Collectin 11 (CL-11, CL-K1) is a MASP-1/3-associated plasma collectin with microbial-binding activity
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Collectin 11 (CL-11, CL-K1) is a MASP-1/3-associated plasma collectin with microbial-binding activity. / Hansen, Soren; Selman, Lana; Palaniyar, Nades; Ziegler, Karel; Brandt, Jette; Kliem, Anette; Jonasson, Maiken; Skjoedt, Mikkel-Ole; Nielsen, Ole; Hartshorn, Kevan; Jørgensen, Thomas J D; Skjødt, Karsten; Holmskov, Uffe.
In: Journal of immunology (Baltimore, Md. : 1950), Vol. 185, No. 10, 15.11.2010, p. 6096-104.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Collectin 11 (CL-11, CL-K1) is a MASP-1/3-associated plasma collectin with microbial-binding activity
AU - Hansen, Soren
AU - Selman, Lana
AU - Palaniyar, Nades
AU - Ziegler, Karel
AU - Brandt, Jette
AU - Kliem, Anette
AU - Jonasson, Maiken
AU - Skjoedt, Mikkel-Ole
AU - Nielsen, Ole
AU - Hartshorn, Kevan
AU - Jørgensen, Thomas J D
AU - Skjødt, Karsten
AU - Holmskov, Uffe
PY - 2010/11/15
Y1 - 2010/11/15
N2 - Collectins play important roles in the innate immune defense against microorganisms. Recently, a new collectin, collectin 11 (CL-11 or CL-K1), was identified via database searches. In present work, we characterize the structural and functional properties of CL-11. Under nonreducing conditions, in gel permeation chromatography recombinant CL-11 forms disulfide-linked oligomers of 100 and 200 kDa. A mAb-based ELISA estimates the concentration of CL-11 in plasma to be 2.1 μg/ml, and the presence of CL-11 in plasma was further verified by Western blotting and mass spectrometry. Mannan-binding lectin-associated serine protease 1 (MASP-1) copurified with CL-11 and the interaction in plasma with MASP-1 and/or MASP-3 was further demonstrated using ELISA. We identified the adrenal glands, the kidneys, and the liver as primary sites of expression. CL-11 lectin activity was demonstrated by ELISA and showed that CL-11 has preference for l-fucose and d-mannose. We finally show that CL-11 binds to intact bacteria, fungi, and viruses and that CL-11 decreases influenza A virus infectivity and forms complexes with DNA. On the basis of the significant concentration of CL-11 in circulation and CL-11's interaction with various microorganisms and MASP-1 and/or MASP-3, it is conceivable that CL-11 plays a role in activation of the complement system and in the defense against invading microorganisms.
AB - Collectins play important roles in the innate immune defense against microorganisms. Recently, a new collectin, collectin 11 (CL-11 or CL-K1), was identified via database searches. In present work, we characterize the structural and functional properties of CL-11. Under nonreducing conditions, in gel permeation chromatography recombinant CL-11 forms disulfide-linked oligomers of 100 and 200 kDa. A mAb-based ELISA estimates the concentration of CL-11 in plasma to be 2.1 μg/ml, and the presence of CL-11 in plasma was further verified by Western blotting and mass spectrometry. Mannan-binding lectin-associated serine protease 1 (MASP-1) copurified with CL-11 and the interaction in plasma with MASP-1 and/or MASP-3 was further demonstrated using ELISA. We identified the adrenal glands, the kidneys, and the liver as primary sites of expression. CL-11 lectin activity was demonstrated by ELISA and showed that CL-11 has preference for l-fucose and d-mannose. We finally show that CL-11 binds to intact bacteria, fungi, and viruses and that CL-11 decreases influenza A virus infectivity and forms complexes with DNA. On the basis of the significant concentration of CL-11 in circulation and CL-11's interaction with various microorganisms and MASP-1 and/or MASP-3, it is conceivable that CL-11 plays a role in activation of the complement system and in the defense against invading microorganisms.
KW - Amino Acid Sequence
KW - Animals
KW - Base Sequence
KW - Blotting, Western
KW - Chromatography, Gel
KW - Collectins
KW - Enzyme-Linked Immunosorbent Assay
KW - Humans
KW - Immunity, Innate
KW - Immunohistochemistry
KW - Mannose-Binding Protein-Associated Serine Proteases
KW - Mass Spectrometry
KW - Molecular Sequence Data
KW - Reverse Transcriptase Polymerase Chain Reaction
KW - Journal Article
KW - Research Support, Non-U.S. Gov't
U2 - 10.4049/jimmunol.1002185
DO - 10.4049/jimmunol.1002185
M3 - Journal article
C2 - 20956340
VL - 185
SP - 6096
EP - 6104
JO - Journal of Immunology
JF - Journal of Immunology
SN - 0022-1767
IS - 10
ER -
ID: 172399627