Advertisement

Glyconectin Glycans as the Self-Assembling Nano-Molecular-Velcrosystem Mediating Self-Nonself Recognition and Adhesion Implicated in Evolution of Multicellularity

  • Gradimir N. Misevic
  • Nikola Misevic
  • Octavian Popescu
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 738)

Abstract

The goal of this chapter is to make a specific contribution about glyconectin glycan as the self-assembling nano-molecular-velcro system mediating initial steps of self-nonself recognition and cell adhesion in Porifera, the first descendants of the most simple primordial multicellular organisms. Two original findings will be described: (i) Velcro like concept based on highly polyvalent and specific intermolecular glycan to glycan associations with extremely low affinity of the single binding site and (ii) novel structures of the large and newly emerging family of glyconectin like glycan molecules. The emphasis will be put on the interdisciplinary approach for studying structure to function relationship at the different size scale levels by combining the knowledge and technologies (instrumentation and methods) of physics, chemistry, biology and mathematics. Applying such strategy which is crossing the boundaries of different science disciplines enabled us to develop a new Atomic Force Microscopy (AFM) based nano-bio-technology and perform the first quantitative measurements of intermolecular binding forces at the single molecular level under physiological conditions. We propose that nano-velcro systems of the glyconectin glycans, which are the constituents on the cell surface that are the most exposed to the environment, were responsible for the molecular self-nonself recognition and adhesion processes that underpinned the emergence of multicellular life forms.

Keywords

Atomic Force Microscopy Cell Recognition Glycan Structure Recognition Molecule Atomic Force Microscopy Experiment 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 2.
    Dammer U, Popescu O, Wagner P et al. Binding strength between cell adhesion proteoglycans measured by atomic force microscopy. Science 1995; 267:1173–1175.PubMedCrossRefGoogle Scholar
  2. 3.
    Popescu O, Misevic GN. Self-recognition by proteoglycans. Nature 1997; 386:231–232.PubMedCrossRefGoogle Scholar
  3. 4.
    Misevic GN, Guerardel Y, Sumanovski L et al. Molecular recognition between glyconectins as an adhesion self-assembly pathway to multicellularity. J Biol Chem 2004; 279:15579–15590.PubMedCrossRefGoogle Scholar
  4. 5.
    Guerardel Y, Czeszak X, Sumanovski LT et al. Molecular fingerprinting of carbohydrate structure phenotypes of three porifera proteoglycanlike glyconectins. J Biol Chem 2004; 279:15591–15603.PubMedCrossRefGoogle Scholar
  5. 6.
    Forrest S, Perelson AS, Allen L et al. Self Nonself Discrimination in a Computer. Proceedings of 1994 IEEE Symposium on Research in Security and Privacy. 1994.Google Scholar
  6. 7.
    Alberts B, Johnson A, Lewis J et al, eds. Molecular Biology of the Cell. 4th ed. New York and London: Garland Science, 2002.Google Scholar
  7. 8.
    Barclay A. Membrane proteins with immunoglobulin-like domains a master superfamily of interaction molecules. Semin Immunol 2003; 15(4):215–223.PubMedCrossRefGoogle Scholar
  8. 9.
    Hulpiau P, van Roy F. Molecular evolution of the cadherin superfamily. Int J Biochem Cell Biol 2009; 41(2):349–369.PubMedCrossRefGoogle Scholar
  9. 10.
    Humphries MJ. Integrin structure. Biochem Soc Trans 2000; 28(4):311–339.PubMedCrossRefGoogle Scholar
  10. 11.
    Sharon N, Lis H. Lectins. New York: Springer, 2007.CrossRefGoogle Scholar
  11. 12.
    Binnig G, Quare CF, Gerber C. Atomic force microscopy. Phys RevLett 1986; 56:930–937.Google Scholar
  12. 13.
    Bucior I, Scheuring S, Engel A et al. Carbohydrate-carbohydrate interaction provides adhesion force and specificity for cellular recognition. J Cell Biol 1994; 165:529–537.CrossRefGoogle Scholar
  13. 14.
    Lee GU, Kidwell DA, Colton RC. Sensing discrete streptavidin-biotin interactions with atomic force microscopy. Langmuir 1994; 10(2):354–357.CrossRefGoogle Scholar
  14. 15.
    Florin EL, Moy VT, Gaub HE. Adhesion forces between individual ligand-receptor pairs. Science 1994; 264:415–417.PubMedCrossRefGoogle Scholar
  15. 16.
    Janeway CA, Travers P, Walport M et al. Immunobiology. 5th ed. New York and London: Garland Science. 2001.Google Scholar
  16. 17.
    Villarreal LP. Persisting Viruses Could Play Role in Driving Host Evolution. ASM News (American Society for Microbiology) 2001. http://newsarchive.asm.org/oct01/feature1.asp.Google Scholar

Copyright information

© Landes Bioscience and Springer Science+Business Media 2012

Authors and Affiliations

  • Gradimir N. Misevic
    • 1
  • Nikola Misevic
    • 2
  • Octavian Popescu
    • 3
    • 4
  1. 1.Gimmune GmbHZugSwitzerland
  2. 2.Institute of Brain ResearchUniversity of BremenBremenGermany
  3. 3.Molecular Biology Center and Institute for Interdisciplinary Experimental ResearchBabes-Bolyai UniversityCluj-NapocaRumania
  4. 4.Institute of BiologyRomanian AcademyBucharestRumania

Personalised recommendations