Collectins play important roles in innate defence against viral, fungal and bacterial pathogens. CL-43, a bovine serum collectin, which appears to have evolutionarily evolved from surfactant protein D (SP-D), shows unique structural and functional properties. In the present study, we describe the initial characterization of a recombinant CL-43 expressed in mammalian cells. Like natural CL-43, the recombinant is secreted as trimeric forms that show a preference for mannose and N-acetyl mannosamine. The natural and recombinant proteins have significantly higher haemagglutination-inhibiting activity against influenza A virus (IAV) than recombinant trimeric forms of SP-D. In contrast with the more highly multimerized forms of SP-D, namely conglutinin or mannose-binding lectin, CL-43 did not induce viral or bacterial aggregation and did not enhance IAV-induced neutrophil H2O2 generation. Like SP-D, CL-43 also strongly enhanced neutrophil uptake of IAV. However, the mechanism of this enhanced internalization is different from that of SP-D in that it did not require viral aggregation. These studies establish that the trimeric structure of CL-43 is specified by its primary sequence and indicate that this naturally occurring trimeric collectin has unique antiviral activities. These findings could facilitate the development of recombinant collectins with novel antimicrobial properties.
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August 2002
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Research Article|
August 15 2002
Distinctive anti-influenza properties of recombinant collectin 43
Kevan L. HARTSHORN;
Kevan L. HARTSHORN
1
∗Department of Medicine, Boston University School of Medicine, EBRC 414, 650 Albany Street, Boston, MA 02118, U.S.A.
1To whom correspondence should be addressed (e-mail Khartsho@bu.edu).
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Uffe HOLMSKOV;
Uffe HOLMSKOV
†Department of Immunology and Microbiology, University of Southern Denmark, Odense, Denmark
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Soren HANSEN;
Soren HANSEN
†Department of Immunology and Microbiology, University of Southern Denmark, Odense, Denmark
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Pengnian ZHANG;
Pengnian ZHANG
‡Department of Pathology, Washington University School of Medicine, St. Louis, MO, U.S.A.
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Joseph MESCHI;
Joseph MESCHI
∗Department of Medicine, Boston University School of Medicine, EBRC 414, 650 Albany Street, Boston, MA 02118, U.S.A.
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Tirsit MOGUES;
Tirsit MOGUES
∗Department of Medicine, Boston University School of Medicine, EBRC 414, 650 Albany Street, Boston, MA 02118, U.S.A.
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Mitchell R. WHITE;
Mitchell R. WHITE
∗Department of Medicine, Boston University School of Medicine, EBRC 414, 650 Albany Street, Boston, MA 02118, U.S.A.
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Erika C. CROUCH
Erika C. CROUCH
‡Department of Pathology, Washington University School of Medicine, St. Louis, MO, U.S.A.
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Publisher: Portland Press Ltd
Received:
December 20 2001
Revision Received:
April 12 2002
Accepted:
April 24 2002
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London ©2002
2002
Biochem J (2002) 366 (1): 87–96.
Article history
Received:
December 20 2001
Revision Received:
April 12 2002
Accepted:
April 24 2002
Citation
Kevan L. HARTSHORN, Uffe HOLMSKOV, Soren HANSEN, Pengnian ZHANG, Joseph MESCHI, Tirsit MOGUES, Mitchell R. WHITE, Erika C. CROUCH; Distinctive anti-influenza properties of recombinant collectin 43. Biochem J 15 August 2002; 366 (1): 87–96. doi: https://doi.org/10.1042/bj20011868
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