Re-evaluation of a bacterial antifreeze protein as an adhesin with ice-binding activity.
A novel role for antifreeze proteins (AFPs) may reside in an exceptionally large 1.5-MDa adhesin isolated from an Antarctic Gram-negative bacterium, Marinomonas primoryensis. MpAFP was purified from bacterial lysates by ice adsorption and gel electrophoresis. We have previously reported that two hig...
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ftdoajarticles:oai:doaj.org/article:2a1ec4efd375459a97808868c86ebef6 2023-05-15T13:59:23+02:00 Re-evaluation of a bacterial antifreeze protein as an adhesin with ice-binding activity. Shuaiqi Guo Christopher P Garnham John C Whitney Laurie A Graham Peter L Davies 2012-01-01T00:00:00Z https://doi.org/10.1371/journal.pone.0048805 https://doaj.org/article/2a1ec4efd375459a97808868c86ebef6 EN eng Public Library of Science (PLoS) http://europepmc.org/articles/PMC3492233?pdf=render https://doaj.org/toc/1932-6203 1932-6203 doi:10.1371/journal.pone.0048805 https://doaj.org/article/2a1ec4efd375459a97808868c86ebef6 PLoS ONE, Vol 7, Iss 11, p e48805 (2012) Medicine R Science Q article 2012 ftdoajarticles https://doi.org/10.1371/journal.pone.0048805 2022-12-31T01:13:23Z A novel role for antifreeze proteins (AFPs) may reside in an exceptionally large 1.5-MDa adhesin isolated from an Antarctic Gram-negative bacterium, Marinomonas primoryensis. MpAFP was purified from bacterial lysates by ice adsorption and gel electrophoresis. We have previously reported that two highly repetitive sequences, region II (RII) and region IV (RIV), divide MpAFP into five distinct regions, all of which require mM Ca(2+) levels for correct folding. Also, the antifreeze activity is confined to the 322-residue RIV, which forms a Ca(2+)-bound beta-helix containing thirteen Repeats-In-Toxin (RTX)-like repeats. RII accounts for approximately 90% of the mass of MpAFP and is made up of ∼120 tandem 104-residue repeats. Because these repeats are identical in DNA sequence, their number was estimated here by pulsed-field gel electrophoresis. Structural homology analysis by the Protein Homology/analogY Recognition Engine (Phyre2) server indicates that the 104-residue RII repeat adopts an immunoglobulin beta-sandwich fold that is typical of many secreted adhesion proteins. Additional RTX-like repeats in RV may serve as a non-cleavable signal sequence for the type I secretion pathway. Immunodetection shows both repeated regions are uniformly distributed over the cell surface. We suggest that the development of an AFP-like domain within this adhesin attached to the bacterial outer surface serves to transiently bind the host bacteria to ice. This association would keep the bacteria within the upper reaches of the water column where oxygen and nutrients are potentially more abundant. This novel envirotactic role would give AFPs a third function, after freeze avoidance and freeze tolerance: that of transiently binding an organism to ice. Article in Journal/Newspaper Antarc* Antarctic Directory of Open Access Journals: DOAJ Articles Antarctic PLoS ONE 7 11 e48805 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
Medicine R Science Q |
spellingShingle |
Medicine R Science Q Shuaiqi Guo Christopher P Garnham John C Whitney Laurie A Graham Peter L Davies Re-evaluation of a bacterial antifreeze protein as an adhesin with ice-binding activity. |
topic_facet |
Medicine R Science Q |
description |
A novel role for antifreeze proteins (AFPs) may reside in an exceptionally large 1.5-MDa adhesin isolated from an Antarctic Gram-negative bacterium, Marinomonas primoryensis. MpAFP was purified from bacterial lysates by ice adsorption and gel electrophoresis. We have previously reported that two highly repetitive sequences, region II (RII) and region IV (RIV), divide MpAFP into five distinct regions, all of which require mM Ca(2+) levels for correct folding. Also, the antifreeze activity is confined to the 322-residue RIV, which forms a Ca(2+)-bound beta-helix containing thirteen Repeats-In-Toxin (RTX)-like repeats. RII accounts for approximately 90% of the mass of MpAFP and is made up of ∼120 tandem 104-residue repeats. Because these repeats are identical in DNA sequence, their number was estimated here by pulsed-field gel electrophoresis. Structural homology analysis by the Protein Homology/analogY Recognition Engine (Phyre2) server indicates that the 104-residue RII repeat adopts an immunoglobulin beta-sandwich fold that is typical of many secreted adhesion proteins. Additional RTX-like repeats in RV may serve as a non-cleavable signal sequence for the type I secretion pathway. Immunodetection shows both repeated regions are uniformly distributed over the cell surface. We suggest that the development of an AFP-like domain within this adhesin attached to the bacterial outer surface serves to transiently bind the host bacteria to ice. This association would keep the bacteria within the upper reaches of the water column where oxygen and nutrients are potentially more abundant. This novel envirotactic role would give AFPs a third function, after freeze avoidance and freeze tolerance: that of transiently binding an organism to ice. |
format |
Article in Journal/Newspaper |
author |
Shuaiqi Guo Christopher P Garnham John C Whitney Laurie A Graham Peter L Davies |
author_facet |
Shuaiqi Guo Christopher P Garnham John C Whitney Laurie A Graham Peter L Davies |
author_sort |
Shuaiqi Guo |
title |
Re-evaluation of a bacterial antifreeze protein as an adhesin with ice-binding activity. |
title_short |
Re-evaluation of a bacterial antifreeze protein as an adhesin with ice-binding activity. |
title_full |
Re-evaluation of a bacterial antifreeze protein as an adhesin with ice-binding activity. |
title_fullStr |
Re-evaluation of a bacterial antifreeze protein as an adhesin with ice-binding activity. |
title_full_unstemmed |
Re-evaluation of a bacterial antifreeze protein as an adhesin with ice-binding activity. |
title_sort |
re-evaluation of a bacterial antifreeze protein as an adhesin with ice-binding activity. |
publisher |
Public Library of Science (PLoS) |
publishDate |
2012 |
url |
https://doi.org/10.1371/journal.pone.0048805 https://doaj.org/article/2a1ec4efd375459a97808868c86ebef6 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
PLoS ONE, Vol 7, Iss 11, p e48805 (2012) |
op_relation |
http://europepmc.org/articles/PMC3492233?pdf=render https://doaj.org/toc/1932-6203 1932-6203 doi:10.1371/journal.pone.0048805 https://doaj.org/article/2a1ec4efd375459a97808868c86ebef6 |
op_doi |
https://doi.org/10.1371/journal.pone.0048805 |
container_title |
PLoS ONE |
container_volume |
7 |
container_issue |
11 |
container_start_page |
e48805 |
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