S-layer glycoprotein from Lactobacillus kefiri CIDCA 8348 enhances macrophages response to LPS in a Ca+2-dependent manner

Malamud, Mariano; Carasi, Paula; Freire, Teresa; Serradell, María de los Ángeles

doi:10.1016/j.bbrc.2017.11.127

Cited by 14 publications

(17 citation statements)

References 40 publications

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“…As surface exposed structures, the SLPs could be a key mediator between bacteria and host immune system contributing to the shaping of the immunological response to pathogenic, commensal and probiotic microorganisms. By using murine macrophages RAW 264.7 cells as model, we have demonstrated that despite the differences between glycosylation patterns of SLP-8321 and SLP-5818, both proteins are able to enhance LPS-induced cell activation ( Figure 7), similarly to previously demonstrated for SLP-8348 (22). These results suggest that O-glycans present in these three mentioned L. kefiri SLPs could be responsible, at least in part, of their immunostimulatory ability.…”

Section: Discussionsupporting

confidence: 75%

“…Regarding the genus Lactobacillus, there are some reports describing the involvement of the carbohydrate receptor DCspecific ICAM-3-grabbing nonintegrin (DC-SIGN) in the functional activity of the S-layer proteins from L. acidophilus NCFM (19), L. plantarum (20) and L. kefiri JCM 5818 (21). In this sense, we have recently demonstrated that the S-layer glycoprotein from L. kefiri CIDCA 8348 is able to enhance the LPS-induced response in murine macrophages in a carbohydrate-receptor mediated process (22). Moreover, this SLP improves the OVA-specific cell immune response by triggering maturation of antigen presenting cells through the recognition of glycan moieties by Mincle (23).…”

Section: Introductionmentioning

confidence: 90%

“…Regarding that we have previously demonstrated that SLP-8348 can enhance LPS-induced activation of antigen presenting cells (22,23), we decided to test the ability of SLP-8321 and SLP-5818 to activate murine macrophage, using RAW 264.7 cells as first model. As it was previously observed for SLP-8348 (22,23), the SLP-8321 and SLP-5818 were not able to induce activation of RAW 264.7 cells by themselves. However, respective significant increments in secreted IL-6 as well as in surface expression of CD40 and CD86 were observed for macrophages simultaneously exposed to E. coli LPS and L. kefiri S-layer glycoproteins in comparison to LPS-treated cells ( Figure 7A, B).…”

Section: Stimulation Of Murine Macrophages By L Kefiri Slpsmentioning

confidence: 99%

“…Extraction from bacterial cells at stationary phase was performed using 5M lithium chloride (LiCl) as described previously (22). The samples were centrifuged and the protein concentration in the supernatant was determined according to Bradford.…”

Section: S-layer Protein Extractionmentioning

confidence: 99%

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Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partners

Malamud

Cavallero

Casabuono

et al. 2020

Journal of Biological Chemistry

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S-layer (glyco)-proteins (SLPs) form a nanostructured envelope that covers the surface of different prokaryotes and show immunomodulatory activity. Previously, we have demonstrated that the S-layer glycoprotein from probiotic Lactobacillus kefiri CIDCA 8348 (SLP-8348) is recognized by Mincle (macrophage inducible C-type lectin receptor) and its adjuvanticity depends on the integrity of its glycans. However, the glycan's structure has not been described so far. Herein, we analyze the glycosylation pattern of three SLPs, SLP-8348, SLP-8321, and SLP-5818, and explore how these patterns impact their recognition by C-type lectin receptors (CLRs) and the immunomodulatory effect of the L. kefiri SLPs on antigen-presenting cells. HPAEC-PAD performed after β-elimination showed glucose as the major component in the O-glycans of the three SLPs, however, some differences in the length of hexose chains were observed. No N-glycosylation signals were detected in SLP-8348 and SLP-8321, but SLP-5818 was observed to have two sites carrying complex N-glycans based on a site-specific analysis and a glycomic workflow of the permethylated glycans. SLP-8348 was previously shown to enhance LPS-induced activation on both RAW264.7 macrophages and murine BMDCs; we now show SLP-8321 and SLP-5818 have a similar effect regardless of the differences in their glycosylation patterns. Studies performed with BMDCs from CLR-deficient mice revealed that the immunostimulatory activity of SLP-8321 depends on its recognition by Mincle, whereas SLP-5818’s effects are dependent on SignR3 (murine ortholog of human DC-SIGN). These findings encourage further investigation of both the potential application of these SLPs as new adjuvants and the protein glycosylation mechanisms in these bacteria.

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Section: Discussionsupporting

confidence: 75%

Section: Introductionmentioning

confidence: 90%

Section: Stimulation Of Murine Macrophages By L Kefiri Slpsmentioning

confidence: 99%

Section: S-layer Protein Extractionmentioning

confidence: 99%

See 2 more Smart Citations

Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partners

Malamud

Cavallero

Casabuono

et al. 2020

Journal of Biological Chemistry

Self Cite

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“…S-layer proteins isolated from Lactobacilli were shown to bind to host cell proteins and extracellular matrix (44, 126). The S-layer protein from L. kefiri CIDCA 8348 improved the response of macrophages to lipopolysaccharide (LPS) (125) and was able to enhance the ovalbumin-specific immune response by triggering maturation of antigen presenting cells through the recognition of glycan moieties in mice (127). Lactobacillus paracasei subp.…”

Section: S-layer Proteinsmentioning

confidence: 99%

Paraprobiotics and Postbiotics of Probiotic Lactobacilli, Their Positive Effects on the Host and Action Mechanisms: A Review

et al. 2020

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Lactobacilli comprise an important group of probiotics for both human and animals. The emerging concern regarding safety problems associated with live microbial cells is enhancing the interest in using cell components and metabolites derived from probiotic strains. Here, we define cell structural components and metabolites of probiotic bacteria as paraprobiotics and postbiotics, respectively. Paraprobiotics and postbiotics produced from Lactobacilli consist of a wide range of molecules including peptidoglycans, surface proteins, cell wall polysaccharides, secreted proteins, bacteriocins, and organic acids, which mediate positive effect on the host, such as immunomodulatory, anti-tumor, antimicrobial, and barrier-preservation effects. In this review, we systematically summarize the paraprobiotics and postbiotics derived from Lactobacilli and their beneficial functions. We also discuss the mechanisms underlying their beneficial effects on the host, and their interaction with the host cells. This review may boost our understanding on the benefits and molecular mechanisms associated with paraprobiotics and probiotics from Lactobacilli, which may promote their applications in humans and animals.

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Paraprobiotics: definition, manufacturing methods, and functionality

Lee

Kang

Paik

2023

Food Sci Biotechnol

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S-layer glycoprotein from Lactobacillus kefiri CIDCA 8348 enhances macrophages response to LPS in a Ca+2-dependent manner

Cited by 14 publications

References 40 publications

Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partners

Immunostimulation by Lactobacillus kefiri S-layer proteins with distinct glycosylation patterns requires different lectin partners

Paraprobiotics and Postbiotics of Probiotic Lactobacilli, Their Positive Effects on the Host and Action Mechanisms: A Review

Paraprobiotics: definition, manufacturing methods, and functionality

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