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Elfeil W.K.,Jilin University | Elfeil W.K.,Suez Canal University | Abouelmaatti R.R.,Jilin University | Abouelmaatti R.R.,Key Laboratory of Animal Epidemiology and Zoonosis | And 12 more authors.
Journal of Animal and Veterinary Advances | Year: 2012

Toll like receptor mediate immune response through recognition of Pathogen-Associated Molecular Patterns (PAMPs) thus play important roles in host defense. Little is known about the Avian Immune System structure and the majority of it based on chicken as a Universal Avian Model while recent researches showed that a lot of factor not common between chicken and other birds. This research aimed to identify and clone the duck TLR4 as a model to Anseriformes species, researchers success to clone a novel functional dTLR4 mRNA and deposit into the NCBI GenBank database where the mRNA consist of 2529 nucleotide and it showed 81 % identity with chicken and 78% identity with zebra finch while showed 95% identity with goose. The translated amino acid showed that the gene consist of 843 amino acid and the transmembrane structure analysis reveal a novel unique LRR motifs in duck and absent in both chicken and zebra finch at the position 56-80 also showed that TIR domain consist of 146 amino acid not 145 like chicken and zebra finch. © 2012 Medwell Journals. Source


Chen Z.,China Agricultural University | Zhang N.,China Agricultural University | Lu S.,China Agricultural University | Tariq M.,China Agricultural University | And 3 more authors.
Acta Crystallographica Section F:Structural Biology Communications | Year: 2015

β2-Microglobulin (β2m) noncovalently associates with the heavy chain of major histocompatibility complex class I (MHC I) molecules, which bind foreign antigen peptides to control the cytotoxic T lymphocyte (CTL) immune response. In contrast to mammals, there are distinct types of β2ms derived from two loci in a number of teleost species. In order to clarify the structures of the β2ms, the zebrafish (Danio rerio) β2ms Dare-β2m-I and Dare-β2m-II were expressed in Escherichia coli, purified and crystallized, and diffraction data were collected to 1.6 and 1.9 Å resolution, respectively. Both crystals belonged to space group P212121. The unit-cell parameters were determined to be a = 38.2, b = 50.4, c = 50.9 Å for Dare-β2m-I and a = 38.9, b = 52.7, c = 65.8 Å for Dare-β2m-II. Each asymmetric unit was constituted of one molecule, with Matthews coefficients of 2.22 and 3.01 Å3 Da-1 and solvent contents of 45 and 59% for Dare-β2m-I and Dare-β2m-II, respectively. These two β2m structures will provide relevant information for further studies of the structures of the MHC I complex. © 2015 International Union of Crystallography. Source


Wang Z.,China Agricultural University | Chen R.,China Agricultural University | Tariq M.,China Agricultural University | Jiang B.,China Agricultural University | And 3 more authors.
Acta Crystallographica Section F:Structural Biology Communications | Year: 2014

In order to clarify the structural characteristics of the bovine MHC class I molecule (BoLA-I) complexed with CD8αα (CD8αα-BoLA-I), bovine CD8αα, BoLA-I (BoLA-202201) and β2m were expressed and purified, and were then assembled with a peptide derived from Foot-and-mouth disease virus (FMDV-VP1YY9) and crystallized. The crystal diffracted to 1.7 Å resolution and belonged to space group P21, with unit-cell parameters a = 53.9, b = 103.8, c = 61.8 Å, α = γ = 90, β = 96°. The asymmetric unit contained one complex, with a Matthews coefficient of 2.41 Å3 Da-1 and a solvent content of 48.9%. The rotation-function Z-score and translation-function Z-score for molecular replacement were 3.4 and 8.9, respectively. In addition, SDS-PAGE analysis of CD8αα-BoLA-I crystals showed three bands corresponding to the molecular weights of BoLA-I heavy chain, β2m and CD8α. The structure of the CD8αα-BoLA-I complex should be helpful in obtaining insight into the interaction between bovine CD8αα and MHC class I molecules. Structure determination of BoLA-202201-FMDV-VP1YY9 will be useful in the design of vaccines for foot-and-mouth disease. © 2014 International Union of Crystallography All rights reserved. Source


Yuan H.,China Agricultural University | Chen R.,China Agricultural University | Liu Y.,China Agricultural University | Tariq M.,China Agricultural University | And 3 more authors.
Acta Crystallographica Section F:Structural Biology Communications | Year: 2014

Complement 1q (C1q) is the first component of the complement system which can initiate the classical complement pathway. In human, C1q is composed of 18 polypeptide chains: six C1qA chains, six C1qB chains and six C1qC chains. Each chain has a signal peptide and is comprised of a collagen-like region and a C-terminal C1q globular domain (C1qgD), which is organized as a heterotrimer. C1qgD can recognize antigen-antibody complexes containing IgG and IgM or can bind directly to the C-reactive protein. Although the classical complement pathway is found from fish to mammals, only the human C1qgD structure has been determined. Compared with that of mammals, fish C1q exhibits similar immune functions and genome arrangement. In order to illustrate the structure of C1qgD in fish, zebrafish (Danio rerio) C1qA globular domain (Dare-C1qAgD) was expressed, purified and crystallized. X-ray diffraction data were collected from a crystal to a resolution of 2.05 Å; the crystal belonged to the orthorhombic space group P212121, with unit-cell parameters a = 50.347, b = 85.059, c = 95.560 Å. It contained three molecules in the asymmetric unit. The Matthews coefficient value V M was 2.31 Å3 Da -1, with a calculated solvent content of 46.7%. The data will help to give insight into the structural basis of C1qA in fish species. © 2014 International Union of Crystallography All rights reserved. Source


Jiang B.,China Agricultural University | Liu Y.,China Agricultural University | Chen R.,China Agricultural University | Wang Z.,China Agricultural University | And 3 more authors.
Acta Crystallographica Section F:Structural Biology Communications | Year: 2014

Amphioxus is regarded as an essential animal model for the study of immune evolution. Discovery of new molecules with the immunoglobulin superfamily (IgSF) variable (V) domain in amphioxus would help in studying the evolution of IgSF V molecules in the immune system. A protein was found which just contains only one IgSF V domain in amphioxus, termed Amphi-IgSF-V; it has over 30% sequence identity to the V domains of human immunoglobulins and mammalian T-cell receptors. In order to clarify the three-dimensional structure of this new molecule in amphioxus, Amphi-IgSF-V was expressed, purified and crystallized, and diffraction data were collected to a resolution of 1.95 Å. The crystal belonged to space group P3221, with unit-cell parameters a = b = 53.9, c = 135.5 Å. The Matthews coefficient and solvent content were calculated to be 2.58 Å3 Da-1 and 52.38%, respectively. The results will provide structural information to study the evolution of IgSF V molecules in the immune system. © 2014 CrossMark. Source

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