title: Characterization and comparative analyses of two amphioxus intelectins involved in the innate immune response.
abstract: Intelectin is a new type of soluble galactofuranose-binding lectin involved in innate immunity. Here we report another intelectin homolog, AmphiITLN239631, obtained from amphioxus, the transitional form between vertebrates and invertebrates. AmphiITLN239631 encoded 396 amino acids with a highly conserved fibrinogen-related domain (FReD), An intelectin domain and a putative Collagen domain. AmphiITLN239631 was ubiquitously expressed in all tissues we tested and transcripts in skin increased after challenge of both Escherichia coli and Staphylococcus aureus, although in different levels. Recombinant AmphiITLN239631 expressed in E. coli system could agglutinate both Gram-positive and Gram-negative bacteria in a calcium independent manner. Furthermore, recombinant protein was able to bind to lipopolysaccharide (LPS) and peptidoglycan (PGN), the major components of Gram-positive and Gram-negative bacteria cell walls, respectively. We also compared AmphiITLN239631 with previously identified AmphiITLN71469 and found that their tissue specificities, expression patterns upon bacteria challenge, and polysaccharide-binding affinities etc vary considerably. Our results could provide insight into the evolution and function of the intelectin family.
authors: Marine Biotechnology Research Center, Shandong Provincial Key Laboratory of Animal Cells and Developmental Biology, Institute of Developmental Biology, School of Life Sciences, Shandong University, Jinan, Shandong 250100, PR China.
authors: Jie
authors: J
authors: Yan
authors: Changqing
authors: C
authors: Zhang
authors: Yan
authors: Y
authors: Zhang
authors: Kailin
authors: K
authors: Li
authors: Lingxiao
authors: L
authors: Xu
authors: Lanboling
authors: L
authors: Guo
authors: Yu
authors: Y
authors: Kong
authors: Lijun
authors: L
authors: Feng
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002816:Chordata, Nonvertebrate / Q000737:chemistry / Q000235:genetics* / Q000276:immunology* / Q000378:metabolism; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000502:physiology; D019143:Evolution, Molecular; D006023:Glycoproteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D037102:Lectins / Q000737:chemistry / Q000235:genetics* / Q000276:immunology* / Q000378:metabolism; D008070:Lipopolysaccharides / Q000378:metabolism; D008969:Molecular Sequence Data; D009928:Organ Specificity; D010457:Peptidoglycan / Q000378:metabolism; D010802:Phylogeny; D012313:RNA / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D016415:Sequence Alignment; D013211:Staphylococcus aureus / Q000502:physiology
chemical_list: D018076:DNA, Complementary; D006023:Glycoproteins; D037102:Lectins; D008070:Lipopolysaccharides; D010457:Peptidoglycan; D011994:Recombinant Proteins; D012313:RNA