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Host Langerin (CD207) is a receptor for Yersinia pestis phagocytosis and promotes dissemination.

Yang K, Park CG, Cheong C, Bulgheresi S, Zhang S, Zhang P, He Y, Jiang L, Huang H, Ding H, Wu Y, Wang S, Zhang L, Li A, Xia L, Bartra SS, Plano GV, Skurnik M, Klena JD, Chen T - Immunol. Cell Biol. (2015)

Bottom Line: However, when the bacterial core oligosaccharides are shielded or truncated, Y. pestis propensity to invade Langerhans and Langerin-expressing cells decreases.Furthermore, covering core oligosaccharides reduces the mortality associated with murine infection by adversely affecting the transmission of Y. pestis to lymph nodes.These results demonstrate that direct interaction of core oligosaccharides with Langerin facilitates the invasion of LCs by Y. pestis.

View Article: PubMed Central - PubMed

Affiliation: Department of Clinical Immunology, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, Hubei, China.

ABSTRACT
Yersinia pestis is a Gram-negative bacterium that causes plague. After Y. pestis overcomes the skin barrier, it encounters antigen-presenting cells (APCs), such as Langerhans and dendritic cells. They transport the bacteria from the skin to the lymph nodes. However, the molecular mechanisms involved in bacterial transmission are unclear. Langerhans cells (LCs) express Langerin (CD207), a calcium-dependent (C-type) lectin. Furthermore, Y. pestis possesses exposed core oligosaccharides. In this study, we show that Y. pestis invades LCs and Langerin-expressing transfectants. However, when the bacterial core oligosaccharides are shielded or truncated, Y. pestis propensity to invade Langerhans and Langerin-expressing cells decreases. Moreover, the interaction of Y. pestis with Langerin-expressing transfectants is inhibited by purified Langerin, a DC-SIGN (DC-specific intercellular adhesion molecule 3 grabbing nonintegrin)-like molecule, an anti-CD207 antibody, purified core oligosaccharides and several oligosaccharides. Furthermore, covering core oligosaccharides reduces the mortality associated with murine infection by adversely affecting the transmission of Y. pestis to lymph nodes. These results demonstrate that direct interaction of core oligosaccharides with Langerin facilitates the invasion of LCs by Y. pestis. Therefore, Langerin-mediated binding of Y. pestis to APCs may promote its dissemination and infection.

No MeSH data available.


Related in: MedlinePlus

Purified FLAG-hLangerin and DC-SIGN-like molecules bind to Y. pestis core oligosaccharides. Y. pestis KIM10−, KIM10−-O+, CS180 and CS1861 were incubated with 10 μg of FITC-His-Mermaid and purified FLAG-Langerin for 30 min. The ability of FITC-His-Mermaid and Langerin to bind the bacteria was measured using flow cytometry. The fluorescence intensities of KIM10− or CS180 and KIM10−-O+ or CS1861 are represented by non-filled and filled curves, respectively. E. coli strains CS180 and CS1861 should be regarded as positive and negative controls, respectively, as shown previously.14, 45.
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fig6: Purified FLAG-hLangerin and DC-SIGN-like molecules bind to Y. pestis core oligosaccharides. Y. pestis KIM10−, KIM10−-O+, CS180 and CS1861 were incubated with 10 μg of FITC-His-Mermaid and purified FLAG-Langerin for 30 min. The ability of FITC-His-Mermaid and Langerin to bind the bacteria was measured using flow cytometry. The fluorescence intensities of KIM10− or CS180 and KIM10−-O+ or CS1861 are represented by non-filled and filled curves, respectively. E. coli strains CS180 and CS1861 should be regarded as positive and negative controls, respectively, as shown previously.14, 45.

Mentions: Purified FLAG-Langerin and His-Mermaid have previously been shown to inhibit the interaction between Y. pestis core oligosaccharides and hLangerin. To determine whether this inhibition was due to competition between these two lectins and hLangerin for binding to core oligosaccharides, the abilities of purified FLAG-Langerin and His-Mermaid to bind to KIM10− and KIM10−-O+ were tested. E. coli strains CS180 and CS1861 were included as positive and negative controls, respectively, for the His-Mermaid-binding experiments. Figure 6 shows that purified fluorescein isothiocyanate (FITC)-Langerin and FITC-His-Mermaid bind more strongly to KIM10− and CS180 than to KIM10−-O+ and CS1861, indicating that these two molecules directly interact with the core oligosaccharides of Y. pestis.


Host Langerin (CD207) is a receptor for Yersinia pestis phagocytosis and promotes dissemination.

Yang K, Park CG, Cheong C, Bulgheresi S, Zhang S, Zhang P, He Y, Jiang L, Huang H, Ding H, Wu Y, Wang S, Zhang L, Li A, Xia L, Bartra SS, Plano GV, Skurnik M, Klena JD, Chen T - Immunol. Cell Biol. (2015)

Purified FLAG-hLangerin and DC-SIGN-like molecules bind to Y. pestis core oligosaccharides. Y. pestis KIM10−, KIM10−-O+, CS180 and CS1861 were incubated with 10 μg of FITC-His-Mermaid and purified FLAG-Langerin for 30 min. The ability of FITC-His-Mermaid and Langerin to bind the bacteria was measured using flow cytometry. The fluorescence intensities of KIM10− or CS180 and KIM10−-O+ or CS1861 are represented by non-filled and filled curves, respectively. E. coli strains CS180 and CS1861 should be regarded as positive and negative controls, respectively, as shown previously.14, 45.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4612776&req=5

fig6: Purified FLAG-hLangerin and DC-SIGN-like molecules bind to Y. pestis core oligosaccharides. Y. pestis KIM10−, KIM10−-O+, CS180 and CS1861 were incubated with 10 μg of FITC-His-Mermaid and purified FLAG-Langerin for 30 min. The ability of FITC-His-Mermaid and Langerin to bind the bacteria was measured using flow cytometry. The fluorescence intensities of KIM10− or CS180 and KIM10−-O+ or CS1861 are represented by non-filled and filled curves, respectively. E. coli strains CS180 and CS1861 should be regarded as positive and negative controls, respectively, as shown previously.14, 45.
Mentions: Purified FLAG-Langerin and His-Mermaid have previously been shown to inhibit the interaction between Y. pestis core oligosaccharides and hLangerin. To determine whether this inhibition was due to competition between these two lectins and hLangerin for binding to core oligosaccharides, the abilities of purified FLAG-Langerin and His-Mermaid to bind to KIM10− and KIM10−-O+ were tested. E. coli strains CS180 and CS1861 were included as positive and negative controls, respectively, for the His-Mermaid-binding experiments. Figure 6 shows that purified fluorescein isothiocyanate (FITC)-Langerin and FITC-His-Mermaid bind more strongly to KIM10− and CS180 than to KIM10−-O+ and CS1861, indicating that these two molecules directly interact with the core oligosaccharides of Y. pestis.

Bottom Line: However, when the bacterial core oligosaccharides are shielded or truncated, Y. pestis propensity to invade Langerhans and Langerin-expressing cells decreases.Furthermore, covering core oligosaccharides reduces the mortality associated with murine infection by adversely affecting the transmission of Y. pestis to lymph nodes.These results demonstrate that direct interaction of core oligosaccharides with Langerin facilitates the invasion of LCs by Y. pestis.

View Article: PubMed Central - PubMed

Affiliation: Department of Clinical Immunology, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, Hubei, China.

ABSTRACT
Yersinia pestis is a Gram-negative bacterium that causes plague. After Y. pestis overcomes the skin barrier, it encounters antigen-presenting cells (APCs), such as Langerhans and dendritic cells. They transport the bacteria from the skin to the lymph nodes. However, the molecular mechanisms involved in bacterial transmission are unclear. Langerhans cells (LCs) express Langerin (CD207), a calcium-dependent (C-type) lectin. Furthermore, Y. pestis possesses exposed core oligosaccharides. In this study, we show that Y. pestis invades LCs and Langerin-expressing transfectants. However, when the bacterial core oligosaccharides are shielded or truncated, Y. pestis propensity to invade Langerhans and Langerin-expressing cells decreases. Moreover, the interaction of Y. pestis with Langerin-expressing transfectants is inhibited by purified Langerin, a DC-SIGN (DC-specific intercellular adhesion molecule 3 grabbing nonintegrin)-like molecule, an anti-CD207 antibody, purified core oligosaccharides and several oligosaccharides. Furthermore, covering core oligosaccharides reduces the mortality associated with murine infection by adversely affecting the transmission of Y. pestis to lymph nodes. These results demonstrate that direct interaction of core oligosaccharides with Langerin facilitates the invasion of LCs by Y. pestis. Therefore, Langerin-mediated binding of Y. pestis to APCs may promote its dissemination and infection.

No MeSH data available.


Related in: MedlinePlus