Interaction of purified lipoteichoic acid with the classical complement pathway

Loos, Michael; Clas, F; Fischer, Werner

doi:10.1128/iai.53.3.595-599.1986

Cited by 54 publications

(20 citation statements)

References 40 publications

(53 reference statements)

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“…The resuits reported here showed that LTA from S. mutans caused a dose-dependent conversion of C3 when tested in solution (Figs. 1, 2), The finding complies with results from other studies, based on hemolytic assays (Fiedel & Jackson 1978, Wilkinson et al, 198i, Hummell et al 1985, Loos et al 1986). Degradation of C3 yields split products with important inflammatory potential.…”

Section: Discussionsupporting

confidence: 89%

“…First, CI can be activated by certain polyanions in a way simiiar to the effect of immune complexes (Loos & Bitter-Suermann 1976). Thus Loos et al (1986) showed that some forms of LTAs interacted directly with Clq, and triggered a significant consumption of classical pathway proteins. The degree of complement consumption was dependent upon the carbohydrate content of the hydrophihc backbone chain of the LTAs and on their miceliar organization, LTAs with negative charges masked by bulky carbohydrate groups were comparatively weak activators.…”

Section: Discussionmentioning

confidence: 99%

“…When pneumococcal LTA was bound to the surface of sheep erythrocytes (RBCs), it activated the alternative pathway, but was inactive when tested in solution (Hummell et aJ, 1985). Later, Loos et al (1986) showed that some forms of LTA bound directly to purified CL and thus activated the classical pathway in an antibody-independent manner.…”

mentioning

confidence: 99%

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Effects of a streptococcal lipoteichoic acid on complement activation in vitro

Monefeldt

Tollefsen

1993

J Clinic Periodontology

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This study describes activation of serum complement by lipoteichoic acid (LTA) from Streptococcus mutans OMZ 176, while in solution. Serum from 16 healthy students was taken. Test samples were incubated with increasing doses (1-5,000 micrograms/ml) of LTA or lipopolysaccharide (LPS) from Escherichia coli 0111:B4 for 1 h at 37 degrees C; then assayed for degradation of C3, C4 or factor B by crossed immunoelectrophoresis. Each preparation caused a significant (p < 0.05) dose-dependent conversion of C3. The response curves obtained were not statistically different. LPS was a stronger activator of the alternative pathway than LTA, as judged from analysis of C3 degradation in the presence of Mg2+/EGTA, and from their effects on factor B cleavage. LTA caused, however, pronounced alterations in the shape of C4 precipitation in the gels. Functional (hemolytic) assays showed that, when tested at 200 micrograms/ml, LTA and LPS triggered significant (p < 0.05) consumptions of both classical and alternative pathway proteins. LPS was a significantly (p < 0.05) stronger activator than LTA. Apparently, the C3 degradation found for this LTA involved the alternative pathway to a small extent; thus some other mechanism of fluid-phase C3 cleavage seemed also to be operative.

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Section: Discussionsupporting

confidence: 89%

Section: Discussionmentioning

confidence: 99%

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Effects of a streptococcal lipoteichoic acid on complement activation in vitro

Monefeldt

Tollefsen

1993

J Clinic Periodontology

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“…If the latter is true, it would be interesting to study the effect of InlB-LTA complexes on cells. LTA are known to be able to insert into eukaryotic membranes by their lipid moiety and to bind several components, such as the C1q, the type 1 scavenger receptor and fibronectin (Courtney et al, 1983;Loos et al, 1986;Dunne et al, 1994;Hauf et al, 1997). Therefore, how the loose attachment of InlB plays a role in the infectious process of L. monocytogenes remains a challenging issue.…”

Section: Discussionmentioning

confidence: 99%

Interaction between the protein InlB of Listeria monocytogenes and lipoteichoic acid: a novel mechanism of protein association at the surface of Gram‐positive bacteria

Jonquières

Bierne

Fiedler

et al. 1999

Molecular Microbiology

226

249

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SummaryInlB is a Listeria monocytogenes protein that is sufficient to promote entry in a variety of mammalian cells. The last 232-amino-acid domain (Csa) of InlB has been shown to mediate attachment on the listerial surface, although its sequence does not suggest any known mechanism of association to the bacterial surface. InlB is present both on the bacterial surface and in culture supernatants. As has been recently demonstrated, both forms of InlB, soluble and surfacebound, can trigger signalling in host cells. To elucidate the specific role of each of the two forms, it was important to understand how InlB associates with the bacterial surface. Using microscopy, we find evidence that InlB is partially buried in the cell wall layer, and using fractionation experiments we demonstrate that InlB associates with the bacterial cytoplasmic membrane. Moreover, using purified lipoteichoic acid (LTA) and the three polypeptides InlB, Csa, or InlB⌬Csa (InlB lacking the last 232 amino acids), we demonstrate that LTA is a ligand for the Csa domain of InlB. These results provide the first evidence of an interaction between lipoteichoic acids and a bacterial protein involved in adhesion and signalling, and highlight a new mechanism of protein association on the surface of Gram-positive bacteria.

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“…Alternatively, C1q can bind directly to the bacterial surface to activate the CP. C1q was found to bind to a variety of microbial structures including the lipid A region of LPS (Cooper & Morrison, 1978;Tan et al, 2011) and different outer membrane proteins on Gram-negative bacteria (Loos & Clas, 1987;Albert ı et al, 1993;Mintz et al, 1995;Merino et al, 1998), and LTA on Gram-positive bacteria (Loos et al, 1986). Moreover, C1q can bind to various carbohydrates (Pa€ ıdassi et al, 2008), which potentially mediates direct binding to bacteria.…”

Section: (A) (B)mentioning

confidence: 99%

Bacteria under stress by complement and coagulation

Berends¹,

Kuipers²,

Ravesloot³

et al. 2014

FEMS Microbiol Rev

103

108

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The complement and coagulation systems are two related protein cascades in plasma that serve important roles in host defense and hemostasis, respectively. Complement activation on bacteria supports cellular immune responses and leads to direct killing of bacteria via assembly of the Membrane Attack Complex (MAC). Recent studies have indicated that the coagulation system also contributes to mammalian innate defense since coagulation factors can entrap bacteria inside clots and generate small antibacterial peptides. In this review, we will provide detailed insights into the molecular interplay between these protein cascades and bacteria. We take a closer look at how these pathways are activated on bacterial surfaces and discuss the mechanisms by which they directly cause stress to bacterial cells. The poorly understood mechanism for bacterial killing by the MAC will be reevaluated in light of recent structural insights. Finally, we highlight the strategies used by pathogenic bacteria to modulate these protein networks. Overall, these insights will contribute to a better understanding of the host defense roles of complement and coagulation against bacteria.

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Interaction of purified lipoteichoic acid with the classical complement pathway

Cited by 54 publications

References 40 publications

Effects of a streptococcal lipoteichoic acid on complement activation in vitro

Effects of a streptococcal lipoteichoic acid on complement activation in vitro

Interaction between the protein InlB of Listeria monocytogenes and lipoteichoic acid: a novel mechanism of protein association at the surface of Gram‐positive bacteria

Bacteria under stress by complement and coagulation

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