IgE-binding Protein Lectin as a Chimeric Gene Product with Homology to an Identification of the Metastasis-associated, Galactoside-binding
نویسندگان
چکیده
We report the complete primary and secondary structures of a metas tasis-associated M, 34,000 galactoside-binding lectin. The polypeptide sequence (264 amino acids) was derived from the nucleotide sequence of three overlapping complementary DNA clones isolated from Xgtll and XgtlO phage libraries of UV-induced murine fibrosarcomas. Striking features of the polypeptide sequence are two distinct regions of /3-sheet and globular structures at the amino and carboxy terminals, respectively. Homology search suggests that the polypeptide is a chimeric gene product formed by fusion of the S'-end of an M, -14,000 galactoside-binding lectin with an internal domain of the collagen a gene. Enzymatic treatment with collagenase confirmed the presence of a collagen-like structure in the polypeptide. Unexpectedly, the entire sequence is >85% homologous to a rat low affinity IgE-binding protein.
منابع مشابه
Identification of the Metastasis-associated, Galactoside-binding Lectin as a Chimeric Gene Product with Homology to an IgE-binding Protein1
We report the complete primary and secondary structures of a metas tasis-associated M, 34,000 galactoside-binding lectin. The polypeptide sequence (264 amino acids) was derived from the nucleotide sequence of three overlapping complementary DNA clones isolated from Xgtll and XgtlO phage libraries of UV-induced murine fibrosarcomas. Striking features of the polypeptide sequence are two distinct ...
متن کاملMolecular Cloning, Characterization, and Expression of Cuc m 2, a Major Allergen in Cucumis melo
Background: Several studies reported the clinical features of IgE-mediated hypersensitivity after ingestion of melon. Melon allergy is a common IgE-mediated fruit allergy in Iran. This prompted us to investigate immunochemical and molecular properties of the major allergen in melon fruit, to compare the IgE-binding capacity of the natural protein with the recombinant allergen, and to determine ...
متن کاملP 144: Sunflower Mannose binding Lectin-Associated Serine Protease Inhibitor-1 (SFMI-1) and -2: Significant Inhibitors of Mannose binding Lectin Pathway which Helps in Multiple Sclerosis Treatment
One of the important parts of innate immunity is complement system that occurs in three different ways; the classic, the alternative and the lectin pathway. The four pattern recognition molecules that have been identified till now are Mannose binding lectin (MBL), a component of lectin pathway, and three ficolins (ficolin1,-2 and -3) which compound to the carbohydrates of the cell surface. MBL ...
متن کاملCloning and evaluation of gene expression and purification of gene encoding recombinant protein containing binding subunit of coli surface antigens CS1 and CS2 from Enterotoxigenic Escherichia coli
Background & Objective: Enterotoxigenic Escherichia coli (ETEC) is a major causative agent of diarrhea. Enterotoxins and the colonization factors (CFs) are major virulence factors in ETEC infections. The bacterium binds to the intestinal epithelial cell surface through colonization factors and produces enterotoxins that cause excessive fluid and electrolyte secretion in the lumen of the intesti...
متن کاملHuman keratinocytes release the endogenous beta-galactoside-binding soluble lectin immunoglobulin E (IgE-binding protein) which binds to Langerhans cells where it modulates their binding capacity for IgE glycoforms
A better understanding of the pathophysiological role of Langerhans cells (LC) in atopic diseases is dictated by the characterization of the structures involved in immunoglobulin (IgE)-binding on their cell surface. We previously reported that human LC express the high affinity receptor for IgE (Fc epsilon RI), as well as the low affinity receptor for IgE (Fc epsilon RII/CD23). In the present s...
متن کامل