Taming the symbiont for coexistence: a host PGRP neutralizes a bacterial symbiont toxin
Summary In horizontally transmitted mutualisms between marine animals and their bacterial partners, the host environment promotes the initial colonization by specific symbionts that it harvests from the surrounding bacterioplankton. Subsequently, the host must develop long‐term tolerance to immunoge...
Saved in:
Published in | Environmental microbiology Vol. 12; no. 8; pp. 2190 - 2203 |
---|---|
Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
Oxford, UK
Blackwell Publishing Ltd
01.08.2010
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Summary
In horizontally transmitted mutualisms between marine animals and their bacterial partners, the host environment promotes the initial colonization by specific symbionts that it harvests from the surrounding bacterioplankton. Subsequently, the host must develop long‐term tolerance to immunogenic bacterial molecules, such as peptidoglycan and lipopolysaccaride derivatives. We describe the characterization of the activity of a host peptidoglycan recognition protein (EsPGRP2) during establishment of the symbiosis between the squid Euprymna scolopes and its luminous bacterial symbiont Vibrio fischeri. Using confocal immunocytochemistry, we localized EsPGRP2 to all epithelial surfaces of the animal, and determined that it is exported in association with mucus shedding. Most notably, EsPGRP2 was released by the crypt epithelia into the extracellular spaces housing the symbionts. This translocation occurred only after the symbionts had triggered host morphogenesis, a process that is induced by exposure to the peptidoglycan monomer tracheal cytotoxin (TCT), a bacterial ‘toxin’ that is constitutively exported by V. fischeri. Enzymatic analyses demonstrated that, like many described PGRPs, EsPGRP2 has a TCT‐degrading amidase activity. The timing of EsPGRP2 export into the crypts provides evidence that the host does not export this protein until after TCT induces morphogenesis, and thereafter EsPGRP2 is constantly present in the crypts ameliorating the effects of V. fischeri TCT. |
---|---|
AbstractList | In horizontally transmitted mutualisms between marine animals and their bacterial partners, the host environment promotes the initial colonization by specific symbionts that it harvests from the surrounding bacterioplankton. Subsequently, the host must develop long-term tolerance to immunogenic bacterial molecules, such as peptidoglycan and lipopolysaccaride derivatives. We describe the characterization of the activity of a host peptidoglycan recognition protein (EsPGRP2) during establishment of the symbiosis between the squid Euprymna scolopes and its luminous bacterial symbiont Vibrio fischeri. Using confocal immunocytochemistry, we localized EsPGRP2 to all epithelial surfaces of the animal, and determined that it is exported in association with mucus shedding. Most notably, EsPGRP2 was released by the crypt epithelia into the extracellular spaces housing the symbionts. This translocation occurred only after the symbionts had triggered host morphogenesis, a process that is induced by exposure to the peptidoglycan monomer tracheal cytotoxin (TCT), a bacterial 'toxin' that is constitutively exported by V. fischeri. Enzymatic analyses demonstrated that, like many described PGRPs, EsPGRP2 has a TCT-degrading amidase activity. The timing of EsPGRP2 export into the crypts provides evidence that the host does not export this protein until after TCT induces morphogenesis, and thereafter EsPGRP2 is constantly present in the crypts ameliorating the effects of V. fischeri TCT. Summary In horizontally transmitted mutualisms between marine animals and their bacterial partners, the host environment promotes the initial colonization by specific symbionts that it harvests from the surrounding bacterioplankton. Subsequently, the host must develop long‐term tolerance to immunogenic bacterial molecules, such as peptidoglycan and lipopolysaccaride derivatives. We describe the characterization of the activity of a host peptidoglycan recognition protein (EsPGRP2) during establishment of the symbiosis between the squid Euprymna scolopes and its luminous bacterial symbiont Vibrio fischeri . Using confocal immunocytochemistry, we localized EsPGRP2 to all epithelial surfaces of the animal, and determined that it is exported in association with mucus shedding. Most notably, EsPGRP2 was released by the crypt epithelia into the extracellular spaces housing the symbionts. This translocation occurred only after the symbionts had triggered host morphogenesis, a process that is induced by exposure to the peptidoglycan monomer tracheal cytotoxin (TCT), a bacterial ‘toxin’ that is constitutively exported by V. fischeri . Enzymatic analyses demonstrated that, like many described PGRPs, EsPGRP2 has a TCT‐degrading amidase activity. The timing of EsPGRP2 export into the crypts provides evidence that the host does not export this protein until after TCT induces morphogenesis, and thereafter EsPGRP2 is constantly present in the crypts ameliorating the effects of V. fischeri TCT. In horizontally-transmitted mutualisms between marine animals and their bacterial partners, the host environment promotes the initial colonization by specific symbionts that it harvests from the surrounding bacterioplankton. Subsequently, the host must develop long-term tolerance to immunogenic bacterial molecules, such as peptidoglycan and lipopolysaccaride derivatives. We describe the characterization of the activity of a host peptidoglycan-recognition protein (EsPGRP2) during establishment of the symbiosis between the squid Euprymna scolopes and its luminous bacterial symbiont Vibrio fischeri . Using confocal immunocytochemistry, we localized EsPGRP2 to all epithelial surfaces of the animal, and determined that it is exported in association with mucus shedding. Most notably, EsPGRP2 was released by the crypt epithelia into the extracellular spaces housing the symbionts. This translocation occurred only after the symbionts had triggered host morphogenesis, a process that is induced by exposure to the peptidoglycan monomer (TCT), a bacterial ‘toxin’ that is constitutively exported by V. fischeri . Enzymatic analyses demonstrated that, like many described PGRPs, EsPGRP2 has a TCT-degrading amidase activity. The timing of EsPGRP2 export into the crypts provides evidence that the host does not export this protein until after TCT induces morphogenesis, and thereafter EsPGRP2 is constantly present in the crypts ameliorating the effects of V. fischeri TCT. Summary In horizontally transmitted mutualisms between marine animals and their bacterial partners, the host environment promotes the initial colonization by specific symbionts that it harvests from the surrounding bacterioplankton. Subsequently, the host must develop long‐term tolerance to immunogenic bacterial molecules, such as peptidoglycan and lipopolysaccaride derivatives. We describe the characterization of the activity of a host peptidoglycan recognition protein (EsPGRP2) during establishment of the symbiosis between the squid Euprymna scolopes and its luminous bacterial symbiont Vibrio fischeri. Using confocal immunocytochemistry, we localized EsPGRP2 to all epithelial surfaces of the animal, and determined that it is exported in association with mucus shedding. Most notably, EsPGRP2 was released by the crypt epithelia into the extracellular spaces housing the symbionts. This translocation occurred only after the symbionts had triggered host morphogenesis, a process that is induced by exposure to the peptidoglycan monomer tracheal cytotoxin (TCT), a bacterial ‘toxin’ that is constitutively exported by V. fischeri. Enzymatic analyses demonstrated that, like many described PGRPs, EsPGRP2 has a TCT‐degrading amidase activity. The timing of EsPGRP2 export into the crypts provides evidence that the host does not export this protein until after TCT induces morphogenesis, and thereafter EsPGRP2 is constantly present in the crypts ameliorating the effects of V. fischeri TCT. SummaryIn horizontally transmitted mutualisms between marine animals and their bacterial partners, the host environment promotes the initial colonization by specific symbionts that it harvests from the surrounding bacterioplankton. Subsequently, the host must develop long-term tolerance to immunogenic bacterial molecules, such as peptidoglycan and lipopolysaccaride derivatives. We describe the characterization of the activity of a host peptidoglycan recognition protein (EsPGRP2) during establishment of the symbiosis between the squid Euprymna scolopes and its luminous bacterial symbiont Vibrio fischeri. Using confocal immunocytochemistry, we localized EsPGRP2 to all epithelial surfaces of the animal, and determined that it is exported in association with mucus shedding. Most notably, EsPGRP2 was released by the crypt epithelia into the extracellular spaces housing the symbionts. This translocation occurred only after the symbionts had triggered host morphogenesis, a process that is induced by exposure to the peptidoglycan monomer tracheal cytotoxin (TCT), a bacterial 'toxin' that is constitutively exported by V. fischeri. Enzymatic analyses demonstrated that, like many described PGRPs, EsPGRP2 has a TCT-degrading amidase activity. The timing of EsPGRP2 export into the crypts provides evidence that the host does not export this protein until after TCT induces morphogenesis, and thereafter EsPGRP2 is constantly present in the crypts ameliorating the effects of V. fischeri TCT. |
Author | Wier, Andrew M. Goldman, William E. Silverman, Neal McFall-Ngai, Margaret J. Troll, Joshua V. Pacquette, Nicholas Bent, Eric H. |
AuthorAffiliation | 1 Department of Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, WI 53706, USA 2 Division of Infectious Diseases, Department of Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA 3 Department of Microbiology and Immunology, University of North Carolina, Chapel Hill, NC 27599, USA |
AuthorAffiliation_xml | – name: 1 Department of Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, WI 53706, USA – name: 2 Division of Infectious Diseases, Department of Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA – name: 3 Department of Microbiology and Immunology, University of North Carolina, Chapel Hill, NC 27599, USA |
Author_xml | – sequence: 1 givenname: Joshua V. surname: Troll fullname: Troll, Joshua V. organization: Department of Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, WI 53706, USA – sequence: 2 givenname: Eric H. surname: Bent fullname: Bent, Eric H. organization: Department of Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, WI 53706, USA – sequence: 3 givenname: Nicholas surname: Pacquette fullname: Pacquette, Nicholas organization: Division of Infectious Diseases, Department of Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA – sequence: 4 givenname: Andrew M. surname: Wier fullname: Wier, Andrew M. organization: Department of Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, WI 53706, USA – sequence: 5 givenname: William E. surname: Goldman fullname: Goldman, William E. organization: Department of Microbiology and Immunology, University of North Carolina, Chapel Hill, NC 27599, USA – sequence: 6 givenname: Neal surname: Silverman fullname: Silverman, Neal organization: Division of Infectious Diseases, Department of Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA – sequence: 7 givenname: Margaret J. surname: McFall-Ngai fullname: McFall-Ngai, Margaret J. email: mjmcfallngai@wisc.edu organization: Department of Medical Microbiology and Immunology, University of Wisconsin-Madison, Madison, WI 53706, USA |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21966913$$D View this record in MEDLINE/PubMed |
BookMark | eNqNUcuO1DAQtNAi9gG_gHLjlOBHXkYCCa2WYaUFRqtBc2w5ns6Oh8Re7Axk-HocZglwwxe33FXV5a5zcmKdRUISRjMWz8tdxvKSp1xymnFKZUY54ywbH5GzuXEy14yfkvMQdpSySlT0CTnlTJalZOKMrFeqN_YuGbaYhEPfGGeHpHU-0Q5HEwa0Gl8lKtm6MCTLxe0ysbgfvOrMDwzxvVF6QG9U94c9uNHYp-Rxq7qAzx7uC_L53dXq8n1682lxffn2JtUllSxtCqVodMk5Q8GE0ErXWOdVwxitWo2iRSk2dUUlRU0x_r1o6o2UJWUMW1mKC_LmqHu_b3rcaLSTObj3plf-AE4Z-LdjzRbu3DfgdS15TqPAiwcB777uMQzQm6Cx65RFtw9QFXktSynziKyPSO1dCB7beQqjMMUCO5g2DtP2YYoFfsUCY6Q-_9vlTPydQwS8PgK-mw4P_y0MVx-upyry0yN_imyc-cp_gTJmXsD64wIEXRXL23UJufgJWUOtVA |
CitedBy_id | crossref_primary_10_1098_rstb_2023_0060 crossref_primary_10_1016_j_molimm_2013_06_019 crossref_primary_10_1038_ni_2635 crossref_primary_10_1126_science_1209728 crossref_primary_10_1128_mBio_00167_13 crossref_primary_10_1002_mbo3_858 crossref_primary_10_1021_jm100086u crossref_primary_10_1093_icb_icad087 crossref_primary_10_3389_fmicb_2016_01982 crossref_primary_10_1016_j_dci_2016_12_009 crossref_primary_10_1007_s13199_022_00855_y crossref_primary_10_1111_ede_12291 crossref_primary_10_3389_fmars_2022_1026742 crossref_primary_10_1098_rspb_2014_0504 crossref_primary_10_1128_mBio_00040_17 crossref_primary_10_1038_s41385_018_0010_y crossref_primary_10_1186_s12864_016_3293_y crossref_primary_10_1371_journal_pone_0119949 crossref_primary_10_1128_mSystems_00867_21 crossref_primary_10_1086_BBLv223n1p103 crossref_primary_10_1016_j_fsi_2019_08_022 crossref_primary_10_1091_mbc_E24_01_0044 crossref_primary_10_1016_j_fsi_2022_01_015 crossref_primary_10_1016_j_micinf_2015_08_016 crossref_primary_10_1016_j_chom_2013_07_006 crossref_primary_10_1038_nri3089 crossref_primary_10_3390_ijms231911062 crossref_primary_10_3389_fimmu_2020_01251 crossref_primary_10_1016_j_immuni_2019_08_003 crossref_primary_10_1186_s40168_023_01714_8 crossref_primary_10_1007_s13355_020_00680_z crossref_primary_10_1128_AEM_00890_15 crossref_primary_10_15741_revbio_11_e1521 crossref_primary_10_3389_fcell_2021_768783 crossref_primary_10_3389_fmicb_2019_00500 crossref_primary_10_1128_JB_00121_18 crossref_primary_10_1038_s41579_021_00567_y crossref_primary_10_1016_j_fsi_2015_02_036 crossref_primary_10_1038_srep46318 crossref_primary_10_1042_BST0391039 crossref_primary_10_1128_mSystems_00175_19 crossref_primary_10_1371_journal_pone_0025649 crossref_primary_10_1038_pr_2014_165 crossref_primary_10_1038_nrmicro2894 crossref_primary_10_1073_pnas_1821806116 crossref_primary_10_1074_mcp_M113_037259 crossref_primary_10_1111_1462_2920_12496 crossref_primary_10_1038_s41598_024_53477_3 crossref_primary_10_1111_1462_2920_14392 crossref_primary_10_1016_j_immuni_2011_09_018 crossref_primary_10_1098_rspb_2017_0360 crossref_primary_10_3389_fmars_2022_825267 crossref_primary_10_1111_mec_12655 crossref_primary_10_1128_mBio_00093_12 crossref_primary_10_1128_mbio_01671_22 crossref_primary_10_1371_journal_pone_0038267 crossref_primary_10_1073_pnas_2016864117 crossref_primary_10_1016_j_isci_2022_104357 crossref_primary_10_1128_AEM_01800_16 crossref_primary_10_1016_j_smim_2011_11_006 crossref_primary_10_1111_1462_2920_12179 crossref_primary_10_1128_mBio_00853_20 |
Cites_doi | 10.1016/j.bbrc.2006.09.139 10.1016/S1074-7613(04)00104-9 10.2307/1542815 10.1016/S0006-291X(03)01096-9 10.1128/AEM.60.5.1565-1571.1994 10.1016/j.bbrc.2009.01.140 10.1128/AEM.68.10.5113-5122.2002 10.1111/j.1462-5822.2006.00726.x 10.1128/JB.01547-08 10.1126/science.1132913 10.1128/MMBR.68.2.280-300.2004 10.1111/j.1462-5822.2009.01315.x 10.1007/BF00250277 10.1073/pnas.95.4.1818 10.1007/BF00193435 10.1242/dev.120.7.1719 10.1074/jbc.M307758200 10.1002/(SICI)1097-4644(19990315)72:4<445::AID-JCB1>3.0.CO;2-P 10.1128/IAI.66.2.777-785.1998 10.1111/j.0105-2896.2004.0120.x 10.1073/pnas.97.25.13772 10.1128/AEM.72.1.802-810.2006 10.1017/S0029665100000197 10.1016/j.dci.2006.11.006 10.1111/j.1462-5822.2004.00429.x 10.1126/science.1102218 10.1126/science.1962208 10.1182/blood-2005-02-0530 10.1038/nature734 10.1073/pnas.97.18.10231 10.1007/s004270050185 10.1074/jbc.M208900200 10.2307/1542152 10.1128/AEM.71.11.6934-6946.2005 10.1073/pnas.90.6.2365 10.1042/BST0351496 10.1038/414756a 10.1016/j.molimm.2003.10.011 10.1038/nrmicro957 10.1038/nrmicro1486 10.1101/gad.817800 10.1371/journal.ppat.0020014 10.1093/infdis/149.3.378 10.2307/1542448 10.1016/j.micinf.2009.03.004 10.1111/j.1365-2672.2007.03366.x 10.1006/dbio.2000.9868 10.1111/j.1365-2958.1995.tb02434.x 10.1074/jbc.M506385200 10.1016/j.immuni.2006.02.012 10.1128/JB.182.16.4578-4586.2000 |
ContentType | Journal Article |
Copyright | 2009 Society for Applied Microbiology and Blackwell Publishing Ltd 2009 Society for Applied Microbiology and Blackwell Publishing Ltd. |
Copyright_xml | – notice: 2009 Society for Applied Microbiology and Blackwell Publishing Ltd – notice: 2009 Society for Applied Microbiology and Blackwell Publishing Ltd. |
DBID | BSCLL CGR CUY CVF ECM EIF NPM AAYXX CITATION 7QL 7T7 7TN 8FD C1K F1W FR3 H95 L.G P64 5PM |
DOI | 10.1111/j.1462-2920.2009.02121.x |
DatabaseName | Istex Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Bacteriology Abstracts (Microbiology B) Industrial and Applied Microbiology Abstracts (Microbiology A) Oceanic Abstracts Technology Research Database Environmental Sciences and Pollution Management ASFA: Aquatic Sciences and Fisheries Abstracts Engineering Research Database Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources Aquatic Science & Fisheries Abstracts (ASFA) Professional Biotechnology and BioEngineering Abstracts PubMed Central (Full Participant titles) |
DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef Aquatic Science & Fisheries Abstracts (ASFA) Professional Oceanic Abstracts Technology Research Database Bacteriology Abstracts (Microbiology B) ASFA: Aquatic Sciences and Fisheries Abstracts Engineering Research Database Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources Industrial and Applied Microbiology Abstracts (Microbiology A) Biotechnology and BioEngineering Abstracts Environmental Sciences and Pollution Management |
DatabaseTitleList | MEDLINE CrossRef Aquatic Science & Fisheries Abstracts (ASFA) Professional |
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 – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Biology |
EISSN | 1462-2920 |
EndPage | 2203 |
ExternalDocumentID | 10_1111_j_1462_2920_2009_02121_x 21966913 EMI2121 ark_67375_WNG_30T5PRW6_4 |
Genre | article Journal Article Research Support, N.I.H., Extramural |
GrantInformation_xml | – fundername: NIAID NIH HHS grantid: R01 AI060025 – fundername: NIAID NIH HHS grantid: R37 AI050661 – fundername: NIAID NIH HHS grantid: T32 AI055397 – fundername: NIAID NIH HHS grantid: R01-AI50661 – fundername: NIAID NIH HHS grantid: AI55397 – fundername: NIAID NIH HHS grantid: R01 AI050661 – fundername: NIAID NIH HHS grantid: R01 AI050661-08 – fundername: NCRR NIH HHS grantid: RR R01-12294 |
GroupedDBID | --- .3N .GA .Y3 05W 0R~ 10A 1OC 29G 31~ 33P 36B 3SF 4.4 50Y 50Z 51W 51X 52M 52N 52O 52P 52S 52T 52U 52W 52X 53G 5GY 5HH 5LA 5VS 66C 702 7PT 8-0 8-1 8-3 8-4 8-5 8UM 930 A03 AAESR AAEVG AAHHS AAJUZ AANLZ AAONW AASGY AAXRX AAZKR ABCQN ABCUV ABCVL ABEML ABHUG ABJNI ABPTK ABPVW ABWRO ACAHQ ACBWZ ACCFJ ACCZN ACFBH ACGFO ACGFS ACPOU ACPRK ACSCC ACXBN ACXME ACXQS ADAWD ADBBV ADDAD ADEOM ADIZJ ADKYN ADMGS ADOZA ADXAS ADZMN ADZOD AEEZP AEGXH AEIGN AEIMD AENEX AEQDE AEUQT AEUYR AFBPY AFEBI AFFPM AFGKR AFPWT AFRAH AFVGU AFZJQ AGJLS AHBTC AIAGR AIURR AIWBW AJBDE AJXKR ALAGY ALMA_UNASSIGNED_HOLDINGS ALUQN AMBMR AMYDB ASPBG ATUGU AUFTA AVWKF AZBYB AZFZN AZVAB BAFTC BDRZF BFHJK BHBCM BMNLL BMXJE BNHUX BROTX BRXPI BSCLL BY8 C45 CAG COF CS3 D-E D-F DCZOG DPXWK DR2 DRFUL DRSTM DU5 EBS ECGQY EJD ESX F00 F01 F04 F5P FEDTE G-S G.N GODZA H.T H.X HF~ HVGLF HZI HZ~ IHE IX1 J0M K48 LATKE LC2 LC3 LEEKS LH4 LITHE LOXES LP6 LP7 LUTES LW6 LYRES MEWTI MK4 MRFUL MRSTM MSFUL MSSTM MXFUL MXSTM N04 N05 N9A NF~ O66 O9- OBS OVD P2P P2W P2X P4D Q.N Q11 QB0 R.K ROL RX1 SUPJJ TEORI UB1 V8K W8V W99 WBKPD WIH WIK WNSPC WOHZO WQJ WRC WXSBR WYISQ XFK XG1 XIH YUY ZZTAW ~02 ~IA ~KM ~WT AAHBH AITYG HGLYW OIG CGR CUY CVF ECM EIF NPM AAYXX CITATION 7QL 7T7 7TN 8FD C1K F1W FR3 H95 L.G P64 5PM |
ID | FETCH-LOGICAL-c6091-b5aa0462221e3133cac8e847b1107fce3fe93d87090ec0e1115b8d996011ef963 |
IEDL.DBID | DR2 |
ISSN | 1462-2912 |
IngestDate | Tue Sep 17 20:51:09 EDT 2024 Fri Aug 16 01:11:30 EDT 2024 Fri Aug 23 01:46:23 EDT 2024 Wed Oct 23 09:41:55 EDT 2024 Sat Aug 24 01:11:26 EDT 2024 Wed Jan 17 05:01:53 EST 2024 |
IsDoiOpenAccess | false |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 8 |
Language | English |
License | 2009 Society for Applied Microbiology and Blackwell Publishing Ltd. |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c6091-b5aa0462221e3133cac8e847b1107fce3fe93d87090ec0e1115b8d996011ef963 |
Notes | istex:3F7CA3DD9392B1B2EE923BAD542A23F490DD77D9 ArticleID:EMI2121 ark:/67375/WNG-30T5PRW6-4 Present address: Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Current address: Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA |
OpenAccessLink | https://onlinelibrary.wiley.com/doi/pdfdirect/10.1111/j.1462-2920.2009.02121.x |
PMID | 21966913 |
PQID | 754896994 |
PQPubID | 23462 |
PageCount | 14 |
ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_2889240 proquest_miscellaneous_754896994 crossref_primary_10_1111_j_1462_2920_2009_02121_x pubmed_primary_21966913 wiley_primary_10_1111_j_1462_2920_2009_02121_x_EMI2121 istex_primary_ark_67375_WNG_30T5PRW6_4 |
PublicationCentury | 2000 |
PublicationDate | August 2010 |
PublicationDateYYYYMMDD | 2010-08-01 |
PublicationDate_xml | – month: 08 year: 2010 text: August 2010 |
PublicationDecade | 2010 |
PublicationPlace | Oxford, UK |
PublicationPlace_xml | – name: Oxford, UK – name: England |
PublicationTitle | Environmental microbiology |
PublicationTitleAlternate | Environ Microbiol |
PublicationYear | 2010 |
Publisher | Blackwell Publishing Ltd |
Publisher_xml | – name: Blackwell Publishing Ltd |
References | Koropatnick, T.A., Engle, J.T., Apicella, M.A., Stabb, E.V., Goldman, W.E., and McFall-Ngai, M.J. (2004) Microbial factor-mediated development in a host-bacterial mutualism. Science 306: 1186-1188. Luker, K.E., Collier, J.L., Kolodziej, E.W., Marshall, G.R., and Goldman, W.E. (1993) Bordetella pertussis tracheal cytotoxin and other muramyl peptides: distinct structure-activity relationships for respiratory epithelial cytopathology. Proc Natl Acad Sci USA 90: 2365-2369. Kelly, D., and Coutts, A.G. (2000) Early nutrition and the development of immune function in the neonate. Proc Nutr Soc 59: 177-185. Ruby, E.G., and Asato, L.M. (1993) Growth and flagellation of Vibrio fischeri during initiation of the sepiolid squid light organ symbiosis. Arch Microbiol 159: 160-167. Werner, T., Liu, G., Kang, D., Ekengren, S., Steiner, H., and Hultmark, D. (2000) A family of peptidoglycan recognition proteins in the fruit fly Drosophila melanogaster. Proc Natl Acad Sci USA 97: 13772-13777. Montgomery, M.K., and McFall-Ngai, M. (1994) Bacterial symbionts induce host organ morphogenesis during early postembryonic development of the squid Euprymna scolopes. Development 120: 1719-1729. McFall-Ngai, M.J., and Ruby, E.G. (1991) Symbiont recognition and subsequent morphogenesis as early events in an animal-bacterial mutualism. Science 254: 1491-1494. Nyholm, S.V., and McFall-Ngai, M.J. (1998) Sampling the light-organ microenvironment of Euprymna scolopes: description of a population of host cells in association with the bacterial symbiont Vibrio fischeri. Biol Bull 195: 89-97. Lamarcq, L.H., and McFall-Ngai, M.J. (1998) Induction of a gradual, reversible morphogenesis of its host's epithelial brush border by Vibrio fischeri. Infect Immun 66: 777-785. Adin, D.M., Engle, J.T., Goldman, W.E., McFall-Ngai, M.J., and Stabb, E.V. (2008) Mutations in ampG and lytic transglycosylase genes affect the net release of peptidoglycan monomers from Vibrio fischeri. J Bacteriol 191: 2012-2022. Gottar, M., Gobert, V., Michel, T., Belvin, M., Duyk, G., Hoffmann, J.A., et al. (2002) The Drosophila immune response against Gram-negative bacteria is mediated by a peptidoglycan recognition protein. Nature 416: 640-644. Aggrawal, K., and Silverman, N. (2007) Peptidoglycan recognition in Drosophila. Biochem Soc Trans 35: 1496-1500. Mellroth, P., Karlsson, J., and Steiner, H. (2003) A scavenger function for a Drosophila peptidoglycan recognition protein. J Biol Chem 278: 7059-7064. Silverman, N., Zhou, R., Stoven, S., Pandey, N., Hultmark, D., and Maniatis, T. (2000) A Drosophila IkappaB kinase complex required for Relish cleavage and antibacterial immunity. Genes Dev 14: 2461-2471. Dziarski, R., and Gupta, D. (2006) Mammalian PGRPs: novel antibacterial proteins. Cell Microbiol 8: 1059-1069. Michel, T., Reichhart, J.M., Hoffmann, J.A., and Royet, J. (2001) Drosophila Toll is activated by Gram-positive bacteria through a circulating peptidoglycan recognition protein. Nature 414: 756-759. Mellroth, P., and Steiner, H. (2006) PGRP-SB1: an N-acetylmuramoyl l-alanine amidase with antibacterial activity. Biochem Biophys Res Commun 350: 994-999. Wang, Z.M., Li, X., Cocklin, R.R., Wang, M., Fukase, K., Inamura, S., et al. (2003) Human peptidoglycan recognition protein-L is an N-acetylmuramoyl-L-alanine amidase. J Biol Chem 278: 49044-49052. Boettcher, K.J., Ruby, E.G., and McFall-Ngai, M.J. (1996) Bioluminescence in the symbiotic squid Euprymna scolopes is controlled by a daily biological rhythm. J Comp Physiol A Neuroethol Sens Neural Behav Physiol 179: 65-73. Doino, J.A., and McFall-Ngai, M.J. (1995) A transient exposure to symbiosis-competent bacteria induces light organ morphogenesis in the host squid. Biol Bull 189: 347-355. Lützner, N., Pätzold, B., Zoll, S., Stehle, T., and Kalbacher, H. (2009) Development of a novel fluorescent substrate for Autolysin E, a bacterial type II amidase. Biochemical Biophysical Res Comms 380: 554-558. Nyholm, S.V., Deplancke, B., Gaskins, H.R., Apicella, M.A., and McFall-Ngai, M.J. (2002) Roles of Vibrio fischeri and nonsymbiotic bacteria in the dynamics of mucus secretion during symbiont colonization of the Euprymna scolopes light organ. Appl Environ Microbiol 68: 5113-5122. Davidson, S.K., Koropatnick, T.A., Kossmehl, R., Sycuro, L., and McFall-Ngai, M.J. (2004) NO means 'yes' in the squid-vibrio symbiosis: nitric oxide (NO) during the initial stages of a beneficial association. Cell Microbiol 6: 1139-1151. Cooper, J.E. (2007) Early interactions between legumes and rhizobia: disclosing complexity in a molecular dialogue. J Appl Microbiology 103: 1355-1365. Steiner, H. (2004) Peptidoglycan recognition proteins: on and off switches for innate immunity. Immunol Rev 198: 83-96. Montgomery, M.K., and McFall-Ngai, M. (1993) Embryonic-development of the light organ of the sepiolid squid Euprymna-scolopes berry. Biological Bull 184: 296-308. Luker, K.E., Tyler, A.N., Marshall, G.R., and Goldman, W.E. (1995) Tracheal cytotoxin structural requirements for respiratory epithelial damage in pertussis. Mol Microbiol 16: 733-743. Charroux, B., Rival, T., Narbonne-Reveau, K., and Royet, J. (2009) Bacterial detection by Drosophila peptidoglycan recognition proteins. Microbes Infect 11: 631-636. Goodson, M.S., Kojadinovic, M., Troll, J.V., Scheetz, T.E., Casavant, T.L., Soares, M.B., and McFall-Ngai, M.J. (2005) Identifying components of the NF-κB pathway in the beneficial Euprymna scolopes-Vibrio fischeri light organ symbiosis. Appl Environ Microbiol 71: 6934-6946. Markert, S., Arndt, C., Felbeck, H., Becher, D., Sievert, S.M., Hugler, M., et al. (2007) Physiological proteomics of the uncultured endosymbiont of Riftia pachyptila. Science 315: 247-250. Troll, J.V., Adin, D.M., Wier, A.M., Paquette, N., Silverman, N., Goldman, W.E., et al. (2009) Peptidoglycan induces loss of a nuclear peptidoglycan recognition protein during host tissue development in a beneficial animal-bacterial symbiosis. Cell Microbiol 11: 1114-1127. Melly, M.A., McGee, Z.A., and Rosenthal, R.S. (1984) Ability of monomeric peptidoglycan fragments from Neisseria gonorrhoeae to damage human fallopian-tube mucosa. J Infect Dis 149: 378-386. Nyholm, S.V., and McFall-Ngai, M.J. (2004) The winnowing: establishing the squid-vibrio symbiosis. Nat Rev Microbiol 2: 632-642. Nyholm, S.V., Stabb, E.V., Ruby, E.G., and McFall-Ngai, M.J. (2000) Establishment of an animal-bacterial association: recruiting symbiotic vibrios from the environment. Proc Natl Acad Sci USA 97: 10231-10235. Dixon, M., and Webb, E.C. (1964) Enzymes. New York, NY, USA: Academic Press. Lee, K.H., and Ruby, E.G. (1994) Effect of the squid host on the abundance and distribution of symbiotic Vibrio fischeri in nature. Appl Environ Microbiol 60: 1565-1571. Bischoff, V., Vignal, C., Duvic, B., Boneca, I.G., Hoffmann, J.A., and Royet, J. (2006) Downregulation of the Drosophila immune response by peptidoglycan-recognition proteins SC1 and SC2. Plos Pathog 2: e14. Cho, J.H., Fraser, I.P., Fukase, K., Kusumoto, S., Fujimoto, Y., Stahl, G.L., and Ezekowitz, R.A. (2005) Human peptidoglycan recognition protein S is an effector of neutrophil-mediated innate immunity. Blood 106: 2551-2558. Graf, J., and Ruby, E.G. (1998) Host-derived amino acids support the proliferation of symbiotic bacteria. Proc Natl Acad Sci USA 95: 1818-1822. Zaidman-Remy, A., Herve, M., Poidevin, M., Pili-Floury, S., Kim, M.S., Blanot, D., et al. (2006) The Drosophila amidase PGRP-LB modulates the immune response to bacterial infection. Immunity 24: 463-473. Foster, J.S., Apicella, M.A., and McFall-Ngai, M.J. (2000) Vibrio fischeri lipopolysaccharide induces developmental apoptosis, but not complete morphogenesis, of the Euprymna scolopes symbiotic light organ. Dev Biol 226: 242-254. Dunn, A.K., Millikan, D.S., Adin, D.M., Bose, J.L., and Stabb, E.V. (2006) New rfp- and pES213-derived tools for analyzing symbiotic Vibrio fischeri reveal patterns of infection and lux expression in situ. Appl Environ Microbiol 72: 802-810. Visick, K.L., Foster, J., Doino, J., McFall-Ngai, M., and Ruby, E.G. (2000) Vibrio fischeri lux genes play an important role in colonization and development of the host light organ. J Bacteriol 182: 4578-4586. Gelius, E., Persson, C., Karlsson, J., and Steiner, H. (2003) A mammalian peptidoglycan recognition protein with N-acetylmuramoyl-L-alanine amidase activity. Biochem Biophys Res Commun 306: 988-994. Kumar, S., Roychowdhury, A., Ember, B., Wang, Q., Guan, R., Mariuzza, R.A., and Boons, G.J. (2005) Selective recognition of synthetic lysine and meso-diaminopimelic acid-type peptidoglycan fragments by human peptidoglycan recognition proteins Iα and S. J Biol Chem 280: 37005-37012. Coteur, G., Mellroth, P., De Lefortery, C., Gillan, D., Dubois, P., Communi, D., and Steiner, H. (2007) Peptidoglycan recognition proteins with amidase activity in early deuterostomes (Echinodermata). Dev Comp Immunol 31: 790-804. Small, A.L., and McFall-Ngai, M.J. (1999) Halide peroxidase in tissues that interact with bacteria in the host squid Euprymna scolopes. J Cell Biochem 72: 445-457. Kaneko, T., Goldman, W.E., Mellroth, P., Steiner, H., Fukase, K., Kusumoto, S., et al. (2004) Monomeric and polymeric gram-negative peptidoglycan but not purified LPS stimulate the Drosophila IMD pathway. Immunity 20: 637-649. Dziarski, R. (2004) Peptidoglycan recognition proteins (PGRPs). Mol Immunol 40: 877-886. Cloud-Hansen, K.A., Peterson, S.B., Stabb, E.V., Goldman, W.E., McFall-Ngai, M.J., and Handelsman, J. (2006) Breaching the great wall: peptidoglycan and microbial interactions. Nat Rev Microbiol 4: 710-716. Foster, J.S., and McFall-Ngai, M.J. (1998) Induction of apoptosis by cooperative bacteria in the morphogenesis of host epithelial tissues. Dev Genes E 208: 295-303. Gage, D.J. (2004) Infection and invasion of roots by symbiotic, nitrogen-fixing rhizobia during nodulation of temperate legumes. Microbiol Mol Biol Rev 68: 280-300. 2007; 103 2008; 191 2004; 20 2006; 72 2004; 68 2004; 6 1971 2004; 2 2007; 31 2003; 278 1994; 60 2007; 35 1998; 195 2009; 11 2000; 14 2000; 59 2006; 24 2005; 106 2000; 97 1998; 208 2005; 71 1998; 95 1996; 179 2001; 414 2004; 40 1991; 254 1995; 16 2009; 380 1984; 149 2006; 350 2006; 8 1993; 184 2006; 4 1993; 90 2002; 416 2006; 2 2004; 306 1998; 66 2005; 280 2004; 198 2003; 306 2007; 315 2000; 226 1994; 120 2002; 68 2000; 182 1964 1995; 189 1999; 72 1993; 159 e_1_2_6_51_1 e_1_2_6_53_1 e_1_2_6_32_1 e_1_2_6_30_1 e_1_2_6_19_1 e_1_2_6_13_1 e_1_2_6_36_1 e_1_2_6_11_1 e_1_2_6_34_1 e_1_2_6_17_1 e_1_2_6_15_1 e_1_2_6_38_1 e_1_2_6_43_1 e_1_2_6_20_1 e_1_2_6_41_1 e_1_2_6_9_1 e_1_2_6_5_1 e_1_2_6_7_1 e_1_2_6_49_1 e_1_2_6_3_1 e_1_2_6_22_1 Dixon M. (e_1_2_6_12_1) 1964 e_1_2_6_28_1 e_1_2_6_45_1 e_1_2_6_26_1 e_1_2_6_47_1 e_1_2_6_52_1 e_1_2_6_54_1 e_1_2_6_10_1 e_1_2_6_31_1 e_1_2_6_50_1 e_1_2_6_14_1 e_1_2_6_35_1 e_1_2_6_33_1 e_1_2_6_18_1 e_1_2_6_39_1 e_1_2_6_16_1 e_1_2_6_37_1 e_1_2_6_42_1 e_1_2_6_21_1 e_1_2_6_40_1 e_1_2_6_8_1 e_1_2_6_4_1 e_1_2_6_6_1 Kaback H.R. (e_1_2_6_24_1) 1971 e_1_2_6_25_1 e_1_2_6_48_1 e_1_2_6_23_1 e_1_2_6_2_1 e_1_2_6_29_1 e_1_2_6_44_1 e_1_2_6_27_1 e_1_2_6_46_1 |
References_xml | – volume: 106 start-page: 2551 year: 2005 end-page: 2558 article-title: Human peptidoglycan recognition protein S is an effector of neutrophil‐mediated innate immunity publication-title: Blood – volume: 60 start-page: 1565 year: 1994 end-page: 1571 article-title: Effect of the squid host on the abundance and distribution of symbiotic in nature publication-title: Appl Environ Microbiol – volume: 198 start-page: 83 year: 2004 end-page: 96 article-title: Peptidoglycan recognition proteins: on and off switches for innate immunity publication-title: Immunol Rev – volume: 179 start-page: 65 year: 1996 end-page: 73 article-title: Bioluminescence in the symbiotic squid is controlled by a daily biological rhythm publication-title: J Comp Physiol A Neuroethol Sens Neural Behav Physiol – volume: 35 start-page: 1496 year: 2007 end-page: 1500 article-title: Peptidoglycan recognition in publication-title: Biochem Soc Trans – volume: 66 start-page: 777 year: 1998 end-page: 785 article-title: Induction of a gradual, reversible morphogenesis of its host's epithelial brush border by publication-title: Infect Immun – volume: 2 start-page: e14 year: 2006 article-title: Downregulation of the immune response by peptidoglycan‐recognition proteins SC1 and SC2 publication-title: Plos Pathog – volume: 414 start-page: 756 year: 2001 end-page: 759 article-title: Toll is activated by Gram‐positive bacteria through a circulating peptidoglycan recognition protein publication-title: Nature – volume: 72 start-page: 445 year: 1999 end-page: 457 article-title: Halide peroxidase in tissues that interact with bacteria in the host squid publication-title: J Cell Biochem – volume: 278 start-page: 7059 year: 2003 end-page: 7064 article-title: A scavenger function for a Drosophila peptidoglycan recognition protein publication-title: J Biol Chem – volume: 159 start-page: 160 year: 1993 end-page: 167 article-title: Growth and flagellation of during initiation of the sepiolid squid light organ symbiosis publication-title: Arch Microbiol – volume: 103 start-page: 1355 year: 2007 end-page: 1365 article-title: Early interactions between legumes and rhizobia: disclosing complexity in a molecular dialogue publication-title: J Appl Microbiology – volume: 31 start-page: 790 year: 2007 end-page: 804 article-title: Peptidoglycan recognition proteins with amidase activity in early deuterostomes (Echinodermata) publication-title: Dev Comp Immunol – volume: 20 start-page: 637 year: 2004 end-page: 649 article-title: Monomeric and polymeric gram‐negative peptidoglycan but not purified LPS stimulate the IMD pathway publication-title: Immunity – volume: 184 start-page: 296 year: 1993 end-page: 308 article-title: Embryonic‐development of the light organ of the sepiolid squid publication-title: Biological Bull – volume: 2 start-page: 632 year: 2004 end-page: 642 article-title: The winnowing: establishing the squid‐vibrio symbiosis publication-title: Nat Rev Microbiol – volume: 416 start-page: 640 year: 2002 end-page: 644 article-title: The immune response against Gram‐negative bacteria is mediated by a peptidoglycan recognition protein publication-title: Nature – volume: 6 start-page: 1139 year: 2004 end-page: 1151 article-title: NO means ‘yes’ in the squid‐vibrio symbiosis: nitric oxide (NO) during the initial stages of a beneficial association publication-title: Cell Microbiol – volume: 254 start-page: 1491 year: 1991 end-page: 1494 article-title: Symbiont recognition and subsequent morphogenesis as early events in an animal‐bacterial mutualism publication-title: Science – volume: 14 start-page: 2461 year: 2000 end-page: 2471 article-title: A IkappaB kinase complex required for Relish cleavage and antibacterial immunity publication-title: Genes Dev – volume: 24 start-page: 463 year: 2006 end-page: 473 article-title: The amidase PGRP‐LB modulates the immune response to bacterial infection publication-title: Immunity – volume: 306 start-page: 988 year: 2003 end-page: 994 article-title: A mammalian peptidoglycan recognition protein with ‐acetylmuramoyl‐L‐alanine amidase activity publication-title: Biochem Biophys Res Commun – volume: 71 start-page: 6934 year: 2005 end-page: 6946 article-title: Identifying components of the NF‐κB pathway in the beneficial light organ symbiosis publication-title: Appl Environ Microbiol – volume: 4 start-page: 710 year: 2006 end-page: 716 article-title: Breaching the great wall: peptidoglycan and microbial interactions publication-title: Nat Rev Microbiol – volume: 380 start-page: 554 year: 2009 end-page: 558 article-title: Development of a novel fluorescent substrate for Autolysin E, a bacterial type II amidase publication-title: Biochemical Biophysical Res Comms – volume: 11 start-page: 1114 year: 2009 end-page: 1127 article-title: Peptidoglycan induces loss of a nuclear peptidoglycan recognition protein during host tissue development in a beneficial animal‐bacterial symbiosis publication-title: Cell Microbiol – volume: 40 start-page: 877 year: 2004 end-page: 886 article-title: Peptidoglycan recognition proteins (PGRPs) publication-title: Mol Immunol – volume: 68 start-page: 5113 year: 2002 end-page: 5122 article-title: Roles of and nonsymbiotic bacteria in the dynamics of mucus secretion during symbiont colonization of the light organ publication-title: Appl Environ Microbiol – volume: 149 start-page: 378 year: 1984 end-page: 386 article-title: Ability of monomeric peptidoglycan fragments from to damage human fallopian‐tube mucosa publication-title: J Infect Dis – year: 1964 – volume: 97 start-page: 10231 year: 2000 end-page: 10235 article-title: Establishment of an animal‐bacterial association: recruiting symbiotic vibrios from the environment publication-title: Proc Natl Acad Sci USA – volume: 191 start-page: 2012 year: 2008 end-page: 2022 article-title: Mutations in and lytic transglycosylase genes affect the net release of peptidoglycan monomers from publication-title: J Bacteriol – volume: 16 start-page: 733 year: 1995 end-page: 743 article-title: Tracheal cytotoxin structural requirements for respiratory epithelial damage in pertussis publication-title: Mol Microbiol – volume: 306 start-page: 1186 year: 2004 end-page: 1188 article-title: Microbial factor‐mediated development in a host‐bacterial mutualism publication-title: Science – volume: 8 start-page: 1059 year: 2006 end-page: 1069 article-title: Mammalian PGRPs: novel antibacterial proteins publication-title: Cell Microbiol – volume: 278 start-page: 49044 year: 2003 end-page: 49052 article-title: Human peptidoglycan recognition protein‐L is an ‐acetylmuramoyl‐L‐alanine amidase publication-title: J Biol Chem – volume: 97 start-page: 13772 year: 2000 end-page: 13777 article-title: A family of peptidoglycan recognition proteins in the fruit fly publication-title: Proc Natl Acad Sci USA – volume: 72 start-page: 802 year: 2006 end-page: 810 article-title: New rfp‐ and pES213‐derived tools for analyzing symbiotic reveal patterns of infection and expression in situ publication-title: Appl Environ Microbiol – volume: 68 start-page: 280 year: 2004 end-page: 300 article-title: Infection and invasion of roots by symbiotic, nitrogen‐fixing rhizobia during nodulation of temperate legumes publication-title: Microbiol Mol Biol Rev – volume: 120 start-page: 1719 year: 1994 end-page: 1729 article-title: Bacterial symbionts induce host organ morphogenesis during early postembryonic development of the squid publication-title: Development – volume: 182 start-page: 4578 year: 2000 end-page: 4586 article-title: lux genes play an important role in colonization and development of the host light organ publication-title: J Bacteriol – volume: 226 start-page: 242 year: 2000 end-page: 254 article-title: lipopolysaccharide induces developmental apoptosis, but not complete morphogenesis, of the symbiotic light organ publication-title: Dev Biol – volume: 315 start-page: 247 year: 2007 end-page: 250 article-title: Physiological proteomics of the uncultured endosymbiont of publication-title: Science – volume: 95 start-page: 1818 year: 1998 end-page: 1822 article-title: Host‐derived amino acids support the proliferation of symbiotic bacteria publication-title: Proc Natl Acad Sci USA – volume: 90 start-page: 2365 year: 1993 end-page: 2369 article-title: tracheal cytotoxin and other muramyl peptides: distinct structure‐activity relationships for respiratory epithelial cytopathology publication-title: Proc Natl Acad Sci USA – volume: 11 start-page: 631 year: 2009 end-page: 636 article-title: Bacterial detection by peptidoglycan recognition proteins publication-title: Microbes Infect – volume: 189 start-page: 347 year: 1995 end-page: 355 article-title: A transient exposure to symbiosis‐competent bacteria induces light organ morphogenesis in the host squid publication-title: Biol Bull – volume: 280 start-page: 37005 year: 2005 end-page: 37012 article-title: Selective recognition of synthetic lysine and meso‐diaminopimelic acid‐type peptidoglycan fragments by human peptidoglycan recognition proteins Iα and S publication-title: J Biol Chem – start-page: 99 year: 1971 end-page: 120 – volume: 195 start-page: 89 year: 1998 end-page: 97 article-title: Sampling the light‐organ microenvironment of : description of a population of host cells in association with the bacterial symbiont publication-title: Biol Bull – volume: 350 start-page: 994 year: 2006 end-page: 999 article-title: PGRP‐SB1: an ‐acetylmuramoyl l‐alanine amidase with antibacterial activity publication-title: Biochem Biophys Res Commun – volume: 208 start-page: 295 year: 1998 end-page: 303 article-title: Induction of apoptosis by cooperative bacteria in the morphogenesis of host epithelial tissues publication-title: Dev Genes E – volume: 59 start-page: 177 year: 2000 end-page: 185 article-title: Early nutrition and the development of immune function in the neonate publication-title: Proc Nutr Soc – ident: e_1_2_6_36_1 doi: 10.1016/j.bbrc.2006.09.139 – ident: e_1_2_6_25_1 doi: 10.1016/S1074-7613(04)00104-9 – ident: e_1_2_6_42_1 doi: 10.2307/1542815 – ident: e_1_2_6_20_1 doi: 10.1016/S0006-291X(03)01096-9 – ident: e_1_2_6_30_1 doi: 10.1128/AEM.60.5.1565-1571.1994 – ident: e_1_2_6_33_1 doi: 10.1016/j.bbrc.2009.01.140 – ident: e_1_2_6_45_1 doi: 10.1128/AEM.68.10.5113-5122.2002 – ident: e_1_2_6_16_1 doi: 10.1111/j.1462-5822.2006.00726.x – ident: e_1_2_6_2_1 doi: 10.1128/JB.01547-08 – ident: e_1_2_6_35_1 doi: 10.1126/science.1132913 – ident: e_1_2_6_19_1 doi: 10.1128/MMBR.68.2.280-300.2004 – ident: e_1_2_6_50_1 doi: 10.1111/j.1462-5822.2009.01315.x – ident: e_1_2_6_46_1 doi: 10.1007/BF00250277 – ident: e_1_2_6_23_1 doi: 10.1073/pnas.95.4.1818 – ident: e_1_2_6_5_1 doi: 10.1007/BF00193435 – ident: e_1_2_6_41_1 doi: 10.1242/dev.120.7.1719 – ident: e_1_2_6_52_1 doi: 10.1074/jbc.M307758200 – ident: e_1_2_6_48_1 doi: 10.1002/(SICI)1097-4644(19990315)72:4<445::AID-JCB1>3.0.CO;2-P – ident: e_1_2_6_29_1 doi: 10.1128/IAI.66.2.777-785.1998 – ident: e_1_2_6_49_1 doi: 10.1111/j.0105-2896.2004.0120.x – ident: e_1_2_6_53_1 doi: 10.1073/pnas.97.25.13772 – ident: e_1_2_6_14_1 doi: 10.1128/AEM.72.1.802-810.2006 – ident: e_1_2_6_26_1 doi: 10.1017/S0029665100000197 – ident: e_1_2_6_10_1 doi: 10.1016/j.dci.2006.11.006 – start-page: 99 volume-title: Methods in Enzymology year: 1971 ident: e_1_2_6_24_1 contributor: fullname: Kaback H.R. – ident: e_1_2_6_11_1 doi: 10.1111/j.1462-5822.2004.00429.x – ident: e_1_2_6_27_1 doi: 10.1126/science.1102218 – ident: e_1_2_6_34_1 doi: 10.1126/science.1962208 – ident: e_1_2_6_7_1 doi: 10.1182/blood-2005-02-0530 – ident: e_1_2_6_22_1 doi: 10.1038/nature734 – ident: e_1_2_6_44_1 doi: 10.1073/pnas.97.18.10231 – ident: e_1_2_6_17_1 doi: 10.1007/s004270050185 – ident: e_1_2_6_37_1 doi: 10.1074/jbc.M208900200 – ident: e_1_2_6_13_1 doi: 10.2307/1542152 – ident: e_1_2_6_21_1 doi: 10.1128/AEM.71.11.6934-6946.2005 – ident: e_1_2_6_31_1 doi: 10.1073/pnas.90.6.2365 – ident: e_1_2_6_3_1 doi: 10.1042/BST0351496 – ident: e_1_2_6_39_1 doi: 10.1038/414756a – volume-title: Enzymes year: 1964 ident: e_1_2_6_12_1 contributor: fullname: Dixon M. – ident: e_1_2_6_15_1 doi: 10.1016/j.molimm.2003.10.011 – ident: e_1_2_6_43_1 doi: 10.1038/nrmicro957 – ident: e_1_2_6_8_1 doi: 10.1038/nrmicro1486 – ident: e_1_2_6_47_1 doi: 10.1101/gad.817800 – ident: e_1_2_6_4_1 doi: 10.1371/journal.ppat.0020014 – ident: e_1_2_6_38_1 doi: 10.1093/infdis/149.3.378 – ident: e_1_2_6_40_1 doi: 10.2307/1542448 – ident: e_1_2_6_6_1 doi: 10.1016/j.micinf.2009.03.004 – ident: e_1_2_6_9_1 doi: 10.1111/j.1365-2672.2007.03366.x – ident: e_1_2_6_18_1 doi: 10.1006/dbio.2000.9868 – ident: e_1_2_6_32_1 doi: 10.1111/j.1365-2958.1995.tb02434.x – ident: e_1_2_6_28_1 doi: 10.1074/jbc.M506385200 – ident: e_1_2_6_54_1 doi: 10.1016/j.immuni.2006.02.012 – ident: e_1_2_6_51_1 doi: 10.1128/JB.182.16.4578-4586.2000 |
SSID | ssj0017370 |
Score | 2.3312461 |
Snippet | Summary
In horizontally transmitted mutualisms between marine animals and their bacterial partners, the host environment promotes the initial colonization by... In horizontally transmitted mutualisms between marine animals and their bacterial partners, the host environment promotes the initial colonization by specific... SummaryIn horizontally transmitted mutualisms between marine animals and their bacterial partners, the host environment promotes the initial colonization by... In horizontally-transmitted mutualisms between marine animals and their bacterial partners, the host environment promotes the initial colonization by specific... |
SourceID | pubmedcentral proquest crossref pubmed wiley istex |
SourceType | Open Access Repository Aggregation Database Index Database Publisher |
StartPage | 2190 |
SubjectTerms | Aliivibrio fischeri - growth & development Amidohydrolases - metabolism Animals Bacterial Toxins - antagonists & inhibitors Carrier Proteins - metabolism Cytotoxins - antagonists & inhibitors Decapodiformes - metabolism Decapodiformes - microbiology Epithelium - metabolism Euprymna scolopes Morphogenesis Mucus - chemistry Symbiosis Vibrio fischeri |
Title | Taming the symbiont for coexistence: a host PGRP neutralizes a bacterial symbiont toxin |
URI | https://api.istex.fr/ark:/67375/WNG-30T5PRW6-4/fulltext.pdf https://onlinelibrary.wiley.com/doi/abs/10.1111%2Fj.1462-2920.2009.02121.x https://www.ncbi.nlm.nih.gov/pubmed/21966913 https://search.proquest.com/docview/754896994 https://pubmed.ncbi.nlm.nih.gov/PMC2889240 |
Volume | 12 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1LS8QwEB5EEbz4ftQXOYi3Lk3TpzcRHwjKsqyst5C0WZTFrrhdWP31zqTd4q4eRLyVNmnJZCbzTTr5BuCkH-pEBUK7sUk8NwhF5Grf5K6nfBHoXGjPcnfe3Uc3D8HtY_hY5z_RWZiKH6LZcCPLsOs1GbjSo3kj912qtlTTTuIqzFuEJ4lXj_BRp2GS4rGwdePqLnwuqefHF814qiUS-uQnGPo9m_IryrVu6moNBtMBVtkpg9a41K3sY4778X8ksA6rNZpl55X6bcCCKTZhuapv-b4Fva56QdfIEGSy0fuLRh0oGaJklg2JgdPC9TOmGJ00Ye3rTpsVZmy3Xj7MCO_rikoav9D0LoeT52IbHq4uuxc3bl3Jwc0iBCSuDpWiU7C-z43AqDhTWWLQL2qKPvuZEX2TihyXjtQzmWdweKhCORHHcG76uEbswGIxLMwesJzTzmWCGoaRUMZ5mhPEU7nhIgy0Ug7w6azJ14qwQ84EOr4kgVH5zVRagcmJA6d2epsO6m1ACW9xKHv311J43bDd6UUycIBN51-iGdK_FVWY4XgkY4z80ihNsclupQ7Ny9AnRFHKhQPxjKI0DYjhe_ZJ8fxkmb79JMH42HMgsnrw6wFJtGG62v9rxwNYqdIkKNPxEBbLt7E5QvRV6mNrV59rVB_Z |
link.rule.ids | 230,315,786,790,891,1382,27955,27956,46327,46751 |
linkProvider | Wiley-Blackwell |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3dT9swED9NoAleNrbBFmDDD9PeUsVxPveG-CpfVVUVlTfLTlyBGCmiqVT467lz0mgtPCDEW5TYiWzf-X53Of8O4Pcw1IkKhHZjk3huEIrI1b7JXU_5ItC50J7l7jzvRO2L4OQyvKzLAdFZmIofogm4kWbY_ZoUnALSi1ruu1RuqeadxG2YtxBQLqP2h6Sl-72GS4rHwlaOq_vwhbSeF980Z6uWadqnLwHR5_mU_-Nca6gOP8O_2RCr_JSb1qTUrexxgf3xneZgDT7VgJbtVhL4BT6Y4it8rEpcPnyDQV_donVkiDPZ-OFWoxiUDIEyy0ZEwmkR-1-mGB02Yd2jXpcVZmKjL49mjPd1xSaNX2h6l6PpdbEOF4cH_b22WxdzcLMIMYmrQ6XoIKzvcyPQMc5Ulhg0jZoc0GFmxNCkIsfdI_VM5hkcHkpRTtwxnJshbhMbsFSMCvMDWM4peJmgkKEzlHGe5oTyVG64CAOtlAN8tmzyruLskHO-ji9pwqgCZyrthMmpA3_s-jYd1P0N5bzFoRx0jqTw-mG3N4hk4ACbCYBETaTfK6owo8lYxuj8pVGaYpPvlTw0L0OzEEUpFw7Ec5LSNCCS7_knxfWVJfv2kwRdZM-ByArCqwckUY3pavOtHXdgpd0_P5Nnx53TLVitsiYo8XEblsr7ifmJYKzUv6ySPQF6wiP5 |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3fT9swED4hENNextjPsI35Ae0tVRwnTrK3aazANqqqKipvlp04GqpIEU2lwl-_OyeN1o6HCe0tSuxEPt_5vnPO3wEclbFJdSSMn9g08KNYSN-EtvADHYrIFMIEjrvzfCBPL6Lvl_Flm_9EZ2Eafohuw40sw63XZOA3Rblp5KFP1ZZa2klchXkP8eROJEVIgdjxqKOS4olwhePaPnwjq-fBN625qh2S-vIhHPp3OuWfMNf5qf4eTFcjbNJTpr1FbXr5_Qb54_8RwXN41sJZ9qXRv33YstUL2G0KXN69hMlYX6NvZIgy2fzu2qAS1AxhMstnRMHp8PpnphkdNWHDk9GQVXbh9l7u7Rzvm4ZLGr_Q9a5ny6vqFVz0v42_nvptKQc_l4hIfBNrTcdgw5BbgWFxrvPUomM0FH6WuRWlzUSBa0cW2DywODzUoYKYYzi3JS4Sr2G7mlX2LbCC09ZliiqGoVDOeVYQxtOF5SKOjNYe8NWsqZuGsUOtRTqhIoFR_c1MOYGppQef3PR2HfTtlDLeklhNBidKBON4OJpIFXnAVvOv0A7p54qu7GwxVwmGfpnMMmzyplGH7mXoFKTMuPAgWVOUrgFRfK8_qa5-OarvME0xQA48kE4P_nlACo2Yrg4e2_EjPBke99XPs8GPd_C0SZmgrMf3sF3fLuwHRGK1OXQm9hviWyKo |
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=Taming+the+symbiont+for+coexistence%3A+a+host+PGRP+neutralizes+a+bacterial+symbiont+toxin&rft.jtitle=Environmental+microbiology&rft.au=Troll%2C+Joshua+V&rft.au=Bent%2C+Eric+H&rft.au=Pacquette%2C+Nicholas&rft.au=Wier%2C+Andrew+M&rft.date=2010-08-01&rft.issn=1462-2912&rft.volume=12&rft.issue=8&rft.spage=2190&rft.epage=2203&rft_id=info:doi/10.1111%2Fj.1462-2920.2009.02121.x&rft.externalDBID=NO_FULL_TEXT |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1462-2912&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1462-2912&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1462-2912&client=summon |