Plant lectins are major tools in studies of the protein-carbohydrate interactions that play a key role in establishing the specificity of a wide variety of biological recognition and communication events. These carbohydrate binding proteins have also been used for a variety of medical purposes, including blood typing, separation of populations of lymphocytes prior to bone marrow transplantation, targeted drug delivery and various diagnostic assays. It is the long term goal of this research to determine the relationship of plant lectin structure to function. Such information should enhance the utilization and versatility of lectins as tools, provide basic information on protein-carbohydrate interactions and help determine the role of such proteins in oligosaccharide signaling and other recognition events in both plants and animals. The present investigation focuses on a new category of lectins, named LNP, with both carbohydrate binding and apyrase activities. Members of this LNP lectin category are present on the surfaces of legume root hairs and have been found to play a role in the oligosaccharide recognition events that initiate the nitrogen-fixing symbiosis that occurs between rhizobia and legumes. Similarities in sequence suggest that other members of this category of lectins may be present in a wide variety of plants and animals and raise the possibility that they may participate in highly conserved oligosaccharide signaling processes.
The specific aims of this proposal are: (1) to determine the range of carbohydrate specificities found among members of this lectin category and the extent of their distribution in the plant and animal kingdoms; (2) to define the structural prerequisites for the carbohydrate binding and enzymatic activities of a representative legume LNP; and (3) to initiate studies to determine the molecular mechanisms by which legume LNPs elicit the activation of downstream events upon binding to their oligosaccharide ligands. This study will employ a variety of methodologies and approaches in studying LNP structure-function relationships, including carbohydrate binding and enzymatic assays, the recombinant expression of individual and combinations of domains and/or regions of this protein, the initiation of X-ray crystallographic studies, the use of site-specific mutations and transgenic analyses of these mutant lectins.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM021882-24
Application #
6351165
Study Section
Pathobiochemistry Study Section (PBC)
Program Officer
Marino, Pamela
Project Start
1978-02-01
Project End
2003-12-31
Budget Start
2001-02-01
Budget End
2002-01-31
Support Year
24
Fiscal Year
2001
Total Cost
$279,635
Indirect Cost
Name
University of California Davis
Department
Anatomy/Cell Biology
Type
Schools of Arts and Sciences
DUNS #
094878337
City
Davis
State
CA
Country
United States
Zip Code
95618
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Etzler, M E (1994) A comparison of the carbohydrate binding properties of two Dolichos biflorus lectins. Glycoconj J 11:395-9

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