NK-lysin, structure and function of a novel effector molecule of porcine T and NK cells

M. Andersson; H. Gunne; B. Agerberth; A. Boman; T. Bergman; B. Olsson; Å Dagerlind; H. Wigzell; H. G. Boman; G. H. Gudmundsson

doi:10.1016/S0165-2427(96)05677-2

NK-lysin, structure and function of a novel effector molecule of porcine T and NK cells

M. Andersson, H. Gunne, B. Agerberth, A. Boman, T. Bergman, B. Olsson, Å Dagerlind, H. Wigzell, H. G. Boman, G. H. Gudmundsson^*

^*Corresponding author for this work

Faculty of Life and Environmental Sciences

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

51 Citations (Scopus)

Abstract

NK-lysin (NKL), a 78-residue antimicrobial peptide, was isolated from pig small intestine. Standard methods identified the peptide as basic, with six half-cystine residues in three intrachain disulphide bonds. The sequence showed 33% identity with a part of a putative gene product (NKG5) from activated T and NK cells. NK-lysin showed antibacterial activity against Escherichia coli and Bacillus megaterium and marked lytic activity against YAC-1, a NK sensitive tumour cell line, while sheep red blood cells were unaffected. The cDNA clone corresponding to NK-lysin has been characterized. We have also analyzed the cell and tissue specific expression and the induction of the gene. A lymphocyte fraction enriched in T and NK cells, stimulated by human interleukin-2 (IL-2), showed a 30-fold increase of the NKL transcript. NK-lysin specific mRNA is also detectable in spleen, bone marrow and colon. Immunostaining showed NKL to be present in different types of lymphocytes. Our results strongly suggest that NK-lysin is involved in the inducible cytotoxicity of T and NK cells.

Original language	English
Pages (from-to)	123-126
Number of pages	4
Journal	Veterinary Immunology and Immunopathology
Volume	54
Issue number	1-4
DOIs	https://doi.org/10.1016/S0165-2427(96)05677-2
Publication status	Published - Nov 1996

Other keywords

antibacterial peptide
cDNA cloning
cytotoxic peptide
IL-2 induction

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10.1016/S0165-2427(96)05677-2

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@article{8b19c2a1d5fd4fa681940f5a7f9b6ce0,

title = "NK-lysin, structure and function of a novel effector molecule of porcine T and NK cells",

abstract = "NK-lysin (NKL), a 78-residue antimicrobial peptide, was isolated from pig small intestine. Standard methods identified the peptide as basic, with six half-cystine residues in three intrachain disulphide bonds. The sequence showed 33% identity with a part of a putative gene product (NKG5) from activated T and NK cells. NK-lysin showed antibacterial activity against Escherichia coli and Bacillus megaterium and marked lytic activity against YAC-1, a NK sensitive tumour cell line, while sheep red blood cells were unaffected. The cDNA clone corresponding to NK-lysin has been characterized. We have also analyzed the cell and tissue specific expression and the induction of the gene. A lymphocyte fraction enriched in T and NK cells, stimulated by human interleukin-2 (IL-2), showed a 30-fold increase of the NKL transcript. NK-lysin specific mRNA is also detectable in spleen, bone marrow and colon. Immunostaining showed NKL to be present in different types of lymphocytes. Our results strongly suggest that NK-lysin is involved in the inducible cytotoxicity of T and NK cells.",

keywords = "antibacterial peptide, cDNA cloning, cytotoxic peptide, IL-2 induction",

author = "M. Andersson and H. Gunne and B. Agerberth and A. Boman and T. Bergman and B. Olsson and {\AA} Dagerlind and H. Wigzell and Boman, {H. G.} and Gudmundsson, {G. H.}",

year = "1996",

month = nov,

doi = "10.1016/S0165-2427(96)05677-2",

language = "English",

volume = "54",

pages = "123--126",

journal = "Veterinary Immunology and Immunopathology",

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T1 - NK-lysin, structure and function of a novel effector molecule of porcine T and NK cells

AU - Andersson, M.

AU - Gunne, H.

AU - Agerberth, B.

AU - Boman, A.

AU - Bergman, T.

AU - Olsson, B.

AU - Dagerlind, Å

AU - Wigzell, H.

AU - Boman, H. G.

AU - Gudmundsson, G. H.

PY - 1996/11

Y1 - 1996/11

N2 - NK-lysin (NKL), a 78-residue antimicrobial peptide, was isolated from pig small intestine. Standard methods identified the peptide as basic, with six half-cystine residues in three intrachain disulphide bonds. The sequence showed 33% identity with a part of a putative gene product (NKG5) from activated T and NK cells. NK-lysin showed antibacterial activity against Escherichia coli and Bacillus megaterium and marked lytic activity against YAC-1, a NK sensitive tumour cell line, while sheep red blood cells were unaffected. The cDNA clone corresponding to NK-lysin has been characterized. We have also analyzed the cell and tissue specific expression and the induction of the gene. A lymphocyte fraction enriched in T and NK cells, stimulated by human interleukin-2 (IL-2), showed a 30-fold increase of the NKL transcript. NK-lysin specific mRNA is also detectable in spleen, bone marrow and colon. Immunostaining showed NKL to be present in different types of lymphocytes. Our results strongly suggest that NK-lysin is involved in the inducible cytotoxicity of T and NK cells.

AB - NK-lysin (NKL), a 78-residue antimicrobial peptide, was isolated from pig small intestine. Standard methods identified the peptide as basic, with six half-cystine residues in three intrachain disulphide bonds. The sequence showed 33% identity with a part of a putative gene product (NKG5) from activated T and NK cells. NK-lysin showed antibacterial activity against Escherichia coli and Bacillus megaterium and marked lytic activity against YAC-1, a NK sensitive tumour cell line, while sheep red blood cells were unaffected. The cDNA clone corresponding to NK-lysin has been characterized. We have also analyzed the cell and tissue specific expression and the induction of the gene. A lymphocyte fraction enriched in T and NK cells, stimulated by human interleukin-2 (IL-2), showed a 30-fold increase of the NKL transcript. NK-lysin specific mRNA is also detectable in spleen, bone marrow and colon. Immunostaining showed NKL to be present in different types of lymphocytes. Our results strongly suggest that NK-lysin is involved in the inducible cytotoxicity of T and NK cells.

KW - antibacterial peptide

KW - cDNA cloning

KW - cytotoxic peptide

KW - IL-2 induction

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AN - SCOPUS:0030292764

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JO - Veterinary Immunology and Immunopathology

JF - Veterinary Immunology and Immunopathology

IS - 1-4

ER -

NK-lysin, structure and function of a novel effector molecule of porcine T and NK cells

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