacteria (Bottom). α, alpha chain; β, beta chain. The graph represents the quantification by
bio-1dsoftware of the radioactivity associated with β-chains in DC incubated or not with bacteria and then chased in the absence of bacteria.

DC can process bacterial antigens for MHC I presentation very efficiently. DC were incubated with recombinant OVA-gordonii (GP1252, ○), wild-type gordonii (GP204) + exogenous OVA (◊), or OVA alone (•) for 16 h and then washed and fixed. The ratio of bacteria to DC ranges from 500:1 to 0.3:1. Ratio of 500 bacteria to 1 DC corresponds to 1 μg/ml of OVA. IL-2 production by B3Z T cell hybridoma was measured as [3H]thymidine incorporation by IL-2-dependent CTL.

MHC class I presentation of bacterial antigens is TAP dependent. The B3Z hybridoma response to BM-derived TAP−/− DC (A and C) or to D1 TAP+/+ (B) incubated with the following is shown: (A and B) OVA-gordonii (GP1252, •) or wild-type gordonii (GP204, ○); (C) soluble OVA (○) or SIINFEKL peptide. (•).
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