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Structure and Function of Mammalian Carbohydrate-Lectin Interactions

  • Reference work entry
Glycoscience

Abstract

Over the past three decades the field of glycobiology has expanded beyond a basic understanding of the structure and biosynthesis of glycoprotein, proteoglycans, and glycolipids toward a more detailed picture of how these molecules afford communication through binding to mammalian lectins. Although the number of different mammalian lectin domains appears to be finite and even much smaller than early estimates predicated based on the diversity of glycan structures, nature appears capable of using these in numerous combinations to fine tune specificity. The following provides an overview of the major classes of mammalian lectins and discusses their glycan binding specificity. The review provides a snapshot of the field of glycobiology that continues to grow providing an increasing number of examples of biological processes that rely upon glycan-lectin binding.

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Abbreviations

CTLDs:

C-type lectin-like domains

CRD:

C-type carbohydrate recognition domains

MBP-A:

mannose-binding protein-A

MBP:

mannose-binding protein

MDCC:

MBP-dependent cell-mediated cytotoxicity

TNF-α:

tumor necrosis factor-α

IL-1:

interleukin-1

LAD-II:

leukocyte adhesion deficiency type II

EGF:

epidermal growth factor-like

CR:

consensus repeat

HUVECs:

human umbilical cord vein endothelial cells

ASGPR:

asialoglycoprotein receptor

HL:

hepatic lectin

RTG-r:

rat testis Gal receptor

CHL:

chicken hepatic lectin

AHL:

alligator hepatic lectin

MMR:

macrophage mannose receptor

LH:

lutropin

DC-SIGN:

dentritic cell specific ICAM-3 grabbing non-integrin

ICAM-3:

integrin cell adhesion molecule 3

M6P:

Man-6-phosphate

IGF-II/CI-MPR:

insulin-like growth factor II/cation-independent M6P receptor

CLC:

Charcot–Leydon crystal protein

HL:

Hodgkin's lymphoma

CRP:

C reactive protein

SAP:

serum amyloid protein

PE:

phosphoethanolamine

PC:

phosphocholine

Ig:

immunoglobulin

SIGLECS:

sialic acid binding immunoglobulin-like lectins

MAG:

myelin-associated glycoprotein

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Acknowledgement

The authors thank V. Hayden Thomas for valuable suggestions and comments on this manuscript. This work was supported by NIH grants AI33189, GM48049 and NIH training grant GM07767.

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Authors and Affiliations

  1. Division of Medicinal and Natural Products Chemistry, College of Pharmacy, University of Iowa, 115 South Grand Avenue, Iowa City, IA, 52242-1112, USA

    Kevin Anderson, David Evers & Kevin G. Rice

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  1. Kevin Anderson
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  2. David Evers
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Editors and Affiliations

  1. Natural Products and Glycotechnology Research Institute Inc., North Caroline State University, 4118 Swarthmore Road, Durham, NC, 27707, USA

    Bertram O. Fraser-Reid Prof. Dr.

  2. University Graduate School of Science and Engineering, 3-4-1 Ohkubo, Shinjuku, Tokyo, Japan

    Kuniaki Tatsuta Prof. Dr.

  3. Faculty of ScienceDepartment of Chemistry, University of Hamburg, Martin-Luther-King-Platz 6, 20146, Hamburg, Germany

    Joachim Thiem Prof. Dr.

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Anderson, K., Evers, D., Rice, K. (2008). Structure and Function of Mammalian Carbohydrate-Lectin Interactions. In: Fraser-Reid, B.O., Tatsuta, K., Thiem, J. (eds) Glycoscience. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-30429-6_63

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