A β-1,3-Glucan-Binding Protein From Manduca sexta

  • Congcong Ma
  • Michael R. Kanost
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 484)


Insects have pattern recognition molecules [1] which can recognize nonself molecules such as β-1,3-glucan, lipopolysaccharide, and peptidoglycan on the surface of invading pathogens. Upon binding to the foreign invaders, pattern recognition proteins further trigger defense pathways such as the prophenoloxidase pathway in insects. Insects thus can defend themselves efficiently against pathogens even though they lack the immunoglobulin system present in mammals.


Recognition Protein Native Molecular Weight Foreign Invader Peptidoglycan Recognition Protein Pattern Recognition Molecule 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Janeway CA Jr., Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harbor Symp Quant Biol 1989; 54:1–13PubMedCrossRefGoogle Scholar
  2. 2.
    Koizumi N, Imamura M, Kadotani T, Yaoi K, Iwahana H, Sato R. The lipopolysaccharide-binding protein participating in hemocyte nodule formation in the silkworm Bombyx mori is a novel member of the C-type lectin superfamily with two different tandem carbohydrate-recognition domains. FEBS Letters 1999; 443:139–143PubMedCrossRefGoogle Scholar
  3. 3.
    Yoshida H, Kinoshita K, Ashida M. Purification of a peptidoglycan recognition protein from hemolymph of the silkworm, Bombyx mori. J Biol Chem 1996; 271: 13854–13860CrossRefGoogle Scholar
  4. 4.
    Ochiai M, Ahida M. A pattern recognition protein for peptidoglycan. J Biol Chem 1999; 274:11854–11858PubMedCrossRefGoogle Scholar
  5. 5.
    Kang D, Liu G, Lundström A, Gelius E, Streiner H. Apeptidoglycan recognition protein in innate immunity conserved from insects to humans. Proc Natl Acad Sci USA 1998; 95:10078–10082PubMedCrossRefGoogle Scholar
  6. 6.
    Ochiai M, Ashida M. Purification of a 5–1,3-glucan recognition protein in the prophenoloxidase activating system from hemolymph of the silkworm, Bombyx mori. J Biol Chem 1988; 263:12056–12062PubMedGoogle Scholar
  7. 7.
    Chen C, Durant HJ, Newton RP, Ratcliffe NA. A study of novel lectins and their involvement in the activation of the prophenoloxidase system in Blaberus discoidalis. Biochem J 1995; 310:23–31PubMedGoogle Scholar
  8. 8.
    Söderhäll K, Ragener W, Söderhäll I, Newton RP, Ratcliffe NA. The properties and purification of a Blaberus craniifer plasma protein which enhances the activation of haemocyte prophenoloxidase by a f3 1,3-glucan. Insect Biochem 1988; 18:323–330CrossRefGoogle Scholar
  9. 9.
    Lee W-J, Lee J-D, Kravchenko VV, Ulevitch RJ, Brey PT. Purification and molecular cloning of an inducible Gram-negative bacteria-binding protein from the silkworm, Bombyx mori. Proc Natl Acad Sci USA 1996; 93:7888–7893PubMedCrossRefGoogle Scholar
  10. 10.
    Bachman ES, McClay DR. Molecular cloning of the first metazoan 3–1,3 glucanase from eggs of the sea urchin Strongylocentrotus purpuratus. Proc Natl Acad Sci USA 1996; 93:6808–6813PubMedCrossRefGoogle Scholar
  11. 11.
    Yahata N, Watanabe T, Nakamura Y, Yamamoto Y, Kamimiya S, Tanaka H. Structure of the gene encoding 13–1,3-glucanase Al of Bacillus circulans WL-12. Gene 1990; 86:113–117PubMedCrossRefGoogle Scholar
  12. 12.
    Lee E, Linder ME, Gilman AG. Expression of G-protein “ subunits in Escherichia coli. Methods Enzymology 1994; 237:146–163CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2001

Authors and Affiliations

  • Congcong Ma
    • 1
  • Michael R. Kanost
    • 1
  1. 1.Department of BiochemistryKansas State UniversityManhattan

Personalised recommendations