The pattern recognition molecule ficolin-1 exhibits differential binding to lymphocyte subsets, providing a novel link between innate and adaptive immunity

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Standard

The pattern recognition molecule ficolin-1 exhibits differential binding to lymphocyte subsets, providing a novel link between innate and adaptive immunity. / Genster, Ninette; Ma, Ying Jie; Munthe-Fog, Lea; Garred, Peter.

In: Molecular Immunology, Vol. 57, No. 2, 02.2014, p. 181-190.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Genster, N, Ma, YJ, Munthe-Fog, L & Garred, P 2014, 'The pattern recognition molecule ficolin-1 exhibits differential binding to lymphocyte subsets, providing a novel link between innate and adaptive immunity', Molecular Immunology, vol. 57, no. 2, pp. 181-190. https://doi.org/10.1016/j.molimm.2013.09.006

APA

Genster, N., Ma, Y. J., Munthe-Fog, L., & Garred, P. (2014). The pattern recognition molecule ficolin-1 exhibits differential binding to lymphocyte subsets, providing a novel link between innate and adaptive immunity. Molecular Immunology, 57(2), 181-190. https://doi.org/10.1016/j.molimm.2013.09.006

Vancouver

Genster N, Ma YJ, Munthe-Fog L, Garred P. The pattern recognition molecule ficolin-1 exhibits differential binding to lymphocyte subsets, providing a novel link between innate and adaptive immunity. Molecular Immunology. 2014 Feb;57(2):181-190. https://doi.org/10.1016/j.molimm.2013.09.006

Author

Genster, Ninette ; Ma, Ying Jie ; Munthe-Fog, Lea ; Garred, Peter. / The pattern recognition molecule ficolin-1 exhibits differential binding to lymphocyte subsets, providing a novel link between innate and adaptive immunity. In: Molecular Immunology. 2014 ; Vol. 57, No. 2. pp. 181-190.

Bibtex

@article{d2f0bcb5e27f45e28c7980ec70e561d8,
title = "The pattern recognition molecule ficolin-1 exhibits differential binding to lymphocyte subsets, providing a novel link between innate and adaptive immunity",
abstract = "Ficolin-1 is a soluble pattern recognition molecule synthesized by myeloid cells and capable of activating the lectin pathway of complement on the surface of pathogens. It is tethered to the membranes of monocytes and granulocytes; however, the biological significance of cell-associated ficolin-1 is unknown. Recognition of healthy host cells by a pattern recognition molecule constitutes a potential hazard to self cells and tissues, emphasizing the importance of further elucidating the reported self-recognition. In the current study we investigated the potential recognition of lymphocytes by ficolin-1 and demonstrated that CD56(dim) NK-cells and both CD4(+) and CD8(+) subsets of activated T-cells were recognized by ficolin-1. In contrast we did not detect binding of ficolin-1 to CD56(bright) NK-cells, NKT-cells, resting T-cells or B-cells. Furthermore, we showed that the protein-lymphocyte interaction occurred via the pathogen-recognition domain of ficolin-1 to sialic acid on the cell surface. Thus, the differential binding of ficolin-1 to lymphocyte subsets suggests ficolin-1 as a novel link between innate and adaptive immunity. Our results provide new insight about the recognition properties of ficolin-1 and point toward additional immune modulating functions of the molecule besides its role in pathogen recognition.",
keywords = "Adaptive Immunity, Antigens, CD56, CD4-Positive T-Lymphocytes, CD8-Positive T-Lymphocytes, Humans, Immunity, Innate, Killer Cells, Natural, Lectins, Lymphocyte Activation, Lymphocyte Subsets, Natural Killer T-Cells, Protein Binding, Sialic Acids",
author = "Ninette Genster and Ma, {Ying Jie} and Lea Munthe-Fog and Peter Garred",
note = "Copyright {\textcopyright} 2013 Elsevier Ltd. All rights reserved.",
year = "2014",
month = feb,
doi = "10.1016/j.molimm.2013.09.006",
language = "English",
volume = "57",
pages = "181--190",
journal = "Molecular Immunology",
issn = "0161-5890",
publisher = "Pergamon Press",
number = "2",

}

RIS

TY - JOUR

T1 - The pattern recognition molecule ficolin-1 exhibits differential binding to lymphocyte subsets, providing a novel link between innate and adaptive immunity

AU - Genster, Ninette

AU - Ma, Ying Jie

AU - Munthe-Fog, Lea

AU - Garred, Peter

N1 - Copyright © 2013 Elsevier Ltd. All rights reserved.

PY - 2014/2

Y1 - 2014/2

N2 - Ficolin-1 is a soluble pattern recognition molecule synthesized by myeloid cells and capable of activating the lectin pathway of complement on the surface of pathogens. It is tethered to the membranes of monocytes and granulocytes; however, the biological significance of cell-associated ficolin-1 is unknown. Recognition of healthy host cells by a pattern recognition molecule constitutes a potential hazard to self cells and tissues, emphasizing the importance of further elucidating the reported self-recognition. In the current study we investigated the potential recognition of lymphocytes by ficolin-1 and demonstrated that CD56(dim) NK-cells and both CD4(+) and CD8(+) subsets of activated T-cells were recognized by ficolin-1. In contrast we did not detect binding of ficolin-1 to CD56(bright) NK-cells, NKT-cells, resting T-cells or B-cells. Furthermore, we showed that the protein-lymphocyte interaction occurred via the pathogen-recognition domain of ficolin-1 to sialic acid on the cell surface. Thus, the differential binding of ficolin-1 to lymphocyte subsets suggests ficolin-1 as a novel link between innate and adaptive immunity. Our results provide new insight about the recognition properties of ficolin-1 and point toward additional immune modulating functions of the molecule besides its role in pathogen recognition.

AB - Ficolin-1 is a soluble pattern recognition molecule synthesized by myeloid cells and capable of activating the lectin pathway of complement on the surface of pathogens. It is tethered to the membranes of monocytes and granulocytes; however, the biological significance of cell-associated ficolin-1 is unknown. Recognition of healthy host cells by a pattern recognition molecule constitutes a potential hazard to self cells and tissues, emphasizing the importance of further elucidating the reported self-recognition. In the current study we investigated the potential recognition of lymphocytes by ficolin-1 and demonstrated that CD56(dim) NK-cells and both CD4(+) and CD8(+) subsets of activated T-cells were recognized by ficolin-1. In contrast we did not detect binding of ficolin-1 to CD56(bright) NK-cells, NKT-cells, resting T-cells or B-cells. Furthermore, we showed that the protein-lymphocyte interaction occurred via the pathogen-recognition domain of ficolin-1 to sialic acid on the cell surface. Thus, the differential binding of ficolin-1 to lymphocyte subsets suggests ficolin-1 as a novel link between innate and adaptive immunity. Our results provide new insight about the recognition properties of ficolin-1 and point toward additional immune modulating functions of the molecule besides its role in pathogen recognition.

KW - Adaptive Immunity

KW - Antigens, CD56

KW - CD4-Positive T-Lymphocytes

KW - CD8-Positive T-Lymphocytes

KW - Humans

KW - Immunity, Innate

KW - Killer Cells, Natural

KW - Lectins

KW - Lymphocyte Activation

KW - Lymphocyte Subsets

KW - Natural Killer T-Cells

KW - Protein Binding

KW - Sialic Acids

U2 - 10.1016/j.molimm.2013.09.006

DO - 10.1016/j.molimm.2013.09.006

M3 - Journal article

C2 - 24161415

VL - 57

SP - 181

EP - 190

JO - Molecular Immunology

JF - Molecular Immunology

SN - 0161-5890

IS - 2

ER -

ID: 138735853