Involvement of a host Cathepsin L in symbiont‐induced cell death
The cathepsin L gene of the host squid, Euprymna scolopes, is upregulated during the first hours of colonization by the symbiont Vibrio fischeri. At this time, the symbiotic organ begins cell death‐mediated morphogenesis in tissues functional only at the onset of symbiosis. The goal of this study wa...
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Published in | MicrobiologyOpen (Weinheim) Vol. 7; no. 5; pp. e00632 - n/a |
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Main Authors | , , |
Format | Journal Article |
Language | English |
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England
John Wiley & Sons, Inc
01.10.2018
Wiley John Wiley and Sons Inc |
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Abstract | The cathepsin L gene of the host squid, Euprymna scolopes, is upregulated during the first hours of colonization by the symbiont Vibrio fischeri. At this time, the symbiotic organ begins cell death‐mediated morphogenesis in tissues functional only at the onset of symbiosis. The goal of this study was to determine whether Cathepsin L, a cysteine protease associated with apoptosis in other animals, plays a critical role in symbiont‐induced cell death in the host squid. Sequence analysis and biochemical characterization demonstrated that the protein has key residues and domains essential for Cathepsin L function and that it is active within the pH range typical of these proteases. With in situ hybridization and immunocytochemistry, we localized the transcript and protein, respectively, to cells interacting with V. fischeri. Activity of the protein occurred along the path of symbiont colonization. A specific Cathepsin L, nonspecific cysteine protease, and caspase inhibitor each independently attenuated activity and cell death to varying degrees. In addition, a specific antibody decreased cell death by ~50%. Together these data provide evidence that Cathepsin L is a critical component in the symbiont‐induced cell death that transforms the host tissues from a colonization morphology to one that promotes the mature association.
The goal of this study was to determine whether Cathepsin L plays a role in symbiont‐induced cell death in the host squid Euprymna scolopes. A specific Cathepsin L, nonspecific cysteine protease, caspase inhibitor, and specific antibody each independently attenuated enzyme activity and cell death to varying degrees. Our data suggest that Cathepsin L is a critical component in symbiont‐induced cell death that transforms the host tissues from a colonization morphology to one that promotes the mature association. |
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AbstractList | The cathepsin L gene of the host squid, Euprymna scolopes, is upregulated during the first hours of colonization by the symbiont Vibrio fischeri. At this time, the symbiotic organ begins cell death-mediated morphogenesis in tissues functional only at the onset of symbiosis. The goal of this study was to determine whether Cathepsin L, a cysteine protease associated with apoptosis in other animals, plays a critical role in symbiont-induced cell death in the host squid. Sequence analysis and biochemical characterization demonstrated that the protein has key residues and domains essential for Cathepsin L function and that it is active within the pH range typical of these proteases. With in situ hybridization and immunocytochemistry, we localized the transcript and protein, respectively, to cells interacting with V. fischeri. Activity of the protein occurred along the path of symbiont colonization. A specific Cathepsin L, nonspecific cysteine protease, and caspase inhibitor each independently attenuated activity and cell death to varying degrees. In addition, a specific antibody decreased cell death by ~50%. Together these data provide evidence that Cathepsin L is a critical component in the symbiont-induced cell death that transforms the host tissues from a colonization morphology to one that promotes the mature association. Abstract The cathepsin L gene of the host squid, Euprymna scolopes , is upregulated during the first hours of colonization by the symbiont Vibrio fischeri . At this time, the symbiotic organ begins cell death‐mediated morphogenesis in tissues functional only at the onset of symbiosis. The goal of this study was to determine whether Cathepsin L, a cysteine protease associated with apoptosis in other animals, plays a critical role in symbiont‐induced cell death in the host squid. Sequence analysis and biochemical characterization demonstrated that the protein has key residues and domains essential for Cathepsin L function and that it is active within the pH range typical of these proteases. With in situ hybridization and immunocytochemistry, we localized the transcript and protein, respectively, to cells interacting with V. fischeri . Activity of the protein occurred along the path of symbiont colonization. A specific Cathepsin L, nonspecific cysteine protease, and caspase inhibitor each independently attenuated activity and cell death to varying degrees. In addition, a specific antibody decreased cell death by ~50%. Together these data provide evidence that Cathepsin L is a critical component in the symbiont‐induced cell death that transforms the host tissues from a colonization morphology to one that promotes the mature association. The cathepsin L gene of the host squid, Euprymna scolopes , is upregulated during the first hours of colonization by the symbiont Vibrio fischeri . At this time, the symbiotic organ begins cell death‐mediated morphogenesis in tissues functional only at the onset of symbiosis. The goal of this study was to determine whether Cathepsin L, a cysteine protease associated with apoptosis in other animals, plays a critical role in symbiont‐induced cell death in the host squid. Sequence analysis and biochemical characterization demonstrated that the protein has key residues and domains essential for Cathepsin L function and that it is active within the pH range typical of these proteases. With in situ hybridization and immunocytochemistry, we localized the transcript and protein, respectively, to cells interacting with V. fischeri . Activity of the protein occurred along the path of symbiont colonization. A specific Cathepsin L, nonspecific cysteine protease, and caspase inhibitor each independently attenuated activity and cell death to varying degrees. In addition, a specific antibody decreased cell death by ~50%. Together these data provide evidence that Cathepsin L is a critical component in the symbiont‐induced cell death that transforms the host tissues from a colonization morphology to one that promotes the mature association. The cathepsin L gene of the host squid, Euprymna scolopes, is upregulated during the first hours of colonization by the symbiont Vibrio fischeri. At this time, the symbiotic organ begins cell death-mediated morphogenesis in tissues functional only at the onset of symbiosis. The goal of this study was to determine whether Cathepsin L, a cysteine protease associated with apoptosis in other animals, plays a critical role in symbiont-induced cell death in the host squid. Sequence analysis and biochemical characterization demonstrated that the protein has key residues and domains essential for Cathepsin L function and that it is active within the pH range typical of these proteases. With in situ hybridization and immunocytochemistry, we localized the transcript and protein, respectively, to cells interacting with V. fischeri. Activity of the protein occurred along the path of symbiont colonization. A specific Cathepsin L, nonspecific cysteine protease, and caspase inhibitor each independently attenuated activity and cell death to varying degrees. In addition, a specific antibody decreased cell death by ~50%. Together these data provide evidence that Cathepsin L is a critical component in the symbiont-induced cell death that transforms the host tissues from a colonization morphology to one that promotes the mature association. The cathepsin L gene of the host squid, Euprymna scolopes, is upregulated during the first hours of colonization by the symbiont Vibrio fischeri. At this time, the symbiotic organ begins cell death‐mediated morphogenesis in tissues functional only at the onset of symbiosis. The goal of this study was to determine whether Cathepsin L, a cysteine protease associated with apoptosis in other animals, plays a critical role in symbiont‐induced cell death in the host squid. Sequence analysis and biochemical characterization demonstrated that the protein has key residues and domains essential for Cathepsin L function and that it is active within the pH range typical of these proteases. With in situ hybridization and immunocytochemistry, we localized the transcript and protein, respectively, to cells interacting with V. fischeri. Activity of the protein occurred along the path of symbiont colonization. A specific Cathepsin L, nonspecific cysteine protease, and caspase inhibitor each independently attenuated activity and cell death to varying degrees. In addition, a specific antibody decreased cell death by ~50%. Together these data provide evidence that Cathepsin L is a critical component in the symbiont‐induced cell death that transforms the host tissues from a colonization morphology to one that promotes the mature association. The goal of this study was to determine whether Cathepsin L plays a role in symbiont‐induced cell death in the host squid Euprymna scolopes. A specific Cathepsin L, nonspecific cysteine protease, caspase inhibitor, and specific antibody each independently attenuated enzyme activity and cell death to varying degrees. Our data suggest that Cathepsin L is a critical component in symbiont‐induced cell death that transforms the host tissues from a colonization morphology to one that promotes the mature association. |
Author | Kremer, Natacha McFall‐Ngai, Margaret J. Peyer, Suzanne M. |
AuthorAffiliation | 3 Present address: Laboratoire de Biométrie et Biologie Evolutive UMR CNRS 5558 Université Lyon 1 Université de Lyon Villeurbanne France 1 School of Medicine and Public Health Department of Medical Microbiology and Immunology University of Wisconsin Madison WI USA 2 McPherson Eye Research Institute University of Wisconsin Madison WI USA 4 Present address: Pacific Biosciences Research Center University of Hawai'i at Manoa Honolulu HI USA |
AuthorAffiliation_xml | – name: 3 Present address: Laboratoire de Biométrie et Biologie Evolutive UMR CNRS 5558 Université Lyon 1 Université de Lyon Villeurbanne France – name: 2 McPherson Eye Research Institute University of Wisconsin Madison WI USA – name: 1 School of Medicine and Public Health Department of Medical Microbiology and Immunology University of Wisconsin Madison WI USA – name: 4 Present address: Pacific Biosciences Research Center University of Hawai'i at Manoa Honolulu HI USA |
Author_xml | – sequence: 1 givenname: Suzanne M. orcidid: 0000-0002-2142-8597 surname: Peyer fullname: Peyer, Suzanne M. email: smpeyer@wisc.edu organization: University of Wisconsin – sequence: 2 givenname: Natacha surname: Kremer fullname: Kremer, Natacha organization: University of Wisconsin – sequence: 3 givenname: Margaret J. surname: McFall‐Ngai fullname: McFall‐Ngai, Margaret J. email: mcfallng@hawaii.edu organization: University of Wisconsin |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/29692003$$D View this record in MEDLINE/PubMed https://univ-lyon1.hal.science/hal-01916830$$DView record in HAL |
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CitedBy_id | crossref_primary_10_1186_s12866_022_02614_x crossref_primary_10_3390_biom12060808 crossref_primary_10_1128_mSystems_00867_21 crossref_primary_10_1038_s41579_021_00567_y crossref_primary_10_1093_gbe_evab252 crossref_primary_10_1093_molbev_msab203 crossref_primary_10_1016_j_aquaculture_2022_738269 crossref_primary_10_1016_j_ecoenv_2019_04_079 |
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Keywords | cysteine protease development morphogenesis cell death symbiosis apoptosis cathepsin |
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Snippet | The cathepsin L gene of the host squid, Euprymna scolopes, is upregulated during the first hours of colonization by the symbiont Vibrio fischeri. At this time,... Abstract The cathepsin L gene of the host squid, Euprymna scolopes , is upregulated during the first hours of colonization by the symbiont Vibrio fischeri . At... The cathepsin L gene of the host squid, Euprymna scolopes , is upregulated during the first hours of colonization by the symbiont Vibrio fischeri . At this... |
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SubjectTerms | Aliivibrio fischeri - growth & development Animal Structures - enzymology Animal Structures - microbiology Animal Structures - physiology Animals Antibodies Apoptosis Aquatic life Bacteria Bacteriology Biochemistry, Molecular Biology Biodiversity Biodiversity and Ecology Caspase inhibitors cathepsin Cathepsin L Cathepsin L - metabolism Cell Death Colonization Critical components Cysteine cysteine protease Cysteine proteinase Cytology Decapodiformes - enzymology Decapodiformes - microbiology Decapodiformes - physiology development Ecology, environment Environmental Sciences Extracellular matrix Genomics Hybridization Hydrogen-Ion Concentration Immunocytochemistry Immunohistochemistry In Situ Hybridization L gene Life Sciences Light Microbiology and Parasitology Molecular biology Morphogenesis Morphology Mortality Original Populations and Evolution Protease Proteinase inhibitors Proteins Squid Symbiosis Transcription Virology Waterborne diseases |
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Title | Involvement of a host Cathepsin L in symbiont‐induced cell death |
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