Proteomic analysis of cell surface-associated proteins from probiotic<i>Lactobacillus plantarum</i>

Beck, Hans Christian; Madsen, Søren; Glenting, Jacob; Petersen, Jørn Henrik; Israelsen, Hans; Nørrelykke, M.R.; Antonsson, Martin; Hansen, Anders Kragh

doi:10.1111/j.1574-6968.2009.01662.x

Cited by 57 publications

(38 citation statements)

References 43 publications

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“…The exoproteome levels of some carbohydrate metabolism and glycolysis (CMG) proteins was affected by cultivation with PlnA and, especially, with L. sanfranciscensis DPPMA174. Some of these proteins were also identified in the exoproteome of other strains of L. plantarum (7,62,63). A number of CMG proteins express moonlighting activities (64).…”

Section: Figmentioning

confidence: 93%

Effects of the Peptide Pheromone Plantaricin A and Cocultivation with Lactobacillus sanfranciscensis DPPMA174 on the Exoproteome and the Adhesion Capacity of Lactobacillus plantarum DC400

Calasso

Cagno

Angelis

et al. 2013

Appl Environ Microbiol

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This study aimed at investigating the extracellular and cell wall-associated proteins (exoproteome) of Lactobacillus plantarum DC400 when cultivated on modified chemically defined medium (CDM) supplemented with the chemically synthesized pheromone plantaricin A (PlnA) or cocultured with L. plantarum DPPMA20 or Lactobacillus sanfranciscensis DPPMA174. Compared to monoculture, two-dimensional gel electrophoresis (2-DE) analysis showed that the exoproteome of L. plantarum DC400 was affected by PlnA and cocultivation with strains DPPMA20 and, especially, DPPMA174. The highest similarity of the 2-DE maps was found between DC400 cells cultivated in monoculture and in coculture with strain DPPMA20. Almost all extracellular proteins (22 spots) and cell wall-associated proteins (40 spots) which showed decreased or increased levels of synthesis during growth in CDM supplemented with PlnA and/or in coculture with strain DPPMA20 or DPPMA174 were identified. On the basis of the sequences in the Kyoto Encyclopedia of Genes and Genomes database, changes to the exoproteome concerned proteins involved in quorum sensing (QS), the transport system, stress response, carbohydrate metabolism and glycolysis, oxidation/ reduction processes, the proteolytic system, amino acid metabolism, cell wall and catabolic processes, and cell shape, growth, and division. Cultivation with PlnA and cocultivation with strains DPPMA20 and, especially, DPMMA174 markedly increased the capacity of L. plantarum DC400 to form biofilms, to adhere to human Caco-2 cells, and to prevent the adhesion of potential intestinal pathogens. These phenotypic traits were in part related to oversynthesized moonlighting proteins (e.g., DnaK and GroEL, pyruvate kinase, enolase, and glyceraldehyde-3-phosphate dehydrogenase) in response to QS mechanisms and interaction with L. plantarum DPPMA20 and, especially, L. sanfranciscensis DPPMA174.

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Section: Figmentioning

confidence: 93%

Effects of the Peptide Pheromone Plantaricin A and Cocultivation with Lactobacillus sanfranciscensis DPPMA174 on the Exoproteome and the Adhesion Capacity of Lactobacillus plantarum DC400

Calasso

Cagno

Angelis

et al. 2013

Appl Environ Microbiol

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“…This possibility is supported by the detection of numerous ribosomal proteins in negative-control samples (see Table S2 in the supplemental material). On the other hand, ribosomal proteins have been detected in numerous studies that have profiled the surface-exposed, secreted, and cell wall-associated proteins of mycobacteria and many other species of Gram-positive bacteria (1,5,32,74,80,87). In bacteria, some ribosomal proteins may have modified functions beyond the translation of mRNA into protein (79).…”

Section: Discussionmentioning

confidence: 99%

“…Mycobacterial groEL1 and groES genes are expressed in an operon and are dominant antigens in many Mycobacterium infections (69,72,85). These proteins have been previously detected on the surface and in the culture filtrate of several Mycobacterium species, as well as on the more distantly related bacterium Bacillus subtilis (5,32,74,80).…”

Section: Fig 3 Comparison Of Biotinylation Profiles From All Experimementioning

confidence: 99%

“…In most bacteria, elongation factor Tu serves a proof-reading function during ribosomal protein synthesis, a process which normally takes place in the cytoplasmic compartment (75). However, both elongation factor Tu and a range of ribosomal proteins have been consistently identified in studies of surface-exposed proteins in mycobacteria and related Gram-positive bacteria (1,5,32,74,80,87).…”

Section: Fig 3 Comparison Of Biotinylation Profiles From All Experimementioning

confidence: 99%

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Surface Proteome of “Mycobacterium avium subsp. hominissuis” during the Early Stages of Macrophage Infection

et al. 2012

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ABSTRACT“Mycobacterium aviumsubsp.hominissuis” is a robust and pervasive environmental bacterium that can cause opportunistic infections in humans. The bacterium overcomes the host immune response and is capable of surviving and replicating within host macrophages. Little is known about the bacterial mechanisms that facilitate these processes, but it can be expected that surface-exposed proteins play an important role. In this study, the selective biotinylation of surface-exposed proteins, streptavidin affinity purification, and shotgun mass spectrometry were used to characterize the surface-exposed proteome ofM. aviumsubsp.hominissuis. This analysis detected more than 100 proteins exposed at the bacterial surface ofM. aviumsubsp.hominissuis. Comparisons of surface-exposed proteins between conditions simulating early infection identified several groups of proteins whose presence on the bacterial surface was either constitutive or appeared to be unique to specific culture conditions. This proteomic profile facilitates an improved understanding ofM. aviumsubsp.hominissuisand how it establishes infection. Additionally, surface-exposed proteins are excellent targets for the host adaptive immune system, and their identification can inform the development of novel treatments, diagnostic tools, and vaccines for mycobacterial disease.

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“…It has been proposed that cell surface proteins are involved in cell protection and surface recognition and that they could be potential mediators in the initial steps involved in autoaggregation and adhesion [8][9][10]. In cell envelope proteome studies of potentially probiotic bacteria, the cell wall protein fraction has typically been extracted by lysozyme-containing buffer [11][12][13][14][15][16], lithium chloride [16,17], or some other cell surface molecule or proteinsolubilizing agent [15][16][17][18].…”

Section: Introductionmentioning

confidence: 99%

Cell surface proteins play an important role in probiotic activities of Lactobacillus reuteri

Singh

Malik

Kaur

2016

Nutrire

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Background: Eight Lactobacillus reuteri strains, previously isolated from breast-fed human infant feces, were selected to assess the potential contribution of their surface proteins in probiotic activity. These strains were treated with 5 M LiCl to remove their surface proteins, and their tolerance to simulated stomach-duodenum passage, cell surface characteristics, autoaggregation, adhesion, and inhibition of pathogen adhesion to Caco-2 cells were compared with untreated strains.

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Proteomic analysis of cell surface-associated proteins from probioticLactobacillus plantarum

Cited by 57 publications

References 43 publications

Effects of the Peptide Pheromone Plantaricin A and Cocultivation with Lactobacillus sanfranciscensis DPPMA174 on the Exoproteome and the Adhesion Capacity of Lactobacillus plantarum DC400

Effects of the Peptide Pheromone Plantaricin A and Cocultivation with Lactobacillus sanfranciscensis DPPMA174 on the Exoproteome and the Adhesion Capacity of Lactobacillus plantarum DC400

Surface Proteome of “Mycobacterium avium subsp. hominissuis” during the Early Stages of Macrophage Infection

Cell surface proteins play an important role in probiotic activities of Lactobacillus reuteri

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