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Jens Christian Jensenius

Collections and ficolins: humoral lectins of the innate immune defense

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Collections and ficolins: humoral lectins of the innate immune defense. / Holmskov, Uffe; Thiel, Steffen; Jensenius, Jens Christian.

In: Annual Review of Immunology, Vol. 21, 2003, p. 547-78.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

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Holmskov, Uffe ; Thiel, Steffen ; Jensenius, Jens Christian. / Collections and ficolins: humoral lectins of the innate immune defense. In: Annual Review of Immunology. 2003 ; Vol. 21. pp. 547-78.

Bibtex

@article{fbc93e9a4b4147f4a1a21cfe009846be,
title = "Collections and ficolins: humoral lectins of the innate immune defense",
abstract = "Collectins and ficolins, present in plasma and on mucosal surfaces, are humoral molecules of the innate immune systems, which recognize pathogen-associated molecular patterns. The human collectins, mannan-binding lectin (MBL) and surfactant protein A and D (SP-A and SP-D), are oligomeric proteins composed of carbohydrate-recognition domains (CRDs) attached to collagenous regions and are thus structurally similar to the ficolins, L-ficolin, M-ficolin, and H-ficolin. However, they make use of different CRD structures: C-type lectin domains for the collectins and fibrinogen-like domains for the ficolins. Upon recognition of the infectious agent, MBL and the ficolins initiate the lectin pathway of complement activation through attached serine proteases (MASPs), whereas SP-A and SP-D rely on other effector mechanisms: direct opsonization, neutralization, and agglutination. This limits the infection and concurrently orchestrates the subsequent adaptive immune response. Deficiencies of the proteins may predispose to infections or other complications, e.g., reperfusion injuries or autoimmune diseases. Structure, function, clinical implications, and phylogeny are reviewed.",
keywords = "Animals, Bacteria, Carrier Proteins, Collectins, Complement Activation, Fungi, Humans, Immunity, Innate, Lectins, Mannose-Binding Lectin, Mannose-Binding Protein-Associated Serine Proteases, Mice, Models, Molecular, Phylogeny, Polymorphism, Genetic, Pulmonary Surfactant-Associated Protein A, Pulmonary Surfactant-Associated Protein D, Receptors, Immunologic, Serine Endopeptidases, Viruses",
author = "Uffe Holmskov and Steffen Thiel and Jensenius, {Jens Christian}",
year = "2003",
doi = "10.1146/annurev.immunol.21.120601.140954",
language = "English",
volume = "21",
pages = "547--78",
journal = "Annual Review of Immunology",
issn = "0732-0582",
publisher = "Annual Reviews",

}

RIS

TY - JOUR

T1 - Collections and ficolins: humoral lectins of the innate immune defense

AU - Holmskov, Uffe

AU - Thiel, Steffen

AU - Jensenius, Jens Christian

PY - 2003

Y1 - 2003

N2 - Collectins and ficolins, present in plasma and on mucosal surfaces, are humoral molecules of the innate immune systems, which recognize pathogen-associated molecular patterns. The human collectins, mannan-binding lectin (MBL) and surfactant protein A and D (SP-A and SP-D), are oligomeric proteins composed of carbohydrate-recognition domains (CRDs) attached to collagenous regions and are thus structurally similar to the ficolins, L-ficolin, M-ficolin, and H-ficolin. However, they make use of different CRD structures: C-type lectin domains for the collectins and fibrinogen-like domains for the ficolins. Upon recognition of the infectious agent, MBL and the ficolins initiate the lectin pathway of complement activation through attached serine proteases (MASPs), whereas SP-A and SP-D rely on other effector mechanisms: direct opsonization, neutralization, and agglutination. This limits the infection and concurrently orchestrates the subsequent adaptive immune response. Deficiencies of the proteins may predispose to infections or other complications, e.g., reperfusion injuries or autoimmune diseases. Structure, function, clinical implications, and phylogeny are reviewed.

AB - Collectins and ficolins, present in plasma and on mucosal surfaces, are humoral molecules of the innate immune systems, which recognize pathogen-associated molecular patterns. The human collectins, mannan-binding lectin (MBL) and surfactant protein A and D (SP-A and SP-D), are oligomeric proteins composed of carbohydrate-recognition domains (CRDs) attached to collagenous regions and are thus structurally similar to the ficolins, L-ficolin, M-ficolin, and H-ficolin. However, they make use of different CRD structures: C-type lectin domains for the collectins and fibrinogen-like domains for the ficolins. Upon recognition of the infectious agent, MBL and the ficolins initiate the lectin pathway of complement activation through attached serine proteases (MASPs), whereas SP-A and SP-D rely on other effector mechanisms: direct opsonization, neutralization, and agglutination. This limits the infection and concurrently orchestrates the subsequent adaptive immune response. Deficiencies of the proteins may predispose to infections or other complications, e.g., reperfusion injuries or autoimmune diseases. Structure, function, clinical implications, and phylogeny are reviewed.

KW - Animals

KW - Bacteria

KW - Carrier Proteins

KW - Collectins

KW - Complement Activation

KW - Fungi

KW - Humans

KW - Immunity, Innate

KW - Lectins

KW - Mannose-Binding Lectin

KW - Mannose-Binding Protein-Associated Serine Proteases

KW - Mice

KW - Models, Molecular

KW - Phylogeny

KW - Polymorphism, Genetic

KW - Pulmonary Surfactant-Associated Protein A

KW - Pulmonary Surfactant-Associated Protein D

KW - Receptors, Immunologic

KW - Serine Endopeptidases

KW - Viruses

U2 - 10.1146/annurev.immunol.21.120601.140954

DO - 10.1146/annurev.immunol.21.120601.140954

M3 - Journal article

C2 - 12524383

VL - 21

SP - 547

EP - 578

JO - Annual Review of Immunology

JF - Annual Review of Immunology

SN - 0732-0582

ER -