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A second uniquely human mutation affecting sialic acid biology.

T Angata1, N M Varki, A Varki

  • 1Glycobiology Research and Training Center, Department of Medicine, University of California at San Diego, 9500 Gilman Dr., La Jolla, CA 92093-0687, USA.

The Journal of Biological Chemistry
|September 8, 2001
PubMed
Summary

Human evolution involved a mutation in Siglec-L1, a sialic acid-binding protein, affecting its function. This change may explain differences in sialic acid expression between humans and other primates.

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Area of Science:

  • Immunology
  • Evolutionary Biology
  • Glycobiology

Background:

  • Sialic acids are key glycoconjugate components recognized by Siglecs (sialic acid-binding immunoglobulin-like lectins).
  • Previously known Siglecs require a conserved arginine for optimal sialic acid binding.

Purpose of the Study:

  • To characterize a human Siglec-like molecule (Siglec-L1) and its evolutionary changes.
  • To investigate the functional impact of a specific mutation on sialic acid recognition.

Main Methods:

  • Comparative genomics analysis of Siglec-L1 across species.
  • Functional assays involving mutation and reintroduction of arginine residue.
  • Expression pattern analysis of Siglec-L1.

Main Results:

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  • Human Siglec-L1 lacks a critical arginine residue essential for sialic acid binding.
  • This loss is due to a single nucleotide substitution unique to the human lineage.
  • Chimpanzee Siglec-L1 is functional, recognizing N-glycolylneuraminic acid, unlike human Siglec-L1.
  • Human Siglec-L1 exhibits a distinct epithelial cell surface expression pattern.

Conclusions:

  • A specific mutation in human Siglec-L1 altered its sialic acid recognition properties, potentially linked to changes in sialic acid expression during human evolution.
  • The evolution of Siglec-L1 and associated sialic acid biology in humans warrants further investigation.