PURPOSE: To determine the differences in clinical characteristics, blood chemistry and coronary artery complications between patients with Kawasaki disease who received intravenous immunoglobulin (IVIG) within the fourth day of illness and after the fifth day of illness. METHODS: A retrospective chart review was conducted of all children with Kawasaki disease who were admitted to Ewha Mokdong Hospital between January 2001 and June 2002. The early treatment group received IVIG within the fourth day of illness(n=34) and the control group received IVIG after the fifth day of illness(n=53). Clinical manifestations, fever duration, hospitalization days, CBC, blood chemistry and coronary artery complications were compared between two groups. RESULTS: No demographic differences were noted between the two groups(P>0.05). Total duration of fever was significantly shorter in the early treatment group than the control group(4.8+/-2.5 days vs 7.4+/-3.0 days, P<0.05), but there were no differences in fever duration after IVIG treatment and hospitalization days between two groups(P>0.05). No significant differences were noted in the level of hemoglobin, WBC, ESR, CRP, AST, ALT and albumin between two groups(P>0.05). No significant differences in the incidence of IVIG retreatment were noted between the two groups(11.8% vs 5.7%, P>0.05). No significant differences in the incidence of coronary artery complications were noted between the two groups(11.7% vs 18.9%, P>0.05). No significant differences in the recurrence rate were noted between the two groups(3% vs 2%, P>0.05). CONCLUSION: Early IVIG treatment in patients with Kawasaki disease reduces the total fever duration. Coronary artery complications were not increased in patients with early IVIG treatment.
Chemistry ; Child ; Coronary Vessels ; Fever ; Hospitalization ; Humans ; Immunoglobulins* ; Immunoglobulins, Intravenous ; Incidence ; Mucocutaneous Lymph Node Syndrome* ; Recurrence ; Retreatment ; Retrospective Studies

Animals ; Antibodies ; chemistry ; genetics ; Genetic Engineering ; Humans ; Immunoglobulins ; genetics ; Immunohistochemistry ; Protein Engineering

OBJECTIVETo prepare artificial antigens and anti-citrinin egg yolk-derived immunoglobulin (IgY) to build an enzyme-linked immunosorbent assay (ELISA) for citrinin (CTN).

METHODSCTN was conjugated with bovine serum albumin (BSA), ovalbumin (OVA) with formaldehyde condensation method to prepare artificial antigens and identified by ultraviolet (UV) spectrometry and Infrared (IR) spectrometry. Artificial antigens for CTN and anti-CTN IgY were purified with polyethylene glycol two-step precipitation method and identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). ELISA with IgY was established. Cross-reactivity of IgY with various structural similarities to CTN and possible co-occurrence with CTN in agricultural commodities were studied.

RESULTSUV and IR absorption spectra suggested that CTN was correlated with the carrier protein of BSA or OVA. SDS-PAGE patterns showed that the anti-CTN IgY was almost pure with a molecular weight of approximate 100 KD. The indirect competitive ELISA showed that the detection limit of CTN was 10 ng x mL(-1), with a good linearity ranging 20-640 ng x mL(-1).

CONCLUSIONArtificial antigens of CTN can be successfully synthesized. The established ELISA can be used to determine CTN- contaminated samples.

Animals ; Antibody Specificity ; Antigens ; chemistry ; Chickens ; Citrinin ; chemistry ; Egg Yolk ; immunology ; Enzyme-Linked Immunosorbent Assay ; methods ; Female ; Immunoglobulins ; immunology

Immunoglobulin Y (IgY) is an effective orally administered antibody used to protect against various intestinal pathogens, but which cannot tolerate the acidic gastric environment. In this study, IgY was microencapsulated by alginate (ALG) and coated with chitooligosaccharide (COS). A response surface methodology was used to optimize the formulation, and a simulated gastrointestinal (GI) digestion (SGID) system to evaluate the controlled release of microencapsulated IgY. The microcapsule formulation was optimized as an ALG concentration of 1.56% (15.6 g/L), COS level of 0.61% (6.1 g/L), and IgY/ALG ratio of 62.44% (mass ratio). The microcapsules prepared following this formulation had an encapsulation efficiency of 65.19%, a loading capacity of 33.75%, and an average particle size of 588.75 μm. Under this optimum formulation, the coating of COS provided a less porous and more continuous microstructure by filling the cracks on the surface, and thus the GI release rate of encapsulated IgY was significantly reduced. The release of encapsulated IgY during simulated gastric and intestinal digestion well fitted the zero-order and first-order kinetics functions, respectively. The microcapsule also allowed the IgY to retain 84.37% immune-activity after 4 h simulated GI digestion, significantly higher than that for unprotected IgY (5.33%). This approach could provide an efficient way to preserve IgY and improve its performance in the GI tract.
Alginic Acid/chemistry* ; Chitin/chemistry* ; Chitosan ; Delayed-Action Preparations ; Digestion ; Drug Compounding ; Drug Liberation ; Gastrointestinal Tract/metabolism* ; Immunoglobulins/metabolism* ; Oligosaccharides

Homophilic interaction of the L1 family of cell adhesion molecules plays a pivotal role in regulating neurite outgrowth and neural cell networking in vivo. Functional defects in L1 family members are associated with neurological disorders such as X-linked mental retardation, multiple sclerosis, low-IQ syndrome, developmental delay, and schizophrenia. Various human tumors with poor prognosis also implicate the role of L1, a representative member of the L1 family of cell adhesion molecules, and ectopic expression of L1 in fibroblastic cells induces metastasis-associated gene expression. Previous studies on L1 homologs indicated that four N-terminal immunoglobulin-like domains form a horseshoe-like structure that mediates homophilic interactions. Various models including the zipper, domain-swap, and symmetry-related models are proposed to be involved in structural mechanism of homophilic interaction of the L1 family members. Recently, cryo-electron tomography of L1 and crystal structure studies of neurofascin, an L1 family protein, have been performed. This review focuses on recent discoveries of different models and describes the possible structural mechanisms of homophilic interactions of L1 family members. Understanding structural mechanisms of homophilic interactions in various cell adhesion proteins should aid the development of therapeutic strategies for L1 family cell adhesion molecule-associated diseases.
Cell Adhesion ; Crystallography, X-Ray ; Escherichia coli ; Humans ; Immunoglobulins/chemistry ; Neural Cell Adhesion Molecule L1/*chemistry/*metabolism ; *Neurites/chemistry/metabolism ; Protein Conformation ; *Protein Interaction Domains and Motifs

OBJECTIVETo obtain egg yolk antibody in hen eggs laid by hens immunized with the protein of Porphyromonas gingivalis (Pg). To generate, purify IgY against Pg (anti-Pg-IgY) and identify its specificity.

METHODSPgATCC33277 was cultured under standard anaerobic conditions and harvested after proliferation. Then Pg was extracted by sonication until the cell pellets were shattered completely. After centrifugatiton, the supernatant was collected. Five-month-old Roman hens were immunized for egg antibody production. The antibody was inoculated intramuscularly and subcutaneously in the breast from multiple spot with 1.0 ml of a vaccine consisting of oil-adjuvant protein which was mixed with 1 ml protein of Pg and 1 ml Freund's adjuvant complete every 10 days, for 4 times. The eggs were collected after the first immunization and stored at 4°C. The anti-Pg-IgY was extracted and purified. The protein concentration was tested by bicinchoninic acid (BCA), the specificity of IgY analyzed by SDS polyacrylamide gel electrophoresis (SDS-PAGE), the titre of IgY and its physicochemical character were evaluated by indirect enzyme-linked immunosorbent assay.

RESULTSThe concentration of obtained anti-Pg-IgY was 2.05 g/L. SDS-PAGE analysis of the anti-Pg-IgY showed that the molecular weight of IgY was consistent with the theoretical value. Protein of anti-Pg-IgY appeared approximately 5 days after the first immunization, and reached the peak at 50 - 55 days. Antibody titres reached 1:100 000. Each egg produced more than 10 mg IgY, and its purification was up to 95% as well.

CONCLUSIONSLayer hens immuned by Pg may provide specific IgY of high titre and high concentration. The antibody has high purity and is heat, acid and alkali-resistant.

Animals ; Antibodies ; chemistry ; immunology ; Chickens ; immunology ; Egg Yolk ; chemistry ; immunology ; Electrophoresis, Polyacrylamide Gel ; Enzyme-Linked Immunosorbent Assay ; Immunization ; Immunoglobulins ; chemistry ; immunology ; isolation & purification ; Porphyromonas gingivalis ; immunology

Leukocyte immunoglobulin-like receptors (LILRs), also called CD85s, ILTs, or LIRs, are important mediators of immune activation and tolerance that contain tandem immunoglobulin (Ig)-like folds. There are 11 (in addition to two pseudogenes) LILRs in total, two with two Ig-like domains (D1D2) and the remaining nine with four Ig-like domains (D1D2D3D4). Thus far, the structural features of the D1D2 domains of LILR proteins are well defined, but no structures for the D3D4 domains have been reported. This is a very important field to be studied as it relates to the unknown functions of the D3D4 domains, as well as their relative orientation to the D1D2 domains on the cell surface. Here, we report the crystal structures of the D3D4 domains of both LILRB1 and LILRB2. The two Ig-like domains of both LILRB1-D3D4 and LILRB2-D3D4 are arranged at an acute angle (∼60°) to form a bent structure, resembling the structures of natural killer inhibitory receptors. Based on these two D3D4 domain structures and previously reported D1D2/HLA I complex structures, two alternative models of full-length (four Ig-like domains) LILR molecules bound to HLA I are proposed.
Amino Acid Sequence ; Antigens, CD ; chemistry ; Crystallography, X-Ray ; Histocompatibility Antigens Class I ; chemistry ; Humans ; Immunoglobulins ; chemistry ; Leukocyte Immunoglobulin-like Receptor B1 ; Membrane Glycoproteins ; chemistry ; Models, Molecular ; Peptides ; chemistry ; metabolism ; Protein Binding ; Protein Structure, Tertiary ; Receptors, Immunologic ; chemistry ; Signal Transduction

Serum aspartate aminotransferase (AST) is a common enzyme for the evaluation of the hepatic, muscular and cardiac diseases and is produced also at kidney, brain, pancreas, lung, leukocytes, erythrocytes, etc. The elevation of its activity is usually caused by the necrosis of hepatocytes when there are not muscular injuries or myopathies. Recently, it is found that AST can exist as a macroenzyme by forming a complex with an immunoglobulin and this complex is erroneously considered to indicate the presence of liver disease as a result of elevation of AST activity on routine blood chemistry analysis. We experienced the patient with isolated AST elevation due to the formation of AST-mmunoglobulin complex confirmed by AST isoenzyme electrophoresis (EP).
Aspartate Aminotransferases ; Brain ; Chemistry ; Electrophoresis ; Erythrocytes ; Heart Diseases ; Hepatocytes ; Humans ; Immunoglobulins ; Kidney ; Leukocytes ; Liver Diseases ; Lung ; Muscular Diseases ; Necrosis ; Pancreas

Ig superfamily (IgSF) constitutes the largest superfamily in human genome. In particular, Ig-like domains are the most abundant structural module within cell surface receptors, functioning in nervous as well as immune system. Here I describe some key sequence signature of an I-set Ig-like domain from known structures of IgSF members. These signature residues define the I-set Ig-like domain, which should aid structural and functional studies of cell surface receptors.
Amino Acid Sequence ; Humans ; Hydrogen Bonding ; Immunoglobulins ; chemistry ; metabolism ; Molecular Sequence Data ; Protein Folding ; Protein Structure, Tertiary

The prevalent ages at onset for Kawasaki Disease (KD) and Epstein-Barr virus (EBV) infection are known to be similar in Korea and Japan. We evaluated the correlation between EBV infection and KD. The antibodies to EBV such as anti-viral capsid antigen (VCA) IgG and IgM, anti-diffuse and restricted early antigen IgG (anti-EADR IgG), and the anti-EBV determined nuclear antigen IgG (anti-EBNA IgG) were examined in 29KD patients at five separate times sequentially during a period of one year, and also in 14 other children with a past history of KD. The results of each group were compared with those of age-matched controls. The positive rates of anti-VCA IgG and IgM at presentation in the KD patients were 41.4% (12/29) and 0% (0/29), respectively. Only one patient was found to be anti-VCA IgM-positive within two months. There were no cases of anti-VCA IgG except one, anti-EADR IgG and anti-EBNA IgG positive to negative seroconversion during the year. The children with a past history of KD showed higher anti-EBNA IgG-positive rates than the controls (p=0.04). There was no difference in the seropositive rates of the antibodies to EBV, cytomegalovirus, herpes simplex virus and herpes zoster virus. In conclusion, children with KD were noted to have normal immune responses to EBV infection. Children with a past history of KD seemed to be infected with EBV at a later age than children with no history of KD.
Mucocutaneous Lymph Node Syndrome/*virology ; Male ; Korea ; Infant ; Immunoglobulins/metabolism ; Immunoglobulin M/chemistry ; Immunoglobulin G/chemistry ; Humans ; Herpesvirus 4, Human/*metabolism ; Female ; Epstein-Barr Virus Infections/*complications ; Child, Preschool ; Antibodies, Viral/*chemistry ; Age of Onset