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Sialic acids as ligands in recognition phenomena

A Varki1

  • 1Cancer Center, University of California, San Diego, La Jolla 92093-0687, USA.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|March 1, 1997
PubMed
Summary

Sialic acids, found on cell surfaces, can mediate or block cell interactions. This review details proteins that bind sialic acids, highlighting structural needs for recognition.

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Area of Science:

  • Biochemistry
  • Glycobiology
  • Molecular Biology

Background:

  • Sialic acids are acidic monosaccharides at the terminal positions of glycoconjugate sugar chains.
  • Their negative charge can influence cell interactions, and they serve as ligands for various binding proteins.

Purpose of the Study:

  • To summarize proteins that recognize and bind sialic acids.
  • To compare and contrast the structural requirements and binding mechanisms for sialic acid recognition.

Main Methods:

  • Literature review and comparative analysis of protein-sialic acid interactions.
  • Focus on C-type lectins (selectins), I-type lectins (CD22, sialoadhesin), and complement protein H.

Main Results:

  • Sialic acid recognition is influenced by structural variations, linkage, sugar chain structure, and glycoconjugate type.
  • Specific examples include selectins, CD22, sialoadhesin, and complement protein H, each with distinct binding preferences.
  • The sialic acid side chain and modifications like 9-O-acetylation are crucial for recognition by certain lectins and proteins.

Conclusions:

  • Diverse proteins recognize sialic acids through varied structural mechanisms.
  • Understanding these interactions is key to deciphering cellular communication and immune responses.
  • Further research into sialic acid modifications and their binding partners will reveal new biological insights.

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