Direct identification of amyloids by label-free quantitative LC-MS

Morten Simonsen Dueholm, Heidi Nolsøe Danielsen, Susan Hove Hansen, Florian-Alexander Herbst, Per Halkjær Nielsen

Research output: Contribution to conference without publisher/journalPosterResearch

Abstract

Direct identification of amyloids by label-free quantitative LC-MS
H. N. Danielsen, S. H. Hansen, F.-A. Herbst, P. H. Nielsen, M. S. Dueholm
Amyloids are highly ordered fibrillar protein polymers used by organisms from all domains of life due to their exceptional properties. We have previously shown that amyloids are widespread among microorganisms in biofilms from various habitats. They are therefore believed to play important roles in biofilm ecology. Despite their common appearance in biofilms, few amyloids have been characterized from biofilm-associated bacteria. However, the few amyloids that have been studied so far have already provided an astonishing demonstration of how the amyloids can be exploited with roles ranging structural components of biofilms, cell envelopes and spore coats to cytotoxins and as reservoirs for quorum-sensing signaling molecules.
The identification of novel functional amyloids is key to understand the many roles of amyloid in biofilms. Isolation of amyloids is unfortunately not a straightforward task. The insolubility and extreme stability of most functional amyloids exclude them from traditional protein analyses. Many functional amyloids are also highly adhesive and therefore bind to pipette tips and other consumables. Pure cultures, large sample volumes and high productivity of amyloids are therefore required for successful purification. We here present a quantitative proteomics technique that allow direct identification of functional amyloid candidates in complex samples based on their structural stability in the presence of increasing concentrations of formic acid.

Original languageEnglish
Publication date19 Sep 2016
Publication statusPublished - 19 Sep 2016
EventThe Danish Microbiological Society Annual Congress 2016 - Eigtved's Pakhus, København, Denmark
Duration: 14 Nov 201614 Nov 2016
http://www.dmselskab.dk/en/congress-2/

Conference

ConferenceThe Danish Microbiological Society Annual Congress 2016
LocationEigtved's Pakhus
CountryDenmark
CityKøbenhavn
Period14/11/201614/11/2016
Internet address

Fingerprint

Amyloid
Biofilms
formic acid
Melanocyte-Stimulating Hormones
Quorum Sensing
Cytotoxins
Cellular Structures
Ecology
Spores
Adhesives
Proteomics
Ecosystem
Polymers
Proteins
Bacteria

Cite this

Dueholm, M. S., Danielsen, H. N., Hansen, S. H., Herbst, F-A., & Nielsen, P. H. (2016). Direct identification of amyloids by label-free quantitative LC-MS. Poster presented at The Danish Microbiological Society Annual Congress 2016, København, Denmark.
Dueholm, Morten Simonsen ; Danielsen, Heidi Nolsøe ; Hansen, Susan Hove ; Herbst, Florian-Alexander ; Nielsen, Per Halkjær. / Direct identification of amyloids by label-free quantitative LC-MS. Poster presented at The Danish Microbiological Society Annual Congress 2016, København, Denmark.
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title = "Direct identification of amyloids by label-free quantitative LC-MS",
abstract = "Direct identification of amyloids by label-free quantitative LC-MSH. N. Danielsen, S. H. Hansen, F.-A. Herbst, P. H. Nielsen, M. S. DueholmAmyloids are highly ordered fibrillar protein polymers used by organisms from all domains of life due to their exceptional properties. We have previously shown that amyloids are widespread among microorganisms in biofilms from various habitats. They are therefore believed to play important roles in biofilm ecology. Despite their common appearance in biofilms, few amyloids have been characterized from biofilm-associated bacteria. However, the few amyloids that have been studied so far have already provided an astonishing demonstration of how the amyloids can be exploited with roles ranging structural components of biofilms, cell envelopes and spore coats to cytotoxins and as reservoirs for quorum-sensing signaling molecules. The identification of novel functional amyloids is key to understand the many roles of amyloid in biofilms. Isolation of amyloids is unfortunately not a straightforward task. The insolubility and extreme stability of most functional amyloids exclude them from traditional protein analyses. Many functional amyloids are also highly adhesive and therefore bind to pipette tips and other consumables. Pure cultures, large sample volumes and high productivity of amyloids are therefore required for successful purification. We here present a quantitative proteomics technique that allow direct identification of functional amyloid candidates in complex samples based on their structural stability in the presence of increasing concentrations of formic acid.",
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Dueholm, MS, Danielsen, HN, Hansen, SH, Herbst, F-A & Nielsen, PH 2016, 'Direct identification of amyloids by label-free quantitative LC-MS', The Danish Microbiological Society Annual Congress 2016, København, Denmark, 14/11/2016 - 14/11/2016.

Direct identification of amyloids by label-free quantitative LC-MS. / Dueholm, Morten Simonsen; Danielsen, Heidi Nolsøe; Hansen, Susan Hove; Herbst, Florian-Alexander; Nielsen, Per Halkjær.

2016. Poster presented at The Danish Microbiological Society Annual Congress 2016, København, Denmark.

Research output: Contribution to conference without publisher/journalPosterResearch

TY - CONF

T1 - Direct identification of amyloids by label-free quantitative LC-MS

AU - Dueholm, Morten Simonsen

AU - Danielsen, Heidi Nolsøe

AU - Hansen, Susan Hove

AU - Herbst, Florian-Alexander

AU - Nielsen, Per Halkjær

PY - 2016/9/19

Y1 - 2016/9/19

N2 - Direct identification of amyloids by label-free quantitative LC-MSH. N. Danielsen, S. H. Hansen, F.-A. Herbst, P. H. Nielsen, M. S. DueholmAmyloids are highly ordered fibrillar protein polymers used by organisms from all domains of life due to their exceptional properties. We have previously shown that amyloids are widespread among microorganisms in biofilms from various habitats. They are therefore believed to play important roles in biofilm ecology. Despite their common appearance in biofilms, few amyloids have been characterized from biofilm-associated bacteria. However, the few amyloids that have been studied so far have already provided an astonishing demonstration of how the amyloids can be exploited with roles ranging structural components of biofilms, cell envelopes and spore coats to cytotoxins and as reservoirs for quorum-sensing signaling molecules. The identification of novel functional amyloids is key to understand the many roles of amyloid in biofilms. Isolation of amyloids is unfortunately not a straightforward task. The insolubility and extreme stability of most functional amyloids exclude them from traditional protein analyses. Many functional amyloids are also highly adhesive and therefore bind to pipette tips and other consumables. Pure cultures, large sample volumes and high productivity of amyloids are therefore required for successful purification. We here present a quantitative proteomics technique that allow direct identification of functional amyloid candidates in complex samples based on their structural stability in the presence of increasing concentrations of formic acid.

AB - Direct identification of amyloids by label-free quantitative LC-MSH. N. Danielsen, S. H. Hansen, F.-A. Herbst, P. H. Nielsen, M. S. DueholmAmyloids are highly ordered fibrillar protein polymers used by organisms from all domains of life due to their exceptional properties. We have previously shown that amyloids are widespread among microorganisms in biofilms from various habitats. They are therefore believed to play important roles in biofilm ecology. Despite their common appearance in biofilms, few amyloids have been characterized from biofilm-associated bacteria. However, the few amyloids that have been studied so far have already provided an astonishing demonstration of how the amyloids can be exploited with roles ranging structural components of biofilms, cell envelopes and spore coats to cytotoxins and as reservoirs for quorum-sensing signaling molecules. The identification of novel functional amyloids is key to understand the many roles of amyloid in biofilms. Isolation of amyloids is unfortunately not a straightforward task. The insolubility and extreme stability of most functional amyloids exclude them from traditional protein analyses. Many functional amyloids are also highly adhesive and therefore bind to pipette tips and other consumables. Pure cultures, large sample volumes and high productivity of amyloids are therefore required for successful purification. We here present a quantitative proteomics technique that allow direct identification of functional amyloid candidates in complex samples based on their structural stability in the presence of increasing concentrations of formic acid.

M3 - Poster

Y2 - 14 November 2016 through 14 November 2016

ER -

Dueholm MS, Danielsen HN, Hansen SH, Herbst F-A, Nielsen PH. Direct identification of amyloids by label-free quantitative LC-MS. 2016. Poster presented at The Danish Microbiological Society Annual Congress 2016, København, Denmark.