Up-regulation of ICAM-1, CD11a/CD18 and CD11c/CD18 on human THP-1 monocytes stimulated by<i>Streptococcus suis</i>serotype 2

Al-Numani, Dina; Segura, Mariela; Doré, Monique; Gottschalk, Marcelo

doi:10.1046/j.1365-2249.2003.02189.x

Cited by 46 publications

(38 citation statements)

References 52 publications

(70 reference statements)

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“…Leukocyte-leukocyte interactions would likely be the major benefit of increased ICAM-1 expression on a cell of the monocyte/macrophage lineage. Streptococcus suis, a major pathogen of swine and a zoonotic agent for humans, was shown to up-regulate ICAM-1 along with CD11a/CD18 and CD11c/CD18 in the THP-1 cell line (2). It has been reported that Mycobacterium tuberculosis also enhances expression of ICAM-1 on monocytic cells and that this increased expression may enhance monocyte recruitment and enhance antigen presentation of M. tuberculosis (16) since ICAM-1 is an integral component of the immunological synapse between a T lymphocyte and antigen-presenting cell, resulting in T-cell receptor/major histocompatibility complexpeptide interaction (11).…”

Section: Discussionmentioning

confidence: 99%

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THP-1 Monocytes Up-Regulate Intercellular Adhesion Molecule 1 in Response to Pneumolysin fromStreptococcus pneumoniae

Thornton¹,

McDaniel

2005

Infect Immun

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Pneumolysin (PLY) is a major virulence factor of Streptococcus pneumoniae that elicits a variety of proinflammatory responses from cells of the host immune system. Intercellular adhesion molecule 1 (ICAM-1) is a cell adhesion molecule involved in leukocyte trafficking toward inflammatory stimuli in extravascular sites. In this study, we evaluated the effect of PLY on expression of ICAM-1 in THP-1 monocytic cells exposed to S. pneumoniae. Exposure of cells to PLY-expressing S. pneumoniae strain WU2 for 6 h led to significantly higher levels of ICAM-1 message than those in cells exposed to either medium alone or ⌬PLY1, a PLY-negative isogenic mutant of WU2. Cells exposed to purified recombinant PLY also showed a dose-dependent increase in ICAM-1 mRNA compared to cells exposed to medium alone. Exposure to recombinant PLY containing a single amino acid substitution (Trp4333Phe) that decreases cytolytic activity did not increase ICAM-1 mRNA to levels seen with wild-type PLY. In addition, THP-1 cells exposed to wild-type strain WU2 or D39 had increased ICAM-1 on their surface compared to cells exposed to medium alone or their PLY-negative isogenic mutants ⌬PLY1 and ⌬PLY2, respectively. These data indicate that PLY induces transcription and production of a cell adhesion molecule involved in the inflammatory response that may play a role in pneumococcal infection.

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Section: Discussionmentioning

confidence: 99%

“…Quantification of ICAM-1 mRNA levels was achieved by real-time PCR analysis using an iCycler thermocycler (Bio-Rad Laboratories, Hercules, CA 2 , and reaction buffers. The optimized reaction mix included 0.5 M forward primer, 0.5 M reverse primer, SYBR Green Supermix, and PCR-grade H 2 O to adjust the final reaction volume.…”

Section: Methodsmentioning

confidence: 99%

THP-1 Monocytes Up-Regulate Intercellular Adhesion Molecule 1 in Response to Pneumolysin fromStreptococcus pneumoniae

Thornton¹,

McDaniel

2005

Infect Immun

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“…Also, the importance of the adhesion molecule ICAM1, a high-affinity counterreceptor for LFA1, was demonstrated. 38,39 Activation of HECs with LPS induces the expression of adhesion molecules, such as VCAM1, ICAM1, and E-selectin. 40,41 Therefore, in the present study, we questioned the effect of free or Lipo/GOT on LPS-stimulated monocyte adhesion to activated endothelia.…”

Section: Discussionmentioning

confidence: 99%

Lipopolysaccharide-induced inflammation in monocytes/macrophages is blocked by liposomal delivery of G<sub>i</sub>-protein inhibitor

Pirvulescu¹,

Rebleanu²,

Constantinescu³

et al. 2017

IJN

108

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Background Lipopolysaccharide (LPS) is widely recognized as a potent activator of monocytes/macrophages, and its effects include an altered production of key mediators, such as inflammatory cytokines and chemokines. The involvement of G i protein in mediating LPS effects has been demonstrated in murine macrophages and various cell types of human origin. Purpose The aim of the present work was to evaluate the potential of a G i -protein inhibitor encapsulated in liposomes in reducing the inflammatory effects induced by LPS in monocytes/macrophages. Materials and methods Guanosine 5′- O -(2-thiodiphosphate) (GOT), a guanosine diphosphate analog that completely inhibits G-protein activation by guanosine triphosphate and its analogs, was encapsulated into liposomes and tested for anti-inflammatory effects in LPS-activated THP1 monocytes or THP1-derived macrophages. The viability of monocytes/macrophages after incubation with different concentrations of free GOT or liposome-encapsulated GOT was assessed by MTT assay. MAPK activation and production of IL1β, TNFα, IL6, and MCP1 were assessed in LPS-activated monocytes/macrophages in the presence or absence of free or encapsulated GOT. In addition, the effect of free or liposome-encapsulated GOT on LPS-stimulated monocyte adhesion to activated endothelium and on monocyte chemotaxis was evaluated. Results We report here that GOT-loaded liposomes inhibited activation of MAPK and blocked the production of the cytokines IL1β, TNFα, IL6, and MCP1 induced by LPS in monocytes and macrophages. Moreover, GOT encapsulated in liposomes reduced monocyte adhesion and chemotaxis. All demonstrated events were in contrast with free GOT, which showed reduced or no effect on monocyte/macrophage activation with LPS. Conclusion This study demonstrates the potential of liposomal GOT in blocking LPS proinflammatory effects in monocytes/macrophages.

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“…Highly virulent strain 1669 of S. suis serotype 2 (Berthelot-Herault et al, 2005) was kindly provided by Dr M. Kobisch (AFSSA, Ploufragan, France). S. suis strains were grown in Todd-Hewitt broth (THB) (BD) as described previously (Al-Numani et al, 2003). Lateexponential-phase bacteria were washed in PBS, pH 7.3.…”

Section: Methodsmentioning

confidence: 99%

Isolation and characterization of α-enolase, a novel fibronectin-binding protein from Streptococcus suis

et al. 2008

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Streptococcus suis is an important swine pathogen that causes meningitis, endocarditis, arthritis and septicaemia. As a zoonotic agent, S. suis also causes similar diseases in humans. Binding of pathogenic bacteria to extracellular matrix components enhances their adhesion to and invasion of host cells. In the present study we isolated and identified a novel fibronectin-binding protein from S. suis. The native protein (designated SsEno) possessed not only high homology with other bacterial enolases but also enolase activity. We cloned, expressed and purified SsEno and showed that it is ubiquitously expressed by all S. suis serotypes and we identified its surface localization using immunoelectron microscopy. ELISA demonstrated that SsEno binds specifically to fibronectin and plasminogen in a lysine-dependent manner. Additional surface plasmon resonance assays demonstrated that SsEno binds to fibronectin or plasminogen with low nanomolar affinity. Inhibition experiments with anti-SsEno antibodies also showed that bacterial SsEno is important for the adhesion to and invasion of brain microvascular endothelial cells by S. suis. Overall, the present work is the first study, to our knowledge, to demonstrate a fibronectinbinding activity of a bacterial enolase, and shows that, similar to other bacterial fibronectin-binding proteins, SsEno may contribute to the virulence of S. suis. INTRODUCTIONStreptococcus suis is a major swine pathogen that causes septicaemia, meningitis, endocarditis and arthritis (Higgins & Gottschalk, 2005). Of the 35 known serotypes, serotype 2 is the most frequently isolated and associated with disease (Higgins & Gottschalk, 2005). It has been proposed that two serotypes (serotypes 32 and 34) be excluded from S. suis and redesignated Streptococcus orisratti (Hill et al., 2005). S. suis, especially serotype 2, has also been described as an important zoonotic agent that affects people in close contact with infected pigs or pork-derived products (Lun et al., 2007). Indeed, an important number of cases of human disease with a high rate of mortality in China were linked directly to a concurrent outbreak of S. suis infection in pigs (Ye et al., 2006).Little is known about S. suis virulence factors. The capsule polysaccharide (CPS) is a critical virulence factor, given that unencapsulated isogenic mutants are completely avirulent and rapidly cleared from the circulation in pig and mouse infection models (Charland et al., 2000;Smith et al., 1999). However, non-virulent strains are also encapsulated, indicating that the virulence of this pathogen is a multifactorial process . Other potential virulence factors have also been described in S. suis, including a haemolysin (suilysin), a 136 kDa muramidase-released protein (MRP), a 110 kDa extracellular factor (EF) protein, a hyaluronidase, a superoxide dismutase, various proteases, a serum opacity factor and different adhesins (Baums et al., 2006;.The pathogenesis of S. suis infection is not fully understood and likely involves many steps . Binding between b...

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Up-regulation of ICAM-1, CD11a/CD18 and CD11c/CD18 on human THP-1 monocytes stimulated byStreptococcus suisserotype 2

Cited by 46 publications

References 52 publications

THP-1 Monocytes Up-Regulate Intercellular Adhesion Molecule 1 in Response to Pneumolysin fromStreptococcus pneumoniae

THP-1 Monocytes Up-Regulate Intercellular Adhesion Molecule 1 in Response to Pneumolysin fromStreptococcus pneumoniae

Lipopolysaccharide-induced inflammation in monocytes/macrophages is blocked by liposomal delivery of G<sub>i</sub>-protein inhibitor

Isolation and characterization of α-enolase, a novel fibronectin-binding protein from Streptococcus suis

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