Ligilactobacillus agilis BKN88 possesses thermo-/acid-stable heteropolymeric flagellar filaments

Many flagellated bacteria possess multiple flagellins, but the roles and the compositions of each flagellin are diverse and poorly understood. In BKN88, there are two active flagellin gene paralogues but their function and composition in its flagellar filaments have not been described. The aim of th...

Full description

Saved in:
Bibliographic Details
Published inMicrobiology (Society for General Microbiology) Vol. 167; no. 3
Main Authors Eguchi, Naoto, Suzuki, Shunya, Yokota, Kenji, Igimi, Shizunobu, Kajikawa, Akinobu
Format Journal Article
LanguageEnglish
Published England 01.03.2021
Subjects
Online AccessGet full text

Cover

Loading…
Abstract Many flagellated bacteria possess multiple flagellins, but the roles and the compositions of each flagellin are diverse and poorly understood. In BKN88, there are two active flagellin gene paralogues but their function and composition in its flagellar filaments have not been described. The aim of this study is to find the function and composition of the flagellins by employing mutant strains each of which expresses a single flagellin or a modified flagellin. Two single flagellin-expressing strains were both flagellated while the number of flagella per cell in the single flagellin-expressing derivatives was lower than that in the wild type. Nonetheless, these derivative strains were apparently equally motile as the wild type. This indicates that either flagellin is sufficient for cell motility. The immunological activity via Toll-like receptor 5 of the single flagellin-expressing strains or purified single flagellins was readily detectable but mostly variably weaker than that of the wild type. The flagellar filaments of wild type BKN88 were more acid-/thermo-stable than those of single flagellin-expressing derivatives. Using a combination of immunoprecipitation and flagellin-specific staining, wild type BKN88 appeared to possess heteropolymeric flagellar filaments consisting of both flagellins and each flagellin appeared to be equally distributed throughout the filaments. The results of this study suggest that the two flagellins together form a more robust filament than either alone and are thus functionally complementary.
AbstractList Many flagellated bacteria possess multiple flagellins, but the roles and the compositions of each flagellin are diverse and poorly understood. In BKN88, there are two active flagellin gene paralogues but their function and composition in its flagellar filaments have not been described. The aim of this study is to find the function and composition of the flagellins by employing mutant strains each of which expresses a single flagellin or a modified flagellin. Two single flagellin-expressing strains were both flagellated while the number of flagella per cell in the single flagellin-expressing derivatives was lower than that in the wild type. Nonetheless, these derivative strains were apparently equally motile as the wild type. This indicates that either flagellin is sufficient for cell motility. The immunological activity via Toll-like receptor 5 of the single flagellin-expressing strains or purified single flagellins was readily detectable but mostly variably weaker than that of the wild type. The flagellar filaments of wild type BKN88 were more acid-/thermo-stable than those of single flagellin-expressing derivatives. Using a combination of immunoprecipitation and flagellin-specific staining, wild type BKN88 appeared to possess heteropolymeric flagellar filaments consisting of both flagellins and each flagellin appeared to be equally distributed throughout the filaments. The results of this study suggest that the two flagellins together form a more robust filament than either alone and are thus functionally complementary.
Many flagellated bacteria possess multiple flagellins, but the roles and the compositions of each flagellin are diverse and poorly understood. In Ligilactobacillus agilis BKN88, there are two active flagellin gene paralogues but their function and composition in its flagellar filaments have not been described. The aim of this study is to find the function and composition of the flagellins by employing mutant strains each of which expresses a single flagellin or a modified flagellin. Two single flagellin-expressing strains were both flagellated while the number of flagella per cell in the single flagellin-expressing derivatives was lower than that in the wild type. Nonetheless, these derivative strains were apparently equally motile as the wild type. This indicates that either flagellin is sufficient for cell motility. The immunological activity via Toll-like receptor 5 of the single flagellin-expressing strains or purified single flagellins was readily detectable but mostly variably weaker than that of the wild type. The flagellar filaments of wild type L. agilis BKN88 were more acid-/thermo-stable than those of single flagellin-expressing derivatives. Using a combination of immunoprecipitation and flagellin-specific staining, wild type BKN88 appeared to possess heteropolymeric flagellar filaments consisting of both flagellins and each flagellin appeared to be equally distributed throughout the filaments. The results of this study suggest that the two flagellins together form a more robust filament than either alone and are thus functionally complementary.
Author Kajikawa, Akinobu
Yokota, Kenji
Eguchi, Naoto
Suzuki, Shunya
Igimi, Shizunobu
Author_xml – sequence: 1
  givenname: Naoto
  surname: Eguchi
  fullname: Eguchi, Naoto
  organization: Department of Agricultural Chemistry, Graduate School of Tokyo University of Agriculture, 1-1-1 Sakuragaoka, Setagaya, Tokyo 156-8502, Japan
– sequence: 2
  givenname: Shunya
  surname: Suzuki
  fullname: Suzuki, Shunya
  organization: Department of Agricultural Chemistry, Graduate School of Tokyo University of Agriculture, 1-1-1 Sakuragaoka, Setagaya, Tokyo 156-8502, Japan
– sequence: 3
  givenname: Kenji
  surname: Yokota
  fullname: Yokota, Kenji
  organization: Department of Agricultural Chemistry, Tokyo University of Agriculture, 1-1-1 Sakuragaoka, Setagaya, Tokyo 156-8502, Japan
– sequence: 4
  givenname: Shizunobu
  surname: Igimi
  fullname: Igimi, Shizunobu
  organization: Department of Agricultural Chemistry, Tokyo University of Agriculture, 1-1-1 Sakuragaoka, Setagaya, Tokyo 156-8502, Japan
– sequence: 5
  givenname: Akinobu
  surname: Kajikawa
  fullname: Kajikawa, Akinobu
  organization: Department of Agricultural Chemistry, Tokyo University of Agriculture, 1-1-1 Sakuragaoka, Setagaya, Tokyo 156-8502, Japan
BackLink https://www.ncbi.nlm.nih.gov/pubmed/33502302$$D View this record in MEDLINE/PubMed
BookMark eNo9kE1PwzAMhiM0xNjgxhn1yIFuTtOmyREmvsQEFziXNHW2ovSDpD3s35NpA8mSLfvxK_udkUnbtUjIFYUFBSmXTa0XsACgkMAJOacpz-IEBExCzTKIQeTJlMy8_w5MyoGekSkLg4RBck6-1vWmtkoPXal0be3oIxUatY_uX9-EiPrOe9xHNGzRNV28DFgV-0GVFqMtDui6vrO7Bl2tI2PVBq1VLjJBtMF28Bfk1Cjr8fKY5-Tz8eFj9Ryv359eVnfrWDOZDbExKs2rUmScghLIElGKtJJ5zrXUHAVXeV4ZlWW5qVSueVlpmQHNNKaJlJKxObk56Pau-xnRD0VTe70_psVu9EWSCsq5oCwN6O0B1S5859AUvasb5XYFhWLvaVjVBRQHTwN-fVQeywarf_jPRPYLm751Ew
CitedBy_id crossref_primary_10_1128_aem_01277_22
crossref_primary_10_1016_j_mimet_2022_106495
Cites_doi 10.1128/IAI.00654-13
10.1186/s12866-018-1219-3
10.1093/glycob/cwv087
10.1128/JB.178.5.1310-1319.1996
10.1016/j.jmb.2009.10.003
10.1099/13500872-142-2-315
10.1126/science.322276
10.1038/nature01830
10.1128/JB.185.12.3567-3574.2003
10.1111/j.1742-4658.2008.06589.x
10.1126/science.277.5331.1453
10.1128/JB.175.17.5395-5402.1993
10.1186/s12866-016-0667-x
10.1126/science.1155307
10.1128/JB.01172-10
10.1128/JB.186.13.4315-4325.2004
10.1099/mic.0.28735-0
10.1128/AEM.02006-10
10.1111/j.1365-2958.2006.05081.x
10.1074/jbc.M114.562603
10.1126/science.1215584
10.1128/JB.00327-18
10.1371/journal.pone.0040592
10.1099/00221287-139-1-21
10.1128/IAI.69.5.3021-3030.2001
10.1016/S0021-9258(18)38234-6
10.1128/JB.181.1.153-160.1999
10.1074/jbc.M114.552000
10.1128/JB.178.17.5188-5198.1996
10.1529/biophysj.106.093443
10.1038/35074106
10.1002/j.1460-2075.1991.tb07736.x
10.1128/JB.155.1.74-81.1983
10.1038/s41467-018-07802-w
10.1038/ni1011
10.1128/JB.182.17.5001-5004.2000
10.1126/science.aav0748
10.1016/j.pmpp.2009.08.001
10.1128/AEM.03594-14
10.1128/JB.186.20.6721-6727.2004
10.1093/genetics/41.5.743
10.1084/jem.20061400
ContentType Journal Article
DBID NPM
AAYXX
CITATION
7X8
DOI 10.1099/mic.0.001020
DatabaseName PubMed
CrossRef
MEDLINE - Academic
DatabaseTitle PubMed
CrossRef
MEDLINE - Academic
DatabaseTitleList PubMed
CrossRef
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 1465-2080
ExternalDocumentID 10_1099_mic_0_001020
33502302
Genre Research Support, Non-U.S. Gov't
Journal Article
GroupedDBID ---
-DZ
-~X
.55
.GJ
123
186
2WC
3O-
4.4
53G
5RE
ABEFU
ABPPZ
ABTAH
ACNCT
ADCDP
ADIYS
AETEA
AFDAS
AFFNX
AFMIJ
AGCDD
AJKYU
ALMA_UNASSIGNED_HOLDINGS
C1A
CS3
DIK
E3Z
EBS
EJD
F5P
G8K
GX1
HF~
H~9
K-O
L7B
MVM
NPM
P0W
P2P
RGM
RHF
RPM
S10
TAE
UQL
W8F
WH7
WOQ
X7M
Y6R
YR2
ZCG
ZGI
ZXP
ZY4
~02
~KM
AAYXX
CITATION
H13
7X8
ID FETCH-LOGICAL-c395t-ffa47db85610a8e328b84d9776c9c6e86a77dfa557fda7c6bdc95015ce4299933
ISSN 1350-0872
IngestDate Fri Jun 28 06:10:49 EDT 2024
Fri Aug 23 00:23:45 EDT 2024
Thu May 23 23:38:39 EDT 2024
IsDoiOpenAccess false
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 3
Keywords flagella
lactobacilli
motility
flagellin
Ligilactobacillus agilis
Language English
LinkModel OpenURL
MergedId FETCHMERGED-LOGICAL-c395t-ffa47db85610a8e328b84d9776c9c6e86a77dfa557fda7c6bdc95015ce4299933
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ORCID 0000-0002-4164-5361
OpenAccessLink https://doi.org/10.1099/mic.0.001020
PMID 33502302
PQID 2481668134
PQPubID 23479
ParticipantIDs proquest_miscellaneous_2481668134
crossref_primary_10_1099_mic_0_001020
pubmed_primary_33502302
PublicationCentury 2000
PublicationDate 2021-03-00
PublicationDateYYYYMMDD 2021-03-01
PublicationDate_xml – month: 03
  year: 2021
  text: 2021-03-00
PublicationDecade 2020
PublicationPlace England
PublicationPlace_xml – name: England
PublicationTitle Microbiology (Society for General Microbiology)
PublicationTitleAlternate Microbiology (Reading)
PublicationYear 2021
References R41
R21
R43
R20
R42
R23
R22
R44
R25
R24
R27
R26
R29
R28
R1
R2
R3
R5
R6
R7
R8
R9
Deakin (R17) 1995; 69
Aizawa (R4) 2014
R30
R10
R32
R31
R12
R34
R11
R33
R14
R36
Schirm (R40) 2004; 186
R13
R35
R16
R38
R15
R37
R18
R39
R19
References_xml – ident: R20
  doi: 10.1128/IAI.00654-13
– ident: R29
  doi: 10.1186/s12866-018-1219-3
– ident: R41
  doi: 10.1093/glycob/cwv087
– ident: R21
  doi: 10.1128/JB.178.5.1310-1319.1996
– ident: R35
  doi: 10.1016/j.jmb.2009.10.003
– ident: R15
  doi: 10.1099/13500872-142-2-315
– ident: R12
  doi: 10.1126/science.322276
– ident: R3
  doi: 10.1038/nature01830
– ident: R8
  doi: 10.1128/JB.185.12.3567-3574.2003
– ident: R42
  doi: 10.1111/j.1742-4658.2008.06589.x
– ident: R5
  doi: 10.1126/science.277.5331.1453
– ident: R7
  doi: 10.1128/JB.175.17.5395-5402.1993
– ident: R28
  doi: 10.1186/s12866-016-0667-x
– volume-title: The Flagellar World: Electron Microscopic Images of Bacterial Flagella and Related Surface Structures
  year: 2014
  ident: R4
  contributor:
    fullname: Aizawa
– volume: 69
  start-page: 219
  year: 1995
  ident: R17
  article-title: Agrobacterium tumefaciens possesses a fourth flagellin gene located in a large gene cluster concerned with flagellar structure, assembly and motility
  publication-title: J Agric Chem Soiety Japan
  contributor:
    fullname: Deakin
– ident: R1
  doi: 10.1126/science.1155307
– ident: R13
  doi: 10.1128/JB.01172-10
– ident: R24
  doi: 10.1128/JB.186.13.4315-4325.2004
– ident: R39
  doi: 10.1099/mic.0.28735-0
– ident: R30
  doi: 10.1128/AEM.02006-10
– ident: R34
  doi: 10.1111/j.1365-2958.2006.05081.x
– ident: R38
  doi: 10.1074/jbc.M114.562603
– ident: R33
  doi: 10.1126/science.1215584
– ident: R18
  doi: 10.1128/JB.00327-18
– ident: R27
  doi: 10.1371/journal.pone.0040592
– ident: R22
  doi: 10.1099/00221287-139-1-21
– ident: R9
  doi: 10.1128/IAI.69.5.3021-3030.2001
– ident: R16
  doi: 10.1016/S0021-9258(18)38234-6
– ident: R6
  doi: 10.1128/JB.181.1.153-160.1999
– ident: R23
  doi: 10.1074/jbc.M114.552000
– ident: R19
  doi: 10.1128/JB.178.17.5188-5198.1996
– ident: R2
  doi: 10.1529/biophysj.106.093443
– ident: R37
  doi: 10.1038/35074106
– ident: R25
  doi: 10.1002/j.1460-2075.1991.tb07736.x
– ident: R10
  doi: 10.1128/JB.155.1.74-81.1983
– ident: R31
  doi: 10.1038/s41467-018-07802-w
– ident: R32
  doi: 10.1038/ni1011
– ident: R14
  doi: 10.1128/JB.182.17.5001-5004.2000
– ident: R43
  doi: 10.1126/science.aav0748
– ident: R44
  doi: 10.1016/j.pmpp.2009.08.001
– ident: R26
  doi: 10.1128/AEM.03594-14
– volume: 186
  start-page: 6721
  year: 2004
  ident: R40
  article-title: Flagellin from Listeria monocytogenes is glycosylated with β -O-Linked N flagellin from Listeria monocytogenes is glycosylated with
  publication-title: J Bacteriol
  doi: 10.1128/JB.186.20.6721-6727.2004
  contributor:
    fullname: Schirm
– ident: R11
  doi: 10.1093/genetics/41.5.743
– ident: R36
  doi: 10.1084/jem.20061400
SSID ssj0014601
Score 2.3938882
Snippet Many flagellated bacteria possess multiple flagellins, but the roles and the compositions of each flagellin are diverse and poorly understood. In BKN88, there...
Many flagellated bacteria possess multiple flagellins, but the roles and the compositions of each flagellin are diverse and poorly understood. In...
SourceID proquest
crossref
pubmed
SourceType Aggregation Database
Index Database
Title Ligilactobacillus agilis BKN88 possesses thermo-/acid-stable heteropolymeric flagellar filaments
URI https://www.ncbi.nlm.nih.gov/pubmed/33502302
https://search.proquest.com/docview/2481668134
Volume 167
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwELaWIiQuiDdbHgoSnFbZbuPYcY48igqFXmil3oLjxzaQTapuctj9C_xpZuIkG8oiFfYQrZzYiTxfxt9kxjOEvKIxozZk0kfzwQ8NF37K48hnJqZCYx1V2wTIHvPD0_DTGTsbjX4OopbqKp2q9dZ9Jf8jVWgDueIu2X-QbD8oNMB_kC8cQcJwvJaMP2fzLMeCOalUWZ7Xy4mEhmw5eXt0LMTkomw8upjEASSzKH3UyCrTPjBC3DB1jqEwWCRh5QLqbQ7KJcewVAvDLrosTx13_ZINkjYBMR0GfLbZqyfDawYfGQ7mWHPFafOyKjeeqHXtymZ_Pa-LldyooB-lY7WwDnzPevjOs0V7dbauizKth98sgkHQVqtmKcMoOle0Z2pcW4jxdjNX16nXza5WRwtCulXnA8eF6VtkaopRekCYZpu1rfPnX1ny-kBE54KPE-idYJ5U7H2D3AyimKEl__7jUe-SCvnMWe_to7e7KKD33vDev_ObvxgtDXk5uUvutFaH98ZB6B4ZmeI-ueXqkK4ekG9_AMlzQPIaIHk9kLwWSHsDGHlXYOT1MPJ6GD0kpx8OTt4d-m3pDV_B21v51sow0qlAdi2FoYFIRajBVuAqVtwILqNIW8lYZLWMFE-1ihkwS2WQ38SUPiI7RVmYJ8STmOKO6X2teRziaW5SZu2MGvjNrBqT192EJRcuw0qyTSxj8rKbTWhfol9LFqasl0kQovNb7NNwTB67ae5HoiAusLKD3Wve5Sm5vQHsM7JTXdbmOdDOKn3RwOEXoZeF4Q
link.rule.ids 315,786,790,27957,27958
linkProvider Flying Publisher
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Ligilactobacillus+agilis+BKN88+possesses+thermo-%2Facid-stable+heteropolymeric+flagellar+filaments&rft.jtitle=Microbiology+%28Society+for+General+Microbiology%29&rft.au=Eguchi%2C+Naoto&rft.au=Suzuki%2C+Shunya&rft.au=Yokota%2C+Kenji&rft.au=Igimi%2C+Shizunobu&rft.date=2021-03-01&rft.issn=1350-0872&rft.eissn=1465-2080&rft.volume=167&rft.issue=3&rft_id=info:doi/10.1099%2Fmic.0.001020&rft.externalDBID=n%2Fa&rft.externalDocID=10_1099_mic_0_001020
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1350-0872&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1350-0872&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1350-0872&client=summon