Streptococcus agalactiae CAMP factor binds to GPI-anchored proteins

Lang, Shenhui; Xue, Junmin; Guo, Zhongwu; Palmer, Michaël

doi:10.1007/s00430-006-0021-2

Cited by 26 publications

(30 citation statements)

References 29 publications

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“…CAMP factors can bind to several proteins, including immunoglobulins, via their Fc-binding region [48], and GPI-anchored proteins, via their glycan moieties [49]. TLR2 recognition preferentially involves lipoproteins expressed at the bacterial surface, but several members of the no-lipoprotein pore-forming toxin family have been shown to interact with TLRs, consistent with broad specificity for TLR2-mediated recognition [50].…”

Section: Discussionmentioning

confidence: 99%

TLR-2 Recognizes Propionibacterium acnes CAMP Factor 1 from Highly Inflammatory Strains

et al. 2016

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BackgroundPropionibacterium acnes (P. acnes) is an anaerobic, Gram-positive bacteria encountered in inflammatory acne lesions, particularly in the pilosebaceous follicle. P. acnes triggers a strong immune response involving keratinocytes, sebocytes and monocytes, the target cells during acne development. Lipoteicoic acid and peptidoglycan induce the inflammatory reaction, but no P. acnes surface protein interacting with Toll-like receptors has been identified. P. acnes surface proteins have been extracted by lithium stripping and shown to induce CXCL8 production by keratinocytes.Methodology and principal findingsFar-western blotting identified two surface proteins, of 24.5- and 27.5-kDa in size, specifically recognized by TLR2. These proteins were characterized, by LC-MS/MS, as CAMP factor 1 devoid of its signal peptide sequence, as shown by N-terminal sequencing. Purified CAMP factor 1 induces CXCL8 production by activating the CXCL8 gene promoter, triggering the synthesis of CXCL8 mRNA. Antibodies against TLR2 significantly decreased the CXCL8 response. For the 27 P. acnes strains used in this study, CAMP1-TLR2 binding intensity was modulated and appeared to be strong in type IB and II strains, which produced large amounts of CXCL8, whereas most of the type IA1 and IA2 strains presented little or no CAMP1-TLR2 binding and low levels of CXCL8 production. The nucleotide sequence of CAMP factor displays a major polymorphism, defining two distinct genetic groups corresponding to CAMP factor 1 with 14 amino-acid changes from strains phylotyped II with moderate and high levels of CAMP1-TLR2 binding activity, and CAMP factor 1 containing 0, 1 or 2 amino-acid changes from strains phylotyped IA1, IA2, or IB presenting no, weak or moderate CAMP1-TLR2 binding.ConclusionsOur findings indicate that CAMP factor 1 may contribute to P. acnes virulence, by amplifying the inflammation reaction through direct interaction with TLR2.

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Section: Discussionmentioning

confidence: 99%

TLR-2 Recognizes Propionibacterium acnes CAMP Factor 1 from Highly Inflammatory Strains

et al. 2016

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“…In collaboration with Michael Palmer, we also evaluated the influence of synthetic GPI analogs on the cytotoxicity of CAMP factor [86]. It was shown that 139 , a GPI analog without the phospholipid but with a palmitoyl group and a dipeptide linked to the inositol 2- O -position and the phosphoethanolamine moiety at the glycan non-reducing end, respectively, had obvious and concentration-dependent inhibition on CAMP factor-mediated lysis of sheep erythrocytes (Figure 8).…”

Section: Biological Studies Using Synthetic Gpis and Gpi Derivativesmentioning

confidence: 99%

“…Both the binding assays [59] and the hemolysis inhibition study [86] have validated the strong and specific binding of CAMP factor to GPIs and GPI analogs. The observation that a GPI fragment 46 had essentially the same binding affinity as the intact GPI anchor 50 suggests that CAMP factor may interact mainly with the pseudodisaccharide and/or the phospholipid moieties of GPI anchors.…”

Section: Biological Studies Using Synthetic Gpis and Gpi Derivativesmentioning

confidence: 99%

Synthetic Studies of Glycosylphosphatidylinositol (GPI) Anchors and GPI-Anchored Peptides, Glycopeptides, and Proteins

Guo¹

2013

COS

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Glycosylphosphatidylinositol (GPI) anchorage of proteins and glycoproteins onto the cell surface is ubiquitous in eukaryotes, and GPI-anchored proteins and glycoproteins play an important role in many biological processes. To study GPI anchorage and explore the functions of GPIs and GPI-anchored proteins and glycoproteins, it is essential to have access to these molecules in homogeneous and structurally defined forms. This review is focused on the progress that our laboratory has made towards the chemical and chemoenzymatic synthesis of structurally defined GPI anchors and GPI-anchored peptides, glycopeptides, and proteins. Briefly, highly convergent strategies were developed for GPI synthesis and were employed to successfully synthesize a number of GPIs, including those carrying unsaturated lipids and other useful functionalities such as the azido and alkynyl groups. The latter enabled further site-specific modification of GPIs by click chemistry. GPI-linked peptides, glycopeptides, and proteins were prepared by regioselective chemical coupling of properly protected GPIs and peptides/glycopeptides or through site-specific ligation of synthetic GPIs and peptides/glycopeptides/proteins under the influence of sortase A. The investigation of interactions between GPI anchors and pore-forming bacterial toxins by means of synthetic GPI anchors and GPI analogs is also discussed.

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“…It is responsible for the so-called CAMP reaction, which consists in the co-operative hemolysis with Staphylococcus aureus sphingomyelinase [1]. The co-hemolytic activity involves the binding of CAMP factor to GPI-anchored proteins [10] and the formation of oligomeric pores [9]. In addition to this cytolytic activity, CAMP factor was reported to bind to immunoglobulins G and M in a manner similar to protein A of Staphylococcus aureus, and it was therefore given the alternative name 'protein B' [6].…”

Section: Introductionmentioning

confidence: 99%

Streptococcus agalactiae CAMP factor/protein B does not bind to human IgG

El‐Huneidi

Mui

Zhang

et al. 2006

Med Microbiol Immunol

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CAMP factor is an extracellular cytolytic protein produced by Streptococcus agalactiae. CAMP factor has been reported to bind the Fc fragments of immunoglobulin G (IgG) and has therefore also been called protein B, in analogy to protein A of Staphylococcus aureus. We attempted to characterize the interaction of protein B with IgG in more detail. In contrast to protein A, CAMP factor does not inhibit the activation of complement by hemolysin antibodies bound to sheep red cell surfaces. IgG also failed to inhibit the co-hemolytic activity of CAMP factor, which is in disagreement with previous findings. After co-incubation, CAMP factor and IgG were cleanly separated by gel filtration, indicating that no binding had occurred.

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Streptococcus agalactiae CAMP factor binds to GPI-anchored proteins

Cited by 26 publications

References 29 publications

TLR-2 Recognizes Propionibacterium acnes CAMP Factor 1 from Highly Inflammatory Strains

TLR-2 Recognizes Propionibacterium acnes CAMP Factor 1 from Highly Inflammatory Strains

Synthetic Studies of Glycosylphosphatidylinositol (GPI) Anchors and GPI-Anchored Peptides, Glycopeptides, and Proteins

Streptococcus agalactiae CAMP factor/protein B does not bind to human IgG

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