Abstract

This study compared the secretomes (proteins exported out of the cell) of Propionibacterium freudenreichii of different origin to identify plausible adaptation factors. Phylosecretomics indicated strain-specific variation in secretion of adhesins/invasins (SlpA, InlA), cell-wall hydrolysing (NlpC60 peptidase, transglycosylase), protective (RpfB) and moonlighting (DnaK, GroEL, GaPDH, IDH, ENO, ClpB) enzymes and/or proteins. Detailed secretome comparison suggested that one of the cereal strains (JS14) released a tip fimbrillin (FimB) in to the extracellular milieu, which was in line with the electron microscopy and genomic analyses, indicating the lack of surface-associated fimbrial-like structures, predicting a mutated type-2 fimbrial gene cluster (fimB-fimA-srtC2) and production of anchorless FimB. Instead, the cereal strain produced high amounts of SlpB that tentatively mediated adherent growth on hydrophilic surface and adherence to hydrophobic material. One of the dairy strains (JS22), producing non-covalently bound surface-proteins (LspA, ClpB, AraI) and releasing SlpA and InlA into the culture medium, was found to form clumps under physiological conditions. The JS22 strain lacked SlpB and displayed a non-clumping and biofilm-forming phenotype only under conditions of increased ionic strength (300mM NaCl). However, this strain cultured under the same conditions was not adherent to hydrophobic support, which supports the contributory role of SlpB in mediating hydrophobic interactions. Thus, this study reports significant secretome variation in P.freudenreichii and suggests that strain-specific differences in protein export, modification and protein-protein interactions have been the driving forces behind the adaptation of this bacterial species.
Original languageEnglish
JournalMicrobial Biotechnology
Volume11
Issue number3
Pages (from-to)510-526
Number of pages17
ISSN1751-7915
DOIs
Publication statusPublished - 28 Feb 2018
MoE publication typeA1 Journal article-refereed

Fields of Science

  • 1183 Plant biology, microbiology, virology
  • RESUSCITATION-PROMOTING FACTORS
  • LACTOBACILLUS-RHAMNOSUS
  • ANTIINFLAMMATORY PROPERTIES
  • MYCOBACTERIUM-TUBERCULOSIS
  • DAIRY PROPIONIBACTERIA
  • MOONLIGHTING PROTEINS
  • PROVIDES INSIGHTS
  • GENOME SEQUENCE
  • CELL-SURFACE
  • IN-VITRO

Cite this

@article{983eedef848c4c258fa38ed03e452759,
title = "Secretome profiling of Propionibacterium freudenreichii reveals highly variable responses even among the closely related strains",
abstract = "This study compared the secretomes (proteins exported out of the cell) of Propionibacterium freudenreichii of different origin to identify plausible adaptation factors. Phylosecretomics indicated strain-specific variation in secretion of adhesins/invasins (SlpA, InlA), cell-wall hydrolysing (NlpC60 peptidase, transglycosylase), protective (RpfB) and moonlighting (DnaK, GroEL, GaPDH, IDH, ENO, ClpB) enzymes and/or proteins. Detailed secretome comparison suggested that one of the cereal strains (JS14) released a tip fimbrillin (FimB) in to the extracellular milieu, which was in line with the electron microscopy and genomic analyses, indicating the lack of surface-associated fimbrial-like structures, predicting a mutated type-2 fimbrial gene cluster (fimB-fimA-srtC2) and production of anchorless FimB. Instead, the cereal strain produced high amounts of SlpB that tentatively mediated adherent growth on hydrophilic surface and adherence to hydrophobic material. One of the dairy strains (JS22), producing non-covalently bound surface-proteins (LspA, ClpB, AraI) and releasing SlpA and InlA into the culture medium, was found to form clumps under physiological conditions. The JS22 strain lacked SlpB and displayed a non-clumping and biofilm-forming phenotype only under conditions of increased ionic strength (300mM NaCl). However, this strain cultured under the same conditions was not adherent to hydrophobic support, which supports the contributory role of SlpB in mediating hydrophobic interactions. Thus, this study reports significant secretome variation in P.freudenreichii and suggests that strain-specific differences in protein export, modification and protein-protein interactions have been the driving forces behind the adaptation of this bacterial species.",
keywords = "1183 Plant biology, microbiology, virology, RESUSCITATION-PROMOTING FACTORS, LACTOBACILLUS-RHAMNOSUS, ANTIINFLAMMATORY PROPERTIES, MYCOBACTERIUM-TUBERCULOSIS, DAIRY PROPIONIBACTERIA, MOONLIGHTING PROTEINS, PROVIDES INSIGHTS, GENOME SEQUENCE, CELL-SURFACE, IN-VITRO",
author = "Frohnmeyer, {Esther Gesine} and Paulina Deptula and Nyman, {Tuula Anneli} and Laine, {Pia Kati Sofia} and Vihinen, {Anja Helena} and Paulin, {Lars G{\"o}ran} and Auvinen, {Petri Olli Viljami} and Jokitalo, {Eija Sofia} and Piironen, {Vieno Irene} and Varmanen, {Pekka Kristian} and Savijoki, {Kirsi Kristiina}",
year = "2018",
month = "2",
day = "28",
doi = "10.1111/1751-7915.13254",
language = "English",
volume = "11",
pages = "510--526",
journal = "Microbial Biotechnology",
issn = "0964-7562",
publisher = "Wiley",
number = "3",

}

TY - JOUR

T1 - Secretome profiling of Propionibacterium freudenreichii reveals highly variable responses even among the closely related strains

AU - Frohnmeyer, Esther Gesine

AU - Deptula, Paulina

AU - Nyman, Tuula Anneli

AU - Laine, Pia Kati Sofia

AU - Vihinen, Anja Helena

AU - Paulin, Lars Göran

AU - Auvinen, Petri Olli Viljami

AU - Jokitalo, Eija Sofia

AU - Piironen, Vieno Irene

AU - Varmanen, Pekka Kristian

AU - Savijoki, Kirsi Kristiina

PY - 2018/2/28

Y1 - 2018/2/28

N2 - This study compared the secretomes (proteins exported out of the cell) of Propionibacterium freudenreichii of different origin to identify plausible adaptation factors. Phylosecretomics indicated strain-specific variation in secretion of adhesins/invasins (SlpA, InlA), cell-wall hydrolysing (NlpC60 peptidase, transglycosylase), protective (RpfB) and moonlighting (DnaK, GroEL, GaPDH, IDH, ENO, ClpB) enzymes and/or proteins. Detailed secretome comparison suggested that one of the cereal strains (JS14) released a tip fimbrillin (FimB) in to the extracellular milieu, which was in line with the electron microscopy and genomic analyses, indicating the lack of surface-associated fimbrial-like structures, predicting a mutated type-2 fimbrial gene cluster (fimB-fimA-srtC2) and production of anchorless FimB. Instead, the cereal strain produced high amounts of SlpB that tentatively mediated adherent growth on hydrophilic surface and adherence to hydrophobic material. One of the dairy strains (JS22), producing non-covalently bound surface-proteins (LspA, ClpB, AraI) and releasing SlpA and InlA into the culture medium, was found to form clumps under physiological conditions. The JS22 strain lacked SlpB and displayed a non-clumping and biofilm-forming phenotype only under conditions of increased ionic strength (300mM NaCl). However, this strain cultured under the same conditions was not adherent to hydrophobic support, which supports the contributory role of SlpB in mediating hydrophobic interactions. Thus, this study reports significant secretome variation in P.freudenreichii and suggests that strain-specific differences in protein export, modification and protein-protein interactions have been the driving forces behind the adaptation of this bacterial species.

AB - This study compared the secretomes (proteins exported out of the cell) of Propionibacterium freudenreichii of different origin to identify plausible adaptation factors. Phylosecretomics indicated strain-specific variation in secretion of adhesins/invasins (SlpA, InlA), cell-wall hydrolysing (NlpC60 peptidase, transglycosylase), protective (RpfB) and moonlighting (DnaK, GroEL, GaPDH, IDH, ENO, ClpB) enzymes and/or proteins. Detailed secretome comparison suggested that one of the cereal strains (JS14) released a tip fimbrillin (FimB) in to the extracellular milieu, which was in line with the electron microscopy and genomic analyses, indicating the lack of surface-associated fimbrial-like structures, predicting a mutated type-2 fimbrial gene cluster (fimB-fimA-srtC2) and production of anchorless FimB. Instead, the cereal strain produced high amounts of SlpB that tentatively mediated adherent growth on hydrophilic surface and adherence to hydrophobic material. One of the dairy strains (JS22), producing non-covalently bound surface-proteins (LspA, ClpB, AraI) and releasing SlpA and InlA into the culture medium, was found to form clumps under physiological conditions. The JS22 strain lacked SlpB and displayed a non-clumping and biofilm-forming phenotype only under conditions of increased ionic strength (300mM NaCl). However, this strain cultured under the same conditions was not adherent to hydrophobic support, which supports the contributory role of SlpB in mediating hydrophobic interactions. Thus, this study reports significant secretome variation in P.freudenreichii and suggests that strain-specific differences in protein export, modification and protein-protein interactions have been the driving forces behind the adaptation of this bacterial species.

KW - 1183 Plant biology, microbiology, virology

KW - RESUSCITATION-PROMOTING FACTORS

KW - LACTOBACILLUS-RHAMNOSUS

KW - ANTIINFLAMMATORY PROPERTIES

KW - MYCOBACTERIUM-TUBERCULOSIS

KW - DAIRY PROPIONIBACTERIA

KW - MOONLIGHTING PROTEINS

KW - PROVIDES INSIGHTS

KW - GENOME SEQUENCE

KW - CELL-SURFACE

KW - IN-VITRO

U2 - 10.1111/1751-7915.13254

DO - 10.1111/1751-7915.13254

M3 - Article

VL - 11

SP - 510

EP - 526

JO - Microbial Biotechnology

JF - Microbial Biotechnology

SN - 0964-7562

IS - 3

ER -