Lipoteichoic Acid Inhibits Interleukin-2 (IL-2) Function by Direct Binding to IL-2

Plitnick, Lisa M.; Jordan, Robert; Banas, Jeffrey A.; Jelley-Gibbs, Dawn M.; Walsh, Mary F.; Preissler, Mark T.; Gosselin, Edmund J.

doi:10.1128/cdli.8.5.972-979.2001

Cited by 14 publications

(10 citation statements)

References 38 publications

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“…Modulation of TT-induced IL-2 by S. mutans has been demonstrated previously (16), and lipoteichoic acid (LTA) from this and other gram-positive microorganisms was found to inhibit the biological functions of IL-2 through direct binding to IL-2 (17). Results of the present study suggested that GTFs of S. mutans might also play a significant role in the modulation of detectable levels of IL-2 induced by other antigens.…”

Section: Vol 9 2002 Induction Of Cytokines By Glucosyltransferases 895supporting

confidence: 73%

“…Interestingly, the production of IFN-␥, another cytokine associated with a Th1-type response, was also inhibited in the T cells from some but not all individuals. However, LTA stimulated the production of IFN-␥ in T cells in response to TT (17). Therefore, GTFs might play a role distinct from that of LTA in modulating induction or production of cytokines from T cells.…”

Section: Vol 9 2002 Induction Of Cytokines By Glucosyltransferases 895mentioning

confidence: 96%

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Induction of Cytokines by Glucosyltransferases ofStreptococcus mutans

Chia

Lien

Hsueh³

et al. 2002

Clin Vaccine Immunol

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Production of proinflammatory cytokines is implicated in the pathogenesis of viridans streptococcusinduced ␣-streptococcal shock syndrome and infective endocarditis. Streptococcus mutans, one of the opportunistic pathogens causing infective endocarditis, was reported previously to stimulate monocytes and epithelial and endothelial cells in vitro to produce various cytokines. We found that glucosyltransferases (GTFs) GtfC and GtfD of S. mutans stimulated predominantly the production of interleukin-6 (IL-6) from T cells cultured in vitro. The level of IL-6 but not of tumor necrosis factor alpha in blood was significantly elevated when rats were injected intravenously with S. mutans GS-5, whereas IL-6 was detected at a much lower level when rats were challenged with NHS1DD, an isogenic mutant defective in the expression of GTFs. The serum IL-6 level was elevated in patients with endocarditis caused by different species of viridans streptococci which express GTF homologues. Affinity column-purified GTFs reduced the levels of detectable IL-2 of T cells stimulated by another bacterial antigen, tetanus toxoid. These results suggested that GTFs might modulate the production of Th1-type cytokines and that GTFs of S. mutans play a significant role in stimulating the production of the proinflammatory cytokine IL-6 in vivo. Species of viridans streptococci, such as Streptococcus mutans, Streptococcus sanguis, orStreptococcus oralis, are common causes of infective endocarditis in humans (2, 13). In Taiwan, S. oralis and S. sanguis are most frequently isolated from blood cultures in endocarditis, but S. mutans, a primary etiological agent of human dental caries (14), is associated with the highest incidence of endocarditis in bacteremia-associated pyogenic infections (5). S. mutans and other oral streptococci may enter the bloodstream and cause transient bacteremia in humans following dental extractions, brushing of teeth, and chewing (9). Transient bacteremia facilitated S. mutans colonization of the valve tissues, particularly in those patients with preexisting valvular damage. The development of endocarditis depends on a balance between the abilities of the organism to adhere to vegetations and to resist the array of host responses.S. mutans was able to stimulate in vitro the proliferation of peripheral blood mononuclear cells (PBMC), including CD4 ϩ T cells, CD8 ϩ T cells, and natural killer (NK) cells, in an antigen-dependent manner (16). The stimulated PBMC secreted gamma interferon (IFN-␥), tumor necrosis factor ␤ (TNF-␤), and interleukin 10 (IL-10), etc., but the level of detectable IL-2 was relatively low compared to that of the others when PBMC were stimulated by soluble factors secreted from S. mutans (16). Antigen I/II of S. mutans, an adhesin for saliva-coated surfaces, interacted directly with human monocytes or epithelial or endothelial cells through lectin-like binding and stimulated the production of proinflammatory cytokines, such as IL-1, IL-6, 20,22). The induction of excess proinflammatory cytokines, espe...

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Section: Vol 9 2002 Induction Of Cytokines By Glucosyltransferases 895supporting

confidence: 73%

Section: Vol 9 2002 Induction Of Cytokines By Glucosyltransferases 895mentioning

confidence: 96%

Induction of Cytokines by Glucosyltransferases ofStreptococcus mutans

Chia

Lien

Hsueh³

et al. 2002

Clin Vaccine Immunol

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“…Finally, antirabbit-alkaline phosphatase (AP) or anti-mouse-AP was added for 1 h, respectively; the wells were washed again, and AP substrate was added. The anti-hFc␥RI-PspA fusion protein was purified using a nickel affinity column or protein L, also as previously described (51,68). Purified antihFc␥RI-PspA fusion protein was run on an 8% polyacrylamide SDS-PAGE gel (Pierce, Rockford, IL).…”

Section: Methodsmentioning

confidence: 99%

Mucosal Immunization with an Unadjuvanted Vaccine That Targets Streptococcus pneumoniae PspA to Human Fcγ Receptor Type I Protects against Pneumococcal Infection through Complement- and Lactoferrin-Mediated Bactericidal Activity

Bitsaktsis

Iglesias

et al. 2012

Infect Immun

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Targeting an antigen to Fc receptors (FcR) can enhance the immune response to the antigen in the absence of adjuvant. Furthermore, we recently demonstrated that intranasal immunization with an Fc␥R-targeted antigen enhances protection against a category A intracellular mucosal pathogen, Francisella tularensis. To determine if a similar strategy could be applied to the important pathogen Streptococcus pneumoniae, we used an improved mucosal FcR-targeting strategy that specifically targets human Fc␥R type I (hFc␥RI). A humanized single-chain antibody component in which the variable domain binds to hFc␥RI [antihFc␥RI (H22)] was linked in a fusion protein with the pneumococcal surface protein A (PspA). PspA is known to elicit protection against pneumococcal sepsis, carriage, and pneumonia in mouse models when administered with adjuvants. Anti-hFc␥RI-PspA or recombinant PspA (rPspA) alone was used to intranasally immunize wild-type (WT) and hFc␥RI transgenic (Tg) mice in the absence of adjuvant. The hFc␥RI Tg mice receiving anti-hFc␥RI-PspA exhibited elevated S. pneumoniae-specific IgA, IgG2c, and IgG1 antibodies in serum and bronchoalveolar lavage fluid. Neither immunogen was effective in protecting WT mice in the absence of adjuvant, but when PspA was targeted to hFc␥RI as the anti-hFc␥RI-PspA fusion, enhanced protection against lethal S. pneumoniae challenge was observed in the hFc␥RI Tg mice compared to mice given nontargeted rPspA alone. Immune sera from the anti-hFc␥RI-PspA-immunized Tg mice showed enhanced complement C3 deposition on bacterial surfaces, and protection was dependent upon an active complement system. Immune serum also showed an enhanced bactericidal activity directed against S. pneumoniae that appears to be lactoferrin mediated.

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“…A rapid increase in VEGF expression may result in an acute increase in interstitial tissue pressure in the noncompliant pulp space, leading to pulpal necrosis. LTA also exhibits anti-inflammatory effects including anti-phagocytosis and direct binding to interleukin-2 (IL-2) (72,73). LTA from hemolytic streptococci inhibits the uptake of streptococci by epithelial cells.…”

Section: Lipoteichoic Acidmentioning

confidence: 99%