<i>Helicobacter pylori</i>Modulates the T Helper Cell 1/T Helper Cell 2 Balance through Phase-variable Interaction between Lipopolysaccharide and DC-SIGN

Bergman, Mathijs P.; Engering, Anneke; Smits, Hermelijn H.; Vliet, Sandra J. van; Bodegraven, Ad A. van; Wirth, Henry; Kapsenberg, Martien L.; Vandenbroucke-Grauls, Christina M. J. E.; Kooyk, Yvette van; Appelmelk, Ben J.

doi:10.1084/jem.20041061

Cited by 291 publications

(270 citation statements)

References 57 publications

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“…Varying the overall frequency of Lewis antigen expressors within a H. pylori population would be one mechanism whereby H. pylori modulates the inf lammatory response within the stomach (25,26). We envision that, in a persistent infection of a human stomach, a number of variants of a strain exist, and each isolate is more or less unique with respect to surface molecules, such as LPS.…”

Section: Discussionmentioning

confidence: 99%

An enzymatic ruler modulates Lewis antigen glycosylation of Helicobacter pylori LPS during persistent infection

Nilsson

Skoglund

Moran

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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Section: Discussionmentioning

confidence: 99%

An enzymatic ruler modulates Lewis antigen glycosylation of Helicobacter pylori LPS during persistent infection

Nilsson

Skoglund

Moran

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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“…Signal transduction upon ligand binding to DC-SIGN has not yet been proven, although the presence of an intracellular immunoreceptor tyrosine-based activation motif (ITAM) similar to dectin-1 suggests that DC-SIGN could be a signaling receptor [30]. Additionally, interactions of DC-SIGN with certain pathogens may have direct consequences for Th1/Th2 polarization [31]. Interestingly, blocking of the interaction between DC and T cells with an anti-DC-SIGN antibody influences allostimulatory properties in T cells [1].…”

Section: Blocking the Interaction Of L1-vlp With Dc-sign Inhibits Vlpmentioning

confidence: 99%

Role of DC‐SIGN in the activation of dendritic cells by HPV‐16 L1 virus‐like particle vaccine

et al. 2006

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Dendritic cell-specific intercellular adhesion molecule-grabbing non-integrin (DC-SIGN), a specific C-type lectin expressed on DC, binds and transmits different pathogens to susceptible cells. In the present study, we examined the role of DC-SIGN in the capture of human papillomavirus (HPV) pseudovirions and activation of DC. We demonstrate that HPV virus-like particles (VLP) bind to DC-SIGN expressed on transfected Raji cells and that antibodies against DC-SIGN block this interaction. DC take up VLP, which activate expression of costimulatory markers and cytokines/ chemokines. Although our results indicate that DC-SIGN is not the major receptor for VLP in DC, this interaction contributes to the activation of DC surface antigens (HLA class I) and of various cytokines/chemokines, particularly TNF-a, IL-6, and RANTES. Induction of these markers in DC by VLP was significantly abrogated when binding to DC-SIGN was blocked by anti-DC-SIGN antibodies. These results suggest that DC-SIGN has a functional role in DC activation induced by HPV-16 L1-VLP, and thus highlight new aspects of DC interactions with HPV VLP. IntroductionThe C-type lectin dendritic cell-specific intercellular adhesion molecule-grabbing non-integrin (DC-SIGN; CD209) is a pathogen recognition receptor that interacts with mannose residues of glycoproteins in a calciumdependent manner via its C-terminal carbohydrate recognition domain [1,2]. DC-SIGN acts both as an adhesion molecule and pathogen recognition receptor, facilitating DC binding and internalization of several viruses, including HIV-1 [3].In addition to HIV, DC-SIGN was recently shown to bind a variety of microorganisms such as CMV [4], Ebola virus [5], Dengue virus [6], hepatitis C virus [7,8], simian immunodeficiency virus [9], Leishmania [10], Candida albicans [11], Mycobacterium [12][13][14] and Schistosoma [15]. Some pathogens subvert DC functions to escape immune surveillance [16]. DC-SIGN is abundantly expressed primarily on DC, including those derived from monocytes and those located beneath the genital surface [3].Human papillomavirus (HPV) virus-like particles (VLP) are a promising vaccine candidate for HPV and cervical cancer [17][18][19][20]. Recent clinical trials have shown that VLP afford excellent protection against persistent infection [20,21]. Because of the lack of a suitable cell culture system for in vitro propagation of HPV and the unavailability of virions, HPV VLP have been used as soluble surrogates for native virus particles. The routes of HPV-16 L1-VLP entry in DC and the nature of cellular receptors involved in capture have been studied but remain to be fully characterized. HPV VLP Here, we report that HPV-16 L1-VLP particles bind to DC-SIGN in transfected cell lines, and to a lesser extent in DC, and that this interaction participates in L1-VLPinduced activation of DC. Thus, DC-SIGN is likely involved in DC activation by HPV VLP. Results and discussion HPV L1-VLP bind to DC-SIGN in DC-SIGN-transfected cell linesTo study interactions between L1-VLP and DC-SIGN, we...

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“…Bergman et al 48 demonstrated that Le-positive H. pylori strains were able to interact with the C-type lectin DC-SIGN on the surface of gastric dendritic cells. This interaction blocks maturation of T-helper 1 cells and leads to general immune suppression and reduced production of pro-inflammatory cytokines.…”

Section: Peptidoglycanmentioning

confidence: 99%

“…Contrarily, Le-negative strains do not show specific binding to dendritic cells through DC-SIGN, promoting maturation of T-helper 1 cells and thereby inducing a stronger immune response. 48 The marked diversity of Lewis antigen expression makes it difficult to define their role in infection and disease progression. However, evidence abounds to suggest that helical shape of H. pylori.…”

Section: Peptidoglycanmentioning

confidence: 99%

“…48 Hug et al 75 described an all-enzymatic system that generates a tetrasaccharide chain composed of galactose and GlcNAc, N-links it to an acceptor protein in vivo, and then decorates the conjugated glycan with a terminal Le x fucose residue in vitro. To achieve this, E. coli is functionally reconstituted with enzymes from Hemophilus influenza, C. jejuni, and H. pylori, resulting in a cell that produces a glycosylated protein none of the four contributing bacterial species can create on their own.…”

Section: Glycoengineeringmentioning

confidence: 99%

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Colonize, evade, flourish

Rubin

Trent

2013

Gut Microbes

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Helicobacter pyloriModulates the T Helper Cell 1/T Helper Cell 2 Balance through Phase-variable Interaction between Lipopolysaccharide and DC-SIGN

Cited by 291 publications

References 57 publications

An enzymatic ruler modulates Lewis antigen glycosylation of Helicobacter pylori LPS during persistent infection

An enzymatic ruler modulates Lewis antigen glycosylation of Helicobacter pylori LPS during persistent infection

Role of DC‐SIGN in the activation of dendritic cells by HPV‐16 L1 virus‐like particle vaccine

Colonize, evade, flourish

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