Zebrafish intelectin 1 (zITLN1) plays a role in the innate immune response. Issue 83 (December 2018)
- Record Type:
- Journal Article
- Title:
- Zebrafish intelectin 1 (zITLN1) plays a role in the innate immune response. Issue 83 (December 2018)
- Main Title:
- Zebrafish intelectin 1 (zITLN1) plays a role in the innate immune response
- Authors:
- Chen, Lei
Yan, Jie
Shi, Jing
Sun, Wenbo
Chen, Zhi
Yu, Jiang
Qi, Jing
Du, Yijun
Zhang, Haiqing
Feng, Lijun - Abstract:
- Abstract: Intelectin displays carbohydrate binding capacity and has been demonstrated to agglutinate bacteria, suggesting its role in innate immunity. It has also been linked to many pathogenic conditions in human. After reporting two amphioxus orthologs and the zebrafish intelectin 2 ( zITLN2 ), here we cloned and characterized zebrafish intelectin 1 ( zITLN1 ). Like zITLN2, zITLN1 also contains a conserved fibrinogen-related domain (FReD) and a unique intelectin domain (ITLN-D), expresses in all the tissues tested, with the highest level in intestine, and responds to bacterial challenge in acute phase. We also expressed zITLN1 in E. coli system, and purified recombinant zITLN1 could agglutinate both Gram-positive and Gram-negative bacteria in a calcium dependent manner. Its ability to agglutinate Gram-positive bacteria is stronger than that to Gram-negative bacteria whereas zITLN2 did not show such preference. This is probably due to the fact that recombinant zITLN1 could bind peptidoglycan (PGN) with a higher degree to lipopolysaccharide (LPS). Our results of zITLN1 provided new insight into the evolution and function of the intelectin family. Highlights: An zebrafish intelectin ortholog, zITLN1 with a fibrinogen-related domain and a unique intelectin domain was characterized. The zITLN1 is widely expressed with highest level in intestine and upregulated after challenge of Staphylococcus aureus and E.coli. Recombinant zITLN1 binds both LPS and PGN and agglutinates bothAbstract: Intelectin displays carbohydrate binding capacity and has been demonstrated to agglutinate bacteria, suggesting its role in innate immunity. It has also been linked to many pathogenic conditions in human. After reporting two amphioxus orthologs and the zebrafish intelectin 2 ( zITLN2 ), here we cloned and characterized zebrafish intelectin 1 ( zITLN1 ). Like zITLN2, zITLN1 also contains a conserved fibrinogen-related domain (FReD) and a unique intelectin domain (ITLN-D), expresses in all the tissues tested, with the highest level in intestine, and responds to bacterial challenge in acute phase. We also expressed zITLN1 in E. coli system, and purified recombinant zITLN1 could agglutinate both Gram-positive and Gram-negative bacteria in a calcium dependent manner. Its ability to agglutinate Gram-positive bacteria is stronger than that to Gram-negative bacteria whereas zITLN2 did not show such preference. This is probably due to the fact that recombinant zITLN1 could bind peptidoglycan (PGN) with a higher degree to lipopolysaccharide (LPS). Our results of zITLN1 provided new insight into the evolution and function of the intelectin family. Highlights: An zebrafish intelectin ortholog, zITLN1 with a fibrinogen-related domain and a unique intelectin domain was characterized. The zITLN1 is widely expressed with highest level in intestine and upregulated after challenge of Staphylococcus aureus and E.coli. Recombinant zITLN1 binds both LPS and PGN and agglutinates both Gram positive and negative bacteria. … (more)
- Is Part Of:
- Fish & shellfish immunology. Issue 83(2018)
- Journal:
- Fish & shellfish immunology
- Issue:
- Issue 83(2018)
- Issue Display:
- Volume 83, Issue 83 (2018)
- Year:
- 2018
- Volume:
- 83
- Issue:
- 83
- Issue Sort Value:
- 2018-0083-0083-0000
- Page Start:
- 96
- Page End:
- 103
- Publication Date:
- 2018-12
- Subjects:
- Intelectin -- Innate immunity -- Bacterial carbohydrates -- Carbohydrate recognition domain -- Zebrafish
Fishes -- Immunology -- Periodicals
Shellfish -- Immunology -- Periodicals
Poissons -- Immunologie -- Périodiques
Crustacés -- Immunologie -- Périodiques
571.9617 - Journal URLs:
- http://www.sciencedirect.com/science/journal/10504648 ↗
http://firstsearch.oclc.org ↗
http://firstsearch.oclc.org/journal=1050-4648;screen=info;ECOIP ↗
http://www.sciencedirect.com/science/journal/latest/10504648 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.fsi.2018.09.004 ↗
- Languages:
- English
- ISSNs:
- 1050-4648
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3934.880000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 8016.xml