Glycobiology Advance Access published online on July 13, 2005
Glycobiology, doi:10.1093/glycob/cwj008
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1 Departments of Medicine and Cellular & Molecular Medicine Glycobiology Research and Training Center, University of California, San Diego, La Jolla, CA 92093, USA
* To whom correspondence should be addressed. Animal glycan-recognizing proteins can be broadly classified into two groups - lectins (which typically contain an evolutionarily conserved carbohydrate-recognition domain); and sulfated glycosaminoglycan-binding proteins (which appear to have evolved by convergent evolution). Proteins other than antibodies and T cell receptors that mediate glycan recognition via immunoglobulin (Ig)-like domains are called ‘I-type lectins’. The major homologous subfamily of I-type lectins with sialic acid binding properties and characteristic amino-terminal structural features are called the ‘Siglecs’ (Sialic acid-recognizing Ig-superfamily lectins). The Siglecs can be divided into two groups: an evolutionarily conserved sub-group (Siglecs-1, -2 and -4); and a CD33/Siglec 3-related sub-group (Siglecs 3 and 5-13 in primates), which appear to be rapidly evolving. This paper provides an overview of historical and current information about the Siglecs.
Received April 25, 2005
Revised July 2, 2005
Accepted July 2, 2005
Article
Siglecs - the Major Sub-family of I-type Lectins
2 Research Center for Glycoscience, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki 305-8568, Japan
Ajit Varki, E-mail: varkiadmin{at}ucsd.edu
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