This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hartshorn, K. L.
Right arrow Articles by Crouch, E. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hartshorn, K. L.
Right arrow Articles by Crouch, E. C.

 Previous Article  |  Next Article 

Infection and Immunity, November 2002, p. 6129-6139, Vol. 70, No. 11
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.11.6129-6139.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Contributions of the N- and C-Terminal Domains of Surfactant Protein D to the Binding, Aggregation, and Phagocytic Uptake of Bacteria

Kevan L. Hartshorn,1* Mitchell R. White,1 and Erika C. Crouch2

Department of Medicine, Boston University School of Medicine, Boston, Massachussets,1 Department of Pathology, Washington University School of Medicine, St. Louis, Missouri2

Received 8 March 2002/ Returned for modification 29 May 2002/ Accepted 15 August 2002

Collectins play important roles in host defense against infectious microorganisms. We now demonstrate that the serum collectins mannose-binding lectin (MBL) and conglutinin have less ability to bind to, aggregate, and enhance neutrophil uptake of several strains of gram-negative and gram-positive bacteria than pulmonary surfactant protein D (SP-D). Collectins are composed of four major structural domains (i.e., N-terminal, collagen, and neck and carbohydrate recognition domains). To determine which domains of SP-D are responsible for its greater bacterial binding or aggregating activity, activities of chimeric collectins containing the N-terminal and collagen domains of SP-D coupled to the neck recognition domains and carbohydrate recognition domains (CRD) of MBL or conglutinin (SP-D/Congneck+CRD and SP-D/MBLneck+CRD) were tested. The SP-D/Congneck+CRD and SP-D/MBLneck+CRD chimeras bound to and aggregated the bacteria more strongly than did wild-type MBL or conglutinin. SP-D/MBLneck+CRD also enhanced neutrophil uptake of bacteria more so than MBL. Hence, the SP-D N-terminal and/or collagen domains contribute to the enhanced bacterial binding and aggregating activities of SP-D. In prior studies, SP-D/Congneck+CRD and SP-D/MBLneck+CRD had increased ability to bind to influenza virus compared not only with that of conglutinin or MBL but with that of wild-type SP-D as well. In contrast, the chimeras had either reduced or unchanged ability to bind to or aggregate bacteria compared to that of wild-type SP-D. Hence, although replacement of the neck recognition domains and CRDs of SP-D with those of MBL and conglutinin conferred increased viral binding activity, it did not favorably affect bacterial binding activity, suggesting that requirements for optimal collectin binding to influenza virus and bacteria differ.

* Corresponding author. Mailing address: Boston University School of Medicine, EBRC 414, 650 Albany St., Boston, MA 02118. Phone: (617) 638-5638. Fax: (617) 638-7530. E-mail: Khartsho{at}bu.edu.

Editor: J. D. Clements

Infection and Immunity, November 2002, p. 6129-6139, Vol. 70, No. 11
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.11.6129-6139.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Bulmer, M. S., Bachelet, I., Raman, R., Rosengaus, R. B., Sasisekharan, R. (2009). Targeting an antimicrobial effector function in insect immunity as a pest control strategy. Proc. Natl. Acad. Sci. USA 106: 12652-12657 [Abstract] [Full Text]  
  • Hansen, S., Lo, B., Evans, K., Neophytou, P., Holmskov, U., Wright, J. R. (2007). Surfactant Protein D Augments Bacterial Association but Attenuates Major Histocompatibility Complex Class II Presentation of Bacterial Antigens. Am. J. Respir. Cell Mol. Bio. 36: 94-102 [Abstract] [Full Text]  
  • Watanabe, A., Miyazawa, S., Kitami, M., Tabunoki, H., Ueda, K., Sato, R. (2006). Characterization of a Novel C-Type Lectin, Bombyx mori Multibinding Protein, from the B. mori Hemolymph: Mechanism of Wide-Range Microorganism Recognition and Role in Immunity. J. Immunol. 177: 4594-4604 [Abstract] [Full Text]  
  • Kingma, P. S., Zhang, L., Ikegami, M., Hartshorn, K., McCormack, F. X., Whitsett, J. A. (2006). Correction of Pulmonary Abnormalities in Sftpd-/- Mice Requires the Collagenous Domain of Surfactant Protein D. J. Biol. Chem. 281: 24496-24505 [Abstract] [Full Text]  
  • Hall-Stoodley, L., Watts, G., Crowther, J. E., Balagopal, A., Torrelles, J. B., Robison-Cox, J., Bargatze, R. F., Harmsen, A. G., Crouch, E. C., Schlesinger, L. S. (2006). Mycobacterium tuberculosis Binding to Human Surfactant Proteins A and D, Fibronectin, and Small Airway Epithelial Cells under Shear Conditions.. Infect. Immun. 74: 3587-3596 [Abstract] [Full Text]  
  • Hartshorn, K. L., White, M. R., Tecle, T., Holmskov, U., Crouch, E. C. (2006). Innate Defense against Influenza A Virus: Activity of Human Neutrophil Defensins and Interactions of Defensins with Surfactant Protein D.. J. Immunol. 176: 6962-6972 [Abstract] [Full Text]  
  • Meschi, J., Crouch, E. C., Skolnik, P., Yahya, K., Holmskov, U., Leth-Larsen, R., Tornoe, I., Tecle, T., White, M. R., Hartshorn, K. L. (2005). Surfactant protein D binds to human immunodeficiency virus (HIV) envelope protein gp120 and inhibits HIV replication. J. Gen. Virol. 86: 3097-3107 [Abstract] [Full Text]  
  • Schaeffer, L. M., McCormack, F. X., Wu, H., Weiss, A. A. (2004). Interactions of Pulmonary Collectins with Bordetella bronchiseptica and Bordetella pertussis Lipopolysaccharide Elucidate the Structural Basis of Their Antimicrobial Activities. Infect. Immun. 72: 7124-7130 [Abstract] [Full Text]  
  • Oberley, R. E., Ault, K. A., Neff, T. L., Khubchandani, K. R., Crouch, E. C., Snyder, J. M. (2004). Surfactant proteins A and D enhance the phagocytosis of Chlamydia into THP-1 cells. Am. J. Physiol. Lung Cell. Mol. Physiol. 287: L296-L306 [Abstract] [Full Text]  
  • Hirche, T. O., Crouch, E. C., Espinola, M., Brokelman, T. J., Mecham, R. P., DeSilva, N., Cooley, J., Remold-O'Donnell, E., Belaaouaj, A. (2004). Neutrophil Serine Proteinases Inactivate Surfactant Protein D by Cleaving within a Conserved Subregion of the Carbohydrate Recognition Domain. J. Biol. Chem. 279: 27688-27698 [Abstract] [Full Text]  
  • Jounblat, R., Kadioglu, A., Iannelli, F., Pozzi, G., Eggleton, P., Andrew, P. W. (2004). Binding and Agglutination of Streptococcus pneumoniae by Human Surfactant Protein D (SP-D) Vary between Strains, but SP-D Fails To Enhance Killing by Neutrophils. Infect. Immun. 72: 709-716 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»