Identification of a pathogen-binding lectin in salmon serum

K. Vanya Ewart; Stewart C. Johnson; Neil W. Ross

doi:10.1016/S0742-8413(99)00002-X

Identification of a pathogen-binding lectin in salmon serum

K. Vanya Ewart, Stewart C. Johnson, Neil W. Ross

Research output: Contribution to journal › Article › peer-review

65 Citations (Scopus)

Abstract

A mannose-binding lectin was isolated from the blood serum of Atlantic salmon (Salmo salar). Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing and non-reducing conditions revealed a multimeric structure composed of 17 000 M(r) subunits. Hexosamine analysis and glycosidase digestion showed that the lectin is not glycosylated and amino acid analysis revealed no unusual compositional features. Using ruthenium red staining, the lectin was shown to bind Ca²⁺ ions. N-terminal sequencing by Edman degradation gave: H₂N-TGAKGAEEGVVPAETRNQXPTGWFQFGS. A database search revealed no similarity to protein sequences deposited to date. Binding experiments using biotinylated lectin revealed that it specifically recognizes and binds to mannose on the surfaces of two salmon pathogens, Vibrio anguillarum and Aeromonas salmonicida, implying an immunological role for this lectin in Atlantic salmon. Copyright (C) 1999 Elsevier Science Inc.

Original language	English
Pages (from-to)	9-15
Number of pages	7
Journal	Comparative Biochemistry and Physiology - C Pharmacology Toxicology and Endocrinology
Volume	123
Issue number	1
DOIs	https://doi.org/10.1016/S0742-8413(99)00002-X
Publication status	Published - May 1999
Externally published	Yes

ASJC Scopus Subject Areas

Immunology
Pharmacology

PubMed: MeSH publication types

Journal Article

Access to Document

10.1016/S0742-8413(99)00002-X

Cite this

Ewart, K. V., Johnson, S. C., & Ross, N. W. (1999). Identification of a pathogen-binding lectin in salmon serum. Comparative Biochemistry and Physiology - C Pharmacology Toxicology and Endocrinology, 123(1), 9-15. https://doi.org/10.1016/S0742-8413(99)00002-X

@article{893bdc70b7b941ebafbcba88507b7e6b,

title = "Identification of a pathogen-binding lectin in salmon serum",

abstract = "A mannose-binding lectin was isolated from the blood serum of Atlantic salmon (Salmo salar). Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing and non-reducing conditions revealed a multimeric structure composed of 17 000 M(r) subunits. Hexosamine analysis and glycosidase digestion showed that the lectin is not glycosylated and amino acid analysis revealed no unusual compositional features. Using ruthenium red staining, the lectin was shown to bind Ca2+ ions. N-terminal sequencing by Edman degradation gave: H2N-TGAKGAEEGVVPAETRNQXPTGWFQFGS. A database search revealed no similarity to protein sequences deposited to date. Binding experiments using biotinylated lectin revealed that it specifically recognizes and binds to mannose on the surfaces of two salmon pathogens, Vibrio anguillarum and Aeromonas salmonicida, implying an immunological role for this lectin in Atlantic salmon. Copyright (C) 1999 Elsevier Science Inc.",

author = "Ewart, {K. Vanya} and Johnson, {Stewart C.} and Ross, {Neil W.}",

year = "1999",

month = may,

doi = "10.1016/S0742-8413(99)00002-X",

language = "English",

volume = "123",

pages = "9--15",

journal = "Comparative Biochemistry and Physiology - C Pharmacology Toxicology and Endocrinology",

issn = "0742-8413",

publisher = "Elsevier BV",

number = "1",

}

TY - JOUR

T1 - Identification of a pathogen-binding lectin in salmon serum

AU - Ewart, K. Vanya

AU - Johnson, Stewart C.

AU - Ross, Neil W.

PY - 1999/5

Y1 - 1999/5

N2 - A mannose-binding lectin was isolated from the blood serum of Atlantic salmon (Salmo salar). Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing and non-reducing conditions revealed a multimeric structure composed of 17 000 M(r) subunits. Hexosamine analysis and glycosidase digestion showed that the lectin is not glycosylated and amino acid analysis revealed no unusual compositional features. Using ruthenium red staining, the lectin was shown to bind Ca2+ ions. N-terminal sequencing by Edman degradation gave: H2N-TGAKGAEEGVVPAETRNQXPTGWFQFGS. A database search revealed no similarity to protein sequences deposited to date. Binding experiments using biotinylated lectin revealed that it specifically recognizes and binds to mannose on the surfaces of two salmon pathogens, Vibrio anguillarum and Aeromonas salmonicida, implying an immunological role for this lectin in Atlantic salmon. Copyright (C) 1999 Elsevier Science Inc.

AB - A mannose-binding lectin was isolated from the blood serum of Atlantic salmon (Salmo salar). Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing and non-reducing conditions revealed a multimeric structure composed of 17 000 M(r) subunits. Hexosamine analysis and glycosidase digestion showed that the lectin is not glycosylated and amino acid analysis revealed no unusual compositional features. Using ruthenium red staining, the lectin was shown to bind Ca2+ ions. N-terminal sequencing by Edman degradation gave: H2N-TGAKGAEEGVVPAETRNQXPTGWFQFGS. A database search revealed no similarity to protein sequences deposited to date. Binding experiments using biotinylated lectin revealed that it specifically recognizes and binds to mannose on the surfaces of two salmon pathogens, Vibrio anguillarum and Aeromonas salmonicida, implying an immunological role for this lectin in Atlantic salmon. Copyright (C) 1999 Elsevier Science Inc.

UR - http://www.scopus.com/inward/record.url?scp=0033004660&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0033004660&partnerID=8YFLogxK

U2 - 10.1016/S0742-8413(99)00002-X

DO - 10.1016/S0742-8413(99)00002-X

M3 - Article

C2 - 10390051

AN - SCOPUS:0033004660

SN - 0742-8413

VL - 123

SP - 9

EP - 15

JO - Comparative Biochemistry and Physiology - C Pharmacology Toxicology and Endocrinology

JF - Comparative Biochemistry and Physiology - C Pharmacology Toxicology and Endocrinology

IS - 1

ER -

Identification of a pathogen-binding lectin in salmon serum

Abstract

ASJC Scopus Subject Areas

PubMed: MeSH publication types

Access to Document

Other files and links

Fingerprint

Cite this