Bacterial Flagella: Twist and Stick, or Dodge across the Kingdoms
Publication Date
January 15, 2015
Journal
PLOS Pathogens
Authors
Yannick Rossez, Eliza B. Wolfson, Ashleigh Holmes, David L. Gally, et al
Volume
11
Issue
1
Pages
e1004483
DOI
https://dx.plos.org/10.1371/journal.ppat.1004483
Publisher URL
http://journals.plos.org/plospathogens/article?id=10.1371%2Fjournal.ppat.1004483
PubMed
http://www.ncbi.nlm.nih.gov/pubmed/25590430
PubMed Central
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4295861
Europe PMC
http://europepmc.org/abstract/MED/25590430
Web of Science
000349106100001
Scopus
84923844712
Mendeley
http://www.mendeley.com/research/bacterial-flagella-twist-stick-dodge-across-kingdoms
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Mendeley | Further Information

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CrossRef

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1867406"], "description"=>"<p>Left, a summary of key characteristics of the flagella apparatus that are advantageous for adherence, and right, specific properties highlighted on the left. (A) Flagellum length results in a long reach towards colonization surfaces as an early-stage anchor—higher affinity binding can occur at closer proximity with specific adhesins and receptors. (B) Flagella rotation generates force that promotes membrane interactions during initial adherence. (C) Flagella are highly repetitive structures, non-specific low affinity binding can result in adhesion at high avidities.</p>", "links"=>[], "tags"=>["binding epitopes", "adherence", "Bacterial flagella", "flagella binding", "flagellum organelle", "Salmonella enterica", "Campylobacter jejuni", "organelles act", "host tissues", "interaction", "recognition impacts", "context", "Recent work", "plasma membrane components", "Escherichia coli", "function", "favourable surface topologies", "flagellin monomers", "multiprotein assembly", "animal reservoirs", "animal pathogens", "Pseudomonas aeruginosa", "host colonisation"], "article_id"=>1290360, "categories"=>["Uncategorised"], "users"=>["Yannick Rossez", "Eliza B. Wolfson", "Ashleigh Holmes", "David L. Gally", "Nicola J. Holden"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1004483.g001", "stats"=>{"downloads"=>0, "page_views"=>24, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_biophysical_properties_of_flagella_to_8220_twist_and_stick_8221_lend_themselves_towards_nonspecific_adhesion_/1290360", "title"=>"The biophysical properties of flagella, to “twist and stick,” lend themselves towards nonspecific adhesion.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-01-15 14:45:09"}
  • {"files"=>["https://ndownloader.figshare.com/files/1867410"], "description"=>"<p>(A) Flagella filaments degrade, releasing monomeric flagellin, the residues of which are recognised by receptor TLR5, NLRC4, or FLS2, resulting in cytokine release or PTI. The example residues and receptor (right) shown are involved in TLR5 recognition. (B) Flagellin recognition by TLR5, NLRC4, or FLS2 is evaded by variation in key residues involved in flagellin detection, which can necessitate compensatory mutations. (C) Bacteria secrete enzymes that specifically target and degrade monomeric flagellin, preventing its recognition by TLR5, NLRC4, or FLS2. (D) Post-translational glyosylation of flagellin is thought to enhance flagella stability; reduced release of flagellin from flagella filaments will result in reduced recognition by TLR5 or FLS2. (E) Bacteria secrete effector proteins that interfere with TLR5, NLRC4, or FLS2 recognition either by direct inhibition of receptor expression or binding, or by inhibition of downstream signalling pathways. (F) Bacteria down-regulate or switch off flagella expression when motility and/or binding are no longer required.</p>", "links"=>[], "tags"=>["binding epitopes", "adherence", "Bacterial flagella", "flagella binding", "flagellum organelle", "Salmonella enterica", "Campylobacter jejuni", "organelles act", "host tissues", "interaction", "recognition impacts", "context", "Recent work", "plasma membrane components", "Escherichia coli", "function", "favourable surface topologies", "flagellin monomers", "multiprotein assembly", "animal reservoirs", "animal pathogens", "Pseudomonas aeruginosa", "host colonisation"], "article_id"=>1290364, "categories"=>["Uncategorised"], "users"=>["Yannick Rossez", "Eliza B. Wolfson", "Ashleigh Holmes", "David L. Gally", "Nicola J. Holden"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1004483.g003", "stats"=>{"downloads"=>4, "page_views"=>28, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_A_variety_of_mechanisms_employed_to_8220_dodge_8221_the_flagellin_innate_immune_response_/1290364", "title"=>"A variety of mechanisms employed to “dodge” the flagellin innate immune response.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-01-15 14:45:09"}
  • {"files"=>["https://ndownloader.figshare.com/files/1867408"], "description"=>"<p>Top: backbone of the key residues of flagellin recognized by plant (left) and animal (right) innate immune receptors are highlighted in red. FliC from <i>S. enterica</i> is presented as a “model” flagellin, with reports for recognition by both TLR5 and FLS2 receptors. These residues are superimposed on the solved flagellin structure (PDB# 1UCU) in UCSF Chimera [<a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004483#ppat.1004483.ref113\" target=\"_blank\">113</a>]. Surfaces and backbone are coloured according to previously assigned structural domains as indicated below each monomer [<a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1004483#ppat.1004483.ref057\" target=\"_blank\">57</a>]. Bottom: recognition of flagella filaments by plant (left) and animal (right) innate immune receptors does not occur as key residues (surfaces highlighted in red) are hidden within the filament structure. However, immune recognition still occurs in animals via antibody recognition of the D3 domain.</p>", "links"=>[], "tags"=>["binding epitopes", "adherence", "Bacterial flagella", "flagella binding", "flagellum organelle", "Salmonella enterica", "Campylobacter jejuni", "organelles act", "host tissues", "interaction", "recognition impacts", "context", "Recent work", "plasma membrane components", "Escherichia coli", "function", "favourable surface topologies", "flagellin monomers", "multiprotein assembly", "animal reservoirs", "animal pathogens", "Pseudomonas aeruginosa", "host colonisation"], "article_id"=>1290362, "categories"=>["Uncategorised"], "users"=>["Yannick Rossez", "Eliza B. Wolfson", "Ashleigh Holmes", "David L. Gally", "Nicola J. Holden"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1004483.g002", "stats"=>{"downloads"=>0, "page_views"=>73, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Cross_kingdom_immune_recognition_of_flagellin_structures_/1290362", "title"=>"Cross-kingdom immune recognition of flagellin structures.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2015-01-15 14:45:09"}

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{"start_date"=>"2015-01-01T00:00:00Z", "end_date"=>"2015-12-31T00:00:00Z", "subject_areas"=>[]}
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