A glycoproteomic approach reveals that the S-layer glycoprotein of Lactobacillus kefiri CIDCA 83111 is O- and N-glycosylated
In Gram-positive bacteria, such as lactic acid bacteria, general glycosylation systems have not been documented so far. The aim of this work was to characterize in detail the glycosylation of the S-layer protein of Lactobacillus kefiri CIDCA 83111. A reductive β-elimination treatment followed by ani...
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Elsevier B.V.
2017
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| LEADER | 13145caa a22013697a 4500 | ||
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| 001 | PAPER-14940 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518204533.0 | ||
| 008 | 190410s2017 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-85018179395 | |
| 024 | 7 | |2 cas |a asparagine, 70-47-3, 7006-34-0; galacturonic acid, 14982-50-4, 685-73-4; serine, 56-45-1, 6898-95-9; threonine, 36676-50-3, 72-19-5; Bacterial Proteins; Glycoproteins; Membrane Glycoproteins; Oligosaccharides; Polysaccharides; S-layer proteins | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 100 | 1 | |a Cavallero, G.J. | |
| 245 | 1 | 2 | |a A glycoproteomic approach reveals that the S-layer glycoprotein of Lactobacillus kefiri CIDCA 83111 is O- and N-glycosylated |
| 260 | |b Elsevier B.V. |c 2017 | ||
| 270 | 1 | 0 | |m Couto, A.S.; Universidad de Buenos Aires, Facultad de Ciencias Exactas y Naturales, Departamento de Química Orgánica - Consejo Nacional de Investigaciones Científicas y Técnicas, Centro de Investigación en Hidratos de Carbono (CIHIDECAR)Argentina; email: acouto@qo.fcen.uba.ar |
| 506 | |2 openaire |e Política editorial | ||
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| 504 | |a Gerbino, E., Carasi, P., Mobili, P., Serradell, M.A., Gómez-Zavaglia, A., Role of S-layer proteins in bacteria (2015) World J. Microbiol. Biotechnol., 31, pp. 1877-1887 | ||
| 504 | |a Möschl, A., Schäffer, C., Sleytr, U.B., Messner, P., Christian, R., Schulz, G., Characterization of the S-layer glycoproteins of two Lactobacilli (1993) Advances in Bacterial Paracrystalline Surface Layers, 252, pp. 281-284. , T.J. Beveridge S.F. Koval Plenum Press New York | ||
| 504 | |a Anzengruber, J., Pabst, M., Neumann, L., Sekot, G., Heinl, S., Grabherr, R., Altmann, F., Schäffer, C., Protein O-glucosylation in Lactobacillus buchneri (2014) Glycoconj. J., 31 (2), pp. 117-131 | ||
| 504 | |a Mozes, N., Lortal, S., X-ray photoelectron spectroscopy and biochemical analysis of the surface of Lactobacillus helveticus ATCC 12046 (1995) Microbiology, 141, pp. 11-19 | ||
| 504 | |a Konstantinov, S.R., Smidt, H., de Vos, W.M., Bruijns, S.C.M., Singh, S.K., Valence, F., Molle, D., van Kooyk, Y., S layer protein A of Lactobacillus acidophilus NCFM regulates immature dendritic cell and T cell functions (2008) Proc. Natl. Acad. Sci. U. S. A., 105, pp. 19474-19479 | ||
| 504 | |a Mobili, P., Serradell, M.A., Trejo, S., Avilés-Puigvert, X., Abraham, A.G., De Antoni, G.L., Heterogeneity of S-layer proteins from aggregating and non-aggregating Lactobacillus kefir strains (2009) Antonie Van Leeuwenhoek, 95, pp. 363-372 | ||
| 504 | |a Lebeer, S., Verhoeven, T.L.A., Francius, G., Schoofs, G., Lambrichts, I., Dufrene, Y., Vanderleyden, J., De Keersmaecker, S.C.J., Identification of a gene cluster for the biosynthesis of a long, galactose-rich exopolysaccharide in Lactobacillus rhamnosus GG and functional analysis of the priming glycosyltransferase (2009) Appl. Environ. Microbiol., 75, pp. 3554-3563 | ||
| 504 | |a Denou, E., Pridmore, R.D., Berger, B., Panoff, J.M., Arigoni, F., Brussow, H., Identification of genes associated with the long-gut-persistence phenotype of the probiotic Lactobacillus johnsonii strain NCC533 using a combination of genomics and transcriptome analysis (2008) J. Bacteriol., 190, pp. 3161-3168 | ||
| 504 | |a Marco, M.L., de Vries, M.C., Wels, M., Molenaar, D., Mangell, P., Ahrne, S., de Vos, W.M., Kleerebezem, M., Convergence in probiotic Lactobacillus gut-adaptive responses in humans and mice (2010) ISME J., 4, pp. 1481-1484 | ||
| 504 | |a Garrote, G.L., Delfederico, L., Bibiloni, R., Abraham, A.G., Pérez, P.F., Semorile, L., De Antoni GL Lactobacilli isolated from kefir grains: evidence of the presence of S-layer proteins (2004) J. Dairy Res., 71, pp. 222-230 | ||
| 504 | |a Golowczyc, M., Mobili, P., Garrote, G.L., Serradell, M.A., Abraham, A.G., De Antoni, G.L., Interaction between Lactobacillus kefir and Saccharomyces lipolytica isolated from kefir grains: evidence for lectin-like activity of bacterial surface proteins (2009) J. Dairy Res., 76, pp. 111-116 | ||
| 504 | |a Golowczyc, M., Mobili, P., Garrote, G.L., Abraham, A.G., De Antoni, G.L., Protective action of Lactobacillus kefir carrying S-layer protein against Salmonella enterica serovar Enteritidis (2007) Int. J. Food Microbiol., 118, pp. 264-273 | ||
| 504 | |a Carasi, P., Trejo, F.M., Pérez, P.F., De Antoni, G.L., Serradell, M.A., Surface proteins from Lactobacillus kefiri antagonizes in vitro cytotoxic effect of Clostridium difficile toxins (2012) Anaerobe, 18, pp. 135-142 | ||
| 504 | |a Gerbino, E., Carasi, P., Araujo-Andrade, C., Tymczyszyn, E.E., Gómez-Zavaglia, A., Role of S-layer proteins in the biosorption capacity of lead by Lactobacillus kefir (2015) World J. Microbiol. Biotechnol., 31, pp. 583-592 | ||
| 504 | |a Malamud, M., Carasi, P., Bronsoms, S., Trejo, S.A., Serradell, M.A., Lactobacillus kefiri shows inter-strain variations in the amino acid sequence of the S-layer proteins (2016) Antonie Van Leeuwenhoek, , (accepted manuscript) | ||
| 504 | |a Garrote, G.L., Abraham, A.G., De Antoni, G.L., Chemical and microbiological characterization of kefir grains (2001) J. Dairy Res., 68, pp. 639-652 | ||
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| 504 | |a Francius, G., Lebeer, S., Alsteens, D., Wildling, L., Gruber, H.J., Hols, P., De Keersmaecker, S., Dufrêne, Y.F., Detection, localization, and conformational analysis of single polysaccharide molecules on live bacteria (2008) ACS Nano, 2 (9), pp. 1921-1929 | ||
| 504 | |a Sengupta, R., Altermann, E., Anderson, R.C., McNabb, W.C., Moughan, P.J., Roy, N.C., The role of cell surface architecture of lactobacilli in host-microbe interactions in the gastrointestinal tract (2013) Mediat. Inflamm., 2013, p. 237921 | ||
| 504 | |a Mengele, R., Sumper, M., Drastic differences in glycosylation of related S-layer glycoproteins from moderate and extreme halophiles (1992) J. Biol. Chem., 267, pp. 8182-8185 | ||
| 504 | |a Prado Acosta, M., Ruzal, S.M., Cordo, S.M., S-layer proteins from Lactobacillus sp. inhibit bacterial infection by blockage of DC-SIGN cell receptor (2016) Int. J. Biol. Macromol., 92, pp. 998-1005 | ||
| 520 | 3 | |a In Gram-positive bacteria, such as lactic acid bacteria, general glycosylation systems have not been documented so far. The aim of this work was to characterize in detail the glycosylation of the S-layer protein of Lactobacillus kefiri CIDCA 83111. A reductive β-elimination treatment followed by anion exchange high performance liquid chromatography analysis was useful to characterize the O-glycosidic structures. MALDI-TOF mass spectrometry analysis confirmed the presence of oligosaccharides bearing from 5 to 8 glucose units carrying galacturonic acid. Further nanoHPLC-ESI analysis of the glycopeptides showed two O-glycosylated peptides: the peptide sequence SSASSASSA already identified as a signature glycosylation motif in L. buchneri, substituted on average with eight glucose residues and decorated with galacturonic acid and another O-glycosylated site on peptide 471–476, with a Glc5–8GalA2 structure. As ten characteristic sequons (Asn-X-Ser/Thr) are present in the S-layer amino acid sequence, we performed a PNGase F digestion to release N-linked oligosaccharides. Anion exchange chromatography analysis showed mainly short N-linked chains. NanoHPLC-ESI in the positive and negative ion modes were useful to determine two different peptides substituted with short N-glycan structures. To our knowledge, this is the first description of the structure of N-glycans in S-layer glycoproteins from Lactobacillus species. Significance A detailed characterization of protein glycosylation is essential to establish the basis for understanding and investigating its biological role. It is known that S-layer proteins from kefir-isolated L. kefiri strains are involved in the interaction of bacterial cells with yeasts present in kefir grains and are also capable to antagonize the adverse effects of different enteric pathogens. Therefore, characterization of type and site of glycosidic chains in this protein may help to understand these important properties. Furthermore, this is the first description of N-glycosidic chains in S-layer glycoprotein from Lactobacillus spp. © 2017 Elsevier B.V. |l eng | |
| 536 | |a Detalles de la financiación: PICT 2012-0910, PICT-0736 | ||
| 536 | |a Detalles de la financiación: Consejo Nacional de Investigaciones Científicas y Técnicas, PIP-11220110100660 | ||
| 536 | |a Detalles de la financiación: Universidad de Buenos Aires, PME 2012, 20020130100476BA, PME 125 | ||
| 536 | |a Detalles de la financiación: This work was supported by the Consejo Nacional de Investigaciones Cient?ficas y T?cnicas Grant PIP-11220110100660, Agencia Nacional de Promoci?n Cient?fica y Tecnol?gica (ANPCyT) Grants PICT-0736 and PICT 2012-0910, and Universidad de Buenos Aires Grant 20020130100476BA. The Ultraflex II (Bruker) TOF/TOF mass spectrometer was supported by ANPCyT Grant PME 125 and the ESI-Orbitrap by ANPCyT Grant PME 2012. Gustavo J. Cavallero and Mariano Malamud are fellows from ANPCyT and CONICET respectively. Alicia S. Couto and Mar?a de los ?ngeles Serradell are members of Carrera de Investigador Cient?fico y Tecnol?gico of CONICET. | ||
| 593 | |a Universidad de Buenos Aires, Facultad de Ciencias Exactas y Naturales, Departamento de Química Orgánica - Consejo Nacional de Investigaciones Científicas y Técnicas, Centro de Investigación en Hidratos de Carbono (CIHIDECAR), Buenos Aires Argentina, Intendente Güiraldes 2160, Ciudad Universitaria, Buenos Aires, C1428GA, Argentina | ||
| 593 | |a Cátedra de Microbiología, Departamento de Ciencias Biológicas, Facultad de Ciencias Exactas, Universidad Nacional de La Plata (UNLP), 47 y 115, La Plata, 1900, Argentina | ||
| 690 | 1 | 0 | |a GLYCOPROTEOMICS |
| 690 | 1 | 0 | |a L. KEFIRI |
| 690 | 1 | 0 | |a MASS SPECTROMETRY |
| 690 | 1 | 0 | |a N-GLYCOSYLATION |
| 690 | 1 | 0 | |a O-GLYCOSYLATION |
| 690 | 1 | 0 | |a S-LAYER GLYCOPROTEIN |
| 690 | 1 | 0 | |a ASPARAGINE |
| 690 | 1 | 0 | |a BACTERIAL PROTEIN |
| 690 | 1 | 0 | |a GALACTURONIC ACID |
| 690 | 1 | 0 | |a GLYCOPEPTIDE |
| 690 | 1 | 0 | |a GLYCOPROTEIN |
| 690 | 1 | 0 | |a OLIGOSACCHARIDE |
| 690 | 1 | 0 | |a S LAYER GLYCOPROTEIN |
| 690 | 1 | 0 | |a SERINE |
| 690 | 1 | 0 | |a THREONINE |
| 690 | 1 | 0 | |a UNCLASSIFIED DRUG |
| 690 | 1 | 0 | |a BACTERIAL PROTEIN |
| 690 | 1 | 0 | |a GLYCOPROTEIN |
| 690 | 1 | 0 | |a MEMBRANE PROTEIN |
| 690 | 1 | 0 | |a OLIGOSACCHARIDE |
| 690 | 1 | 0 | |a POLYSACCHARIDE |
| 690 | 1 | 0 | |a S-LAYER PROTEINS |
| 690 | 1 | 0 | |a AMINO ACID SEQUENCE |
| 690 | 1 | 0 | |a ANION EXCHANGE CHROMATOGRAPHY |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a BACTERIAL STRAIN |
| 690 | 1 | 0 | |a CARBOHYDRATE ANALYSIS |
| 690 | 1 | 0 | |a CONSENSUS SEQUENCE |
| 690 | 1 | 0 | |a HIGH PERFORMANCE LIQUID CHROMATOGRAPHY |
| 690 | 1 | 0 | |a LACTOBACILLUS |
| 690 | 1 | 0 | |a LACTOBACILLUS BUCHNERI |
| 690 | 1 | 0 | |a LACTOBACILLUS KEFIRI |
| 690 | 1 | 0 | |a MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY |
| 690 | 1 | 0 | |a NEGATIVE ION ELECTROSPRAY |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a POSITIVE ION ELECTROSPRAY |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a PROTEIN ANALYSIS |
| 690 | 1 | 0 | |a PROTEIN GLYCOSYLATION |
| 690 | 1 | 0 | |a PROTEIN METABOLISM |
| 690 | 1 | 0 | |a PROTEIN STRUCTURE |
| 690 | 1 | 0 | |a PROTEOMICS |
| 690 | 1 | 0 | |a RETENTION TIME |
| 690 | 1 | 0 | |a CHEMISTRY |
| 690 | 1 | 0 | |a GLYCOSYLATION |
| 690 | 1 | 0 | |a LACTOBACILLUS |
| 690 | 1 | 0 | |a PROCEDURES |
| 690 | 1 | 0 | |a PROTEIN MOTIF |
| 690 | 1 | 0 | |a PROTEOMICS |
| 690 | 1 | 0 | |a AMINO ACID MOTIFS |
| 690 | 1 | 0 | |a BACTERIAL PROTEINS |
| 690 | 1 | 0 | |a GLYCOPROTEINS |
| 690 | 1 | 0 | |a GLYCOSYLATION |
| 690 | 1 | 0 | |a LACTOBACILLUS |
| 690 | 1 | 0 | |a MEMBRANE GLYCOPROTEINS |
| 690 | 1 | 0 | |a OLIGOSACCHARIDES |
| 690 | 1 | 0 | |a POLYSACCHARIDES |
| 690 | 1 | 0 | |a PROTEOMICS |
| 700 | 1 | |a Malamud, M. | |
| 700 | 1 | |a Casabuono, A.C. | |
| 700 | 1 | |a Serradell, M.D.L.Á. | |
| 700 | 1 | |a Couto, A.S. | |
| 773 | 0 | |d Elsevier B.V., 2017 |g v. 162 |h pp. 20-29 |p J. Proteomics |x 18743919 |t Journal of Proteomics | |
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