Widespread abundance of functional bacterial amyloid in mycolata and other gram-positive bacteria

Peter Bruun Jordal; Morten Simonsen Dueholm; Poul Larsen; Steen Vang Petersen; Jan J. Enghild; Gunna Christiansen; Peter Højrup; Per Halkjaer Nielsen; Daniel Erik Otzen

doi:10.1128/AEM.02107-08

Widespread abundance of functional bacterial amyloid in mycolata and other gram-positive bacteria

Peter Bruun Jordal, Morten Simonsen Dueholm, Poul Larsen, Steen Vang Petersen, Jan J. Enghild, Gunna Christiansen, Peter Højrup, Per Halkjaer Nielsen, Daniel Erik Otzen

Department of Chemistry - Center for Uopløselige Proteinstrukturer

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

63 Citations (Scopus)

Abstract

Until recently, extracellular functional bacterial amyloid (FuBA) has been detected and characterized in only a few bacterial species, including Escherichia coli, Salmonella, and the gram-positive organism Streptomyces coelicolor. Here we probed gram-positive bacteria with conformationally specific antibodies and revealed the existence of FuBA in 12 of 14 examined mycolata species, as well as six other distantly related species examined belonging to the phyla Actinobacteria and Firmicutes. Most of the bacteria produced extracellular fimbriae, sometimes copious amounts of them, and in two cases large extracellular fibrils were also produced. In three cases, FuBA was revealed only after extensive removal of extracellular material by saponification, indicating that there is integrated attachment within the cellular envelope. Spores of species in the genera Streptomyces, Bacillus, and Nocardia were all coated with amyloids. FuBA was purified from Gordonia amarae (from the cell envelope) and Geodermatophilus obscurus, and they had the morphology, tinctorial properties, and beta-rich structure typical of amyloid. The presence of approximately 9-nm-wide amyloids in the cell envelope of G. amarae was visualized by transmission electron microscopy analysis. We conclude that amyloid is widespread among gram-positive bacteria and may in many species constitute a hitherto overlooked integral part of the spore and the cellular envelope.

Original language	English
Journal	Applied and Environmental Microbiology
Volume	75
Issue	12
Pages (from-to)	4101-10
Number of pages	9
ISSN	0099-2240
DOIs	https://doi.org/10.1128/AEM.02107-08
Publication status	Published - 2009

Keywords

Amyloid
Bacterial Proteins
Cell Wall
Gram-Positive Bacteria
Microscopy, Electron, Transmission
Protein Structure, Secondary

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10.1128/AEM.02107-08

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title = "Widespread abundance of functional bacterial amyloid in mycolata and other gram-positive bacteria",

abstract = "Until recently, extracellular functional bacterial amyloid (FuBA) has been detected and characterized in only a few bacterial species, including Escherichia coli, Salmonella, and the gram-positive organism Streptomyces coelicolor. Here we probed gram-positive bacteria with conformationally specific antibodies and revealed the existence of FuBA in 12 of 14 examined mycolata species, as well as six other distantly related species examined belonging to the phyla Actinobacteria and Firmicutes. Most of the bacteria produced extracellular fimbriae, sometimes copious amounts of them, and in two cases large extracellular fibrils were also produced. In three cases, FuBA was revealed only after extensive removal of extracellular material by saponification, indicating that there is integrated attachment within the cellular envelope. Spores of species in the genera Streptomyces, Bacillus, and Nocardia were all coated with amyloids. FuBA was purified from Gordonia amarae (from the cell envelope) and Geodermatophilus obscurus, and they had the morphology, tinctorial properties, and beta-rich structure typical of amyloid. The presence of approximately 9-nm-wide amyloids in the cell envelope of G. amarae was visualized by transmission electron microscopy analysis. We conclude that amyloid is widespread among gram-positive bacteria and may in many species constitute a hitherto overlooked integral part of the spore and the cellular envelope.",

keywords = "Amyloid, Bacterial Proteins, Cell Wall, Gram-Positive Bacteria, Microscopy, Electron, Transmission, Protein Structure, Secondary",

author = "Jordal, {Peter Bruun} and Dueholm, {Morten Simonsen} and Poul Larsen and Petersen, {Steen Vang} and Enghild, {Jan J.} and Gunna Christiansen and Peter H{\o}jrup and Nielsen, {Per Halkjaer} and Otzen, {Daniel Erik}",

year = "2009",

doi = "10.1128/AEM.02107-08",

language = "English",

volume = "75",

pages = "4101--10",

journal = "Applied and Environmental Microbiology",

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publisher = "American Society for Microbiology",

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Widespread abundance of functional bacterial amyloid in mycolata and other gram-positive bacteria. / Jordal, Peter Bruun; Dueholm, Morten Simonsen; Larsen, Poul et al.
In: Applied and Environmental Microbiology, Vol. 75, No. 12, 2009, p. 4101-10.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

TY - JOUR

T1 - Widespread abundance of functional bacterial amyloid in mycolata and other gram-positive bacteria

AU - Jordal, Peter Bruun

AU - Dueholm, Morten Simonsen

AU - Larsen, Poul

AU - Petersen, Steen Vang

AU - Enghild, Jan J.

AU - Christiansen, Gunna

AU - Højrup, Peter

AU - Nielsen, Per Halkjaer

AU - Otzen, Daniel Erik

PY - 2009

Y1 - 2009

N2 - Until recently, extracellular functional bacterial amyloid (FuBA) has been detected and characterized in only a few bacterial species, including Escherichia coli, Salmonella, and the gram-positive organism Streptomyces coelicolor. Here we probed gram-positive bacteria with conformationally specific antibodies and revealed the existence of FuBA in 12 of 14 examined mycolata species, as well as six other distantly related species examined belonging to the phyla Actinobacteria and Firmicutes. Most of the bacteria produced extracellular fimbriae, sometimes copious amounts of them, and in two cases large extracellular fibrils were also produced. In three cases, FuBA was revealed only after extensive removal of extracellular material by saponification, indicating that there is integrated attachment within the cellular envelope. Spores of species in the genera Streptomyces, Bacillus, and Nocardia were all coated with amyloids. FuBA was purified from Gordonia amarae (from the cell envelope) and Geodermatophilus obscurus, and they had the morphology, tinctorial properties, and beta-rich structure typical of amyloid. The presence of approximately 9-nm-wide amyloids in the cell envelope of G. amarae was visualized by transmission electron microscopy analysis. We conclude that amyloid is widespread among gram-positive bacteria and may in many species constitute a hitherto overlooked integral part of the spore and the cellular envelope.

AB - Until recently, extracellular functional bacterial amyloid (FuBA) has been detected and characterized in only a few bacterial species, including Escherichia coli, Salmonella, and the gram-positive organism Streptomyces coelicolor. Here we probed gram-positive bacteria with conformationally specific antibodies and revealed the existence of FuBA in 12 of 14 examined mycolata species, as well as six other distantly related species examined belonging to the phyla Actinobacteria and Firmicutes. Most of the bacteria produced extracellular fimbriae, sometimes copious amounts of them, and in two cases large extracellular fibrils were also produced. In three cases, FuBA was revealed only after extensive removal of extracellular material by saponification, indicating that there is integrated attachment within the cellular envelope. Spores of species in the genera Streptomyces, Bacillus, and Nocardia were all coated with amyloids. FuBA was purified from Gordonia amarae (from the cell envelope) and Geodermatophilus obscurus, and they had the morphology, tinctorial properties, and beta-rich structure typical of amyloid. The presence of approximately 9-nm-wide amyloids in the cell envelope of G. amarae was visualized by transmission electron microscopy analysis. We conclude that amyloid is widespread among gram-positive bacteria and may in many species constitute a hitherto overlooked integral part of the spore and the cellular envelope.

KW - Amyloid

KW - Bacterial Proteins

KW - Cell Wall

KW - Gram-Positive Bacteria

KW - Microscopy, Electron, Transmission

KW - Protein Structure, Secondary

U2 - 10.1128/AEM.02107-08

DO - 10.1128/AEM.02107-08

M3 - Journal article

C2 - 19395568

SN - 0099-2240

VL - 75

SP - 4101

EP - 4110

JO - Applied and Environmental Microbiology

JF - Applied and Environmental Microbiology

IS - 12

ER -

Widespread abundance of functional bacterial amyloid in mycolata and other gram-positive bacteria

Abstract

Keywords

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