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Abstract

Sialic acids (Sias) are typically found as terminal monosaccharides attached to cell surface glycoconjugates. They play many important roles in many physiological and pathological processes, including microbe binding that leads to infections, regulation of the immune response, the progression and spread of human malignancies and in certain aspects of human evolution. This review will provide some examples of these diverse roles of Sias and briefly address immunohistochemical approaches to their detection.

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Avian flu: influenza virus receptors in the human airway.

Kyoko Shinya, Masahito Ebina, Shinya Yamada … (2006)

Although more than 100 people have been infected by H5N1 influenza A viruses, human-to-human transmission is rare. What are the molecular barriers limiting human-to-human transmission? Here we demonstrate an anatomical difference in the distribution in the human airway of the different binding molecules preferred by the avian and human influenza viruses. The respective molecules are sialic acid linked to galactose by an alpha-2,3 linkage (SAalpha2,3Gal) and by an alpha-2,6 linkage (SAalpha2,6Gal). Our findings may provide a rational explanation for why H5N1 viruses at present rarely infect and spread between humans although they can replicate efficiently in the lungs.

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Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins.

Ajit Varki (2007)

All cells in nature are covered by a dense and complex array of carbohydrates. Given their prominence on cell surfaces, it is not surprising that these glycans mediate and/or modulate many cellular interactions. Proteins that bind sialic acid, a sugar that is found on the surface of the cell and on secreted proteins in vertebrates, are involved in a broad range of biological processes, including intercellular adhesion, signalling and microbial attachment. Studying the roles of such proteins in vertebrates has improved our understanding of normal physiology, disease and human evolution.

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History of lectins: from hemagglutinins to biological recognition molecules.

Nathan Sharon, Halina Lis (2004)

The occurrence in nature of erythrocyte-agglutinating proteins has been known since the turn of the 19th century. By the 1960s it became apparent that such proteins also agglutinate other types of cells, and that many of them are sugar-specific. These cell-agglutinating and sugar-specific proteins have been named lectins. Although shown to occur widely in plants and to some extent also in invertebrates, very few lectins had been isolated until the early 1970s, and they had attracted little attention. This attitude changed with the demonstration that lectins are extremely useful tools for the investigation of carbohydrates on cell surfaces, in particular of the changes that the latter undergo in malignancy, as well as for the isolation and characterization of glycoproteins. In subsequent years numerous lectins have been isolated from plants as well as from microorganisms and animals, and during the past two decades the structures of hundreds of them have been established. Concurrently, it was shown that lectins function as recognition molecules in cell-molecule and cell-cell interactions in a variety of biological systems. Here we present a brief account of 100-plus years of lectin research and show how these proteins have become the focus of intense interest for biologists and in particular for the glycobiologists among them.

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PubMed ID:: 17632542

DOI:: 10.1038/labinvest.3700656

ScienceOpen disciplines: Chemistry

Keywords: Animals,Gangliosides,Humans,Immunohistochemistry,Lectins,immunology,Neoplasms,Organ Specificity,physiology,Sialic Acid Binding Immunoglobulin-like Lectins,Sialic Acids,analysis,chemistry

Diversity in cell surface sialic acid presentations: implications for biology and disease.

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Most cited references 46

Avian flu: influenza virus receptors in the human airway.

Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins.

History of lectins: from hemagglutinins to biological recognition molecules.

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