F-type lectin from serum of the Antarctic teleost fish Trematomus bernacchii (Boulenger, 1902): Purification, structural characterization, and bacterial agglutinating activity
The increasing availability of sequenced genomes has enabled a deeper understanding of the complexity of fish lectin repertoires involved in early development and immune recognition. The teleost fucose-type lectin (FTL) family includes proteins that preferentially bind fucose and display tandemly ar...
Published in: | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology |
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Online Access: | http://hdl.handle.net/11368/3028959 https://doi.org/10.1016/j.cbpb.2021.110633 https://www.sciencedirect.com/science/article/pii/S1096495921000725 |
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ftunitriestiris:oai:arts.units.it:11368/3028959 2023-05-15T14:08:46+02:00 F-type lectin from serum of the Antarctic teleost fish Trematomus bernacchii (Boulenger, 1902): Purification, structural characterization, and bacterial agglutinating activity Dara M. Giulianini P. G. Manfrin C. Parisi M. G. Parrinello D. La Corte C. Vasta G. R. Cammarata M. Dara, M. Giulianini, P. G. Manfrin, C. Parisi, M. G. Parrinello, D. La Corte, C. Vasta, G. R. Cammarata, M. 2021 STAMPA http://hdl.handle.net/11368/3028959 https://doi.org/10.1016/j.cbpb.2021.110633 https://www.sciencedirect.com/science/article/pii/S1096495921000725 eng eng info:eu-repo/semantics/altIdentifier/pmid/34126205 info:eu-repo/semantics/altIdentifier/wos/WOS:000684852500016 volume:256 firstpage:"-" lastpage:"-" numberofpages:10 journal:COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY. PART B, BIOCHEMISTRY & MOLECULAR BIOLOGY http://hdl.handle.net/11368/3028959 doi:10.1016/j.cbpb.2021.110633 https://www.sciencedirect.com/science/article/pii/S1096495921000725 info:eu-repo/semantics/restrictedAccess Antarctic fish Bacterial agglutination F-type lectin Lectin Trematomus bernacchii Amino Acid Sequence Animal Antarctic Region Bacteria Base Sequence Fucose Perciforme Phylogeny info:eu-repo/semantics/article 2021 ftunitriestiris https://doi.org/10.1016/j.cbpb.2021.110633 2023-04-09T06:21:13Z The increasing availability of sequenced genomes has enabled a deeper understanding of the complexity of fish lectin repertoires involved in early development and immune recognition. The teleost fucose-type lectin (FTL) family includes proteins that preferentially bind fucose and display tandemly arrayed carbohydrate-recognition domains (CRDs) or are found in mosaic combinations with other domains. They function as opsonins, promoting phagocytosis and the clearance of microbial pathogens. The Antarctic fish Trematomus bernacchii is a Perciforme living at extremely low temperatures (−1.68 °C) which is considered a model for studying adaptability to the variability of environmental waters. Here, we isolated a Ca++-independent fucose-binding protein from the serum of T. bernacchii by affinity chromatography with apparent molecular weights of 32 and 30 kDa under reducing and non-reducing conditions, respectively. We have characterized its carbohydrate binding properties, thermal stability and potential ability to recognize bacterial pathogens. In western blot analysis, the protein showed intense cross-reactivity with antibodies specific for a sea bass (Dicentrarchus labrax) fucose-binding lectin. In addition, its molecular and structural aspects, showing that it contains two CRD-FTLs confirmed that T. bernacchii FTL (TbFTL) is a bona fide member of the FTL family, with binding activity at low temperatures and the ability to agglutinate bacteria, thereby suggesting it participates in host-pathogen interactions in low temperature environments. Article in Journal/Newspaper Antarc* Antarctic Università degli studi di Trieste: ArTS (Archivio della ricerca di Trieste) Antarctic The Antarctic Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 256 110633 |
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Open Polar |
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Università degli studi di Trieste: ArTS (Archivio della ricerca di Trieste) |
op_collection_id |
ftunitriestiris |
language |
English |
topic |
Antarctic fish Bacterial agglutination F-type lectin Lectin Trematomus bernacchii Amino Acid Sequence Animal Antarctic Region Bacteria Base Sequence Fucose Perciforme Phylogeny |
spellingShingle |
Antarctic fish Bacterial agglutination F-type lectin Lectin Trematomus bernacchii Amino Acid Sequence Animal Antarctic Region Bacteria Base Sequence Fucose Perciforme Phylogeny Dara M. Giulianini P. G. Manfrin C. Parisi M. G. Parrinello D. La Corte C. Vasta G. R. Cammarata M. F-type lectin from serum of the Antarctic teleost fish Trematomus bernacchii (Boulenger, 1902): Purification, structural characterization, and bacterial agglutinating activity |
topic_facet |
Antarctic fish Bacterial agglutination F-type lectin Lectin Trematomus bernacchii Amino Acid Sequence Animal Antarctic Region Bacteria Base Sequence Fucose Perciforme Phylogeny |
description |
The increasing availability of sequenced genomes has enabled a deeper understanding of the complexity of fish lectin repertoires involved in early development and immune recognition. The teleost fucose-type lectin (FTL) family includes proteins that preferentially bind fucose and display tandemly arrayed carbohydrate-recognition domains (CRDs) or are found in mosaic combinations with other domains. They function as opsonins, promoting phagocytosis and the clearance of microbial pathogens. The Antarctic fish Trematomus bernacchii is a Perciforme living at extremely low temperatures (−1.68 °C) which is considered a model for studying adaptability to the variability of environmental waters. Here, we isolated a Ca++-independent fucose-binding protein from the serum of T. bernacchii by affinity chromatography with apparent molecular weights of 32 and 30 kDa under reducing and non-reducing conditions, respectively. We have characterized its carbohydrate binding properties, thermal stability and potential ability to recognize bacterial pathogens. In western blot analysis, the protein showed intense cross-reactivity with antibodies specific for a sea bass (Dicentrarchus labrax) fucose-binding lectin. In addition, its molecular and structural aspects, showing that it contains two CRD-FTLs confirmed that T. bernacchii FTL (TbFTL) is a bona fide member of the FTL family, with binding activity at low temperatures and the ability to agglutinate bacteria, thereby suggesting it participates in host-pathogen interactions in low temperature environments. |
author2 |
Dara, M. Giulianini, P. G. Manfrin, C. Parisi, M. G. Parrinello, D. La Corte, C. Vasta, G. R. Cammarata, M. |
format |
Article in Journal/Newspaper |
author |
Dara M. Giulianini P. G. Manfrin C. Parisi M. G. Parrinello D. La Corte C. Vasta G. R. Cammarata M. |
author_facet |
Dara M. Giulianini P. G. Manfrin C. Parisi M. G. Parrinello D. La Corte C. Vasta G. R. Cammarata M. |
author_sort |
Dara M. |
title |
F-type lectin from serum of the Antarctic teleost fish Trematomus bernacchii (Boulenger, 1902): Purification, structural characterization, and bacterial agglutinating activity |
title_short |
F-type lectin from serum of the Antarctic teleost fish Trematomus bernacchii (Boulenger, 1902): Purification, structural characterization, and bacterial agglutinating activity |
title_full |
F-type lectin from serum of the Antarctic teleost fish Trematomus bernacchii (Boulenger, 1902): Purification, structural characterization, and bacterial agglutinating activity |
title_fullStr |
F-type lectin from serum of the Antarctic teleost fish Trematomus bernacchii (Boulenger, 1902): Purification, structural characterization, and bacterial agglutinating activity |
title_full_unstemmed |
F-type lectin from serum of the Antarctic teleost fish Trematomus bernacchii (Boulenger, 1902): Purification, structural characterization, and bacterial agglutinating activity |
title_sort |
f-type lectin from serum of the antarctic teleost fish trematomus bernacchii (boulenger, 1902): purification, structural characterization, and bacterial agglutinating activity |
publishDate |
2021 |
url |
http://hdl.handle.net/11368/3028959 https://doi.org/10.1016/j.cbpb.2021.110633 https://www.sciencedirect.com/science/article/pii/S1096495921000725 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/pmid/34126205 info:eu-repo/semantics/altIdentifier/wos/WOS:000684852500016 volume:256 firstpage:"-" lastpage:"-" numberofpages:10 journal:COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY. PART B, BIOCHEMISTRY & MOLECULAR BIOLOGY http://hdl.handle.net/11368/3028959 doi:10.1016/j.cbpb.2021.110633 https://www.sciencedirect.com/science/article/pii/S1096495921000725 |
op_rights |
info:eu-repo/semantics/restrictedAccess |
op_doi |
https://doi.org/10.1016/j.cbpb.2021.110633 |
container_title |
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology |
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110633 |
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