Animal Lectins: A Functional View by Gerardo R. Vasta PhD, Hafiz Ahmed PhD

By Gerardo R. Vasta PhD, Hafiz Ahmed PhD

Introduces Groundbreaking methods for Assessing Lectin Function

Lectins and their ligands are lower than relatively a heavy microscope as a result of their power purposes to pharmacology, immunology, melanoma treatment, and agriculture. With transforming into curiosity within the glycobiology box, the physique of study regarding lectin roles has grown at an explosive fee, rather some time past twenty years. Animal Lectins: A sensible View provides the main up to date research of those carbohydrate-binding, and very likely lifesaving, proteins in a single finished quantity.

This standard-setting source provides new insights into the organic roles of so much animal lectins, together with their functionality in an infection prevention via innate immunity. It additionally discusses such lectin behaviors as:

  • Glycoprotein folding
  • Sorting and targeting
  • Cell adhesion
  • Embryogenesis
  • Cell-cell interactions and signaling

Describes the Structural foundation of Protein-Carbohydrate Interactions

Under the editorial counsel of 2 best protein chemistry specialists and with contributions from well-recognized box specialists, this publication logically and systematically discusses either intracellular and extracellular lectin features. it's an important springboard for destiny box study and a transparent and concise wisdom base that glycobiology, biochemistry, and immunology researchers can't find the money for to be without.

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Additional info for Animal Lectins: A Functional View

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The author describes in a functional context the structure of the NK cell surface receptors of the C-type lectin superfamily and their complex with the major histocompatibility complex (MHC) Class I or Class I-like molecules that have been resolved through high-resolution x-ray crystallography. In Chapter 26, Yu and Kanost discuss the roles of a family of C-type lectins (immulectins) in innate immunity of tobacco hornworm. Immulectins serve as PRRs and bind to structural molecular patterns, generally termed pathogen-associated molecular patterns, present on the surface of most microorganisms but not on the host cells.

263, 9557–9560. 21. N. E. 2005 The C-type lectin-like domain superfamily. FEBS J. 272, 6179–6217. 22. L. 1998 The ice-binding site of Atlantic herring antifreeze protein corresponds to the carbohydrate-binding site of C-type lectins. Biochemistry 37, 4080–4085. 23. Drickamer, K. B. 1999 C-Type lectin-like domains in Caenorhabditis elegans: Predictions from the complete genome sequence. Glycobiology 9, 1357–1369. 24. N. 2002 Galectinomics: Finding themes in complexity. Biochim. Biophys. Acta. 1572, 209–231.

A brief overview of the role of FREPs in internal defense across the animal phyla is provided. The discovery and basic structural features of FREPs and their roles in defense responses against trematodes are discussed. Kamhawi and Valenzuela (Chapter 33) describe lectins in sand fly–Leishmania interactions and hypothesize that the lectin–Leishmania interactions may be necessary for a successful infection in the fly. In Chapter 34, Matsushita et al. discuss the structural basis for recognition plasticity of ficolins, a family of proteins that have both collagen-like and fibrinogen-like domains with a carbohydrate specificity for N-acetylglucosamine.

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