scholarly journals IL35 modulation altered survival, cytokine environment and histopathological consequences during malaria infection in mice

2019 ◽  
Vol 18 (1) ◽  
Author(s):  
Ramatu Omenesa Bello ◽  
Maizaton Atmadini Abdullah ◽  
Roslaini Abd Majid ◽  
Voon Kin Chin ◽  
Mohammed Faruq Abd Rachman Isnadi ◽  
...  
Keyword(s):  
Plasmodium Berghei ◽  
Malaria Infection ◽  
Time Course ◽  
Systemic Circulation ◽  
Enzyme Linked Immunosorbent Assay ◽  
Therapeutic Modalities ◽  
Barr Virus ◽  
Cytokine Activation ◽  
Human Disorders ◽  
Epstein Barr

Abstract Background The immune modulating potential of IL-35 in multiple human disorders has been reported. Consequent upon the recognition of inflammatory cytokine activation and its preponderance for mediating pathology during malaria infection, the study aimed to characterize the expression and functional contribution(s) of IL-35 in Plasmodium berghei (strain ANKA) infected mice. Methods Plasmodium berghei infection in male ICR mice was used as the rodent model of choice. The time course of IL-35 expression in the systemic circulation and tissues of P. berghei infected mice as well as their healthy control counterparts was assessed by enzyme linked immunosorbent assay and immunohistochemistry respectively. The effect of modulating IL-35 by recombinant IL-35 protein or neutralizing anti-Epstein-Barr virus-induced gene 3 antibody on the cytokine environment during P. berghei infection was assessed by flow cytometry. Furthermore, the influence of modulating IL-35 on histopathological hallmarks of malaria and disease progression was evaluated. Results Interleukin-35 was significantly up regulated in serum and tissues of P. berghei infected mice and correlated with parasitaemia. Neutralization of IL-35 significantly enhanced the release of IFN-γ, decreased the expression of IL-6 and decreased parasitaemia patency. Neutralization of IL-35 was also associated with a tendency towards increased survival as well as the absence of pathological features associated with malaria infection unlike recombinant IL-35 protein administration which sustained a normal course of infection and unfavourable malaria associated histological outcomes in P. berghei infected mice. Conclusion These results indicate the involvement of IL-35 in P. berghei induced malaria infection. IL-35 neutralization strategies may represent viable therapeutic modalities beneficial for the resolution of malaria infection.

scholarly journals Production and nucleotide sequence of an inhibitory human IgM autoantibody directed against platelet glycoprotein Ia/IIa

Blood ◽  
1994 ◽  
Vol 84 (6) ◽  
pp. 1968-1974 ◽  
Author(s):  
H Deckmyn ◽  
J Zhang ◽  
E Van Houtte ◽  
J Vermylen
Keyword(s):  
Platelet Aggregation ◽  
Cell Lines ◽  
Lupus Erythematosus ◽  
Gene Segment ◽  
Platelet Glycoprotein ◽  
Enzyme Linked Immunosorbent Assay ◽  
Germline Gene ◽  
Barr Virus ◽  
Epstein Barr ◽  
Human B Cell

Abstract Human B-cell lines were derived by limiting dilutions of Epstein-Barr virus (EBV) transformed peripheral B cells from a patient with an autoantibody against glycoprotein (GP)Ia/IIa, and manifesting defective collagen-induced platelet aggregation and a bleeding problem. Antibody- producing clones were selected for their reactivity with whole platelets or with affinity-purified GPIa/IIa by enzyme-linked immunosorbent assay (ELISA). One of these cell lines, selected for further evaluation, produced an IgM (E3G6) that interfered with platelet aggregation responses. Polymerase chain reaction (PCR) amplifications with two different sets of primers specific for human kappa-chains resulted in the rescue of a unique and identical sequence. The same was true for the mu-chain, from which it was concluded that the cell line was monoclonal. Further analysis showed that the kappa variable domain sequence is similar to the germline gene A30, to 2E7, an anti-GPIIb human autoantibody, and to HF2–1/17, a systemic lupus erythematosus (SLE)-associated broad-specificity human autoantibody. Thus, the specificity of our antibody, E3G6, appears to be determined by the mu-chain, the sequence of which is encoded by a VHIII gene segment strongly homologous to the germline gene DP-77, by a D gene that is not homologous to any of the germline D genes reported to date, and by JH4 gene segment that is germline. All four mutations versus DP- 77 are in CDRs, and result in amino acid substitutions, which implies that E3G6 may have been derived from an antigen-driven response.

scholarly journals Purified Hexameric Epstein-Barr Virus-Encoded BARF1 Protein for Measuring Anti-BARF1 Antibody Responses in Nasopharyngeal Carcinoma Patients

2010 ◽  
Vol 18 (2) ◽  
pp. 298-304 ◽  
Author(s):  
E. K. Hoebe ◽  
S. H. Hutajulu ◽  
J. van Beek ◽  
S. J. Stevens ◽  
D. K. Paramita ◽  
...  
Keyword(s):  
Nasopharyngeal Carcinoma ◽  
Epstein Barr Virus ◽  
Antibody Responses ◽  
Enzyme Linked Immunosorbent Assay ◽  
Humoral Immune ◽  
Barr Virus ◽  
Humoral Immune Responses ◽  
Human Sera ◽  
Epstein Barr ◽  
Humoral Responses

ABSTRACTWHO type III nasopharyngeal carcinoma (NPC) is highly prevalent in Indonesia and 100% associated with Epstein-Barr virus (EBV). NPC tumor cells express viral proteins, including BARF1, which is secreted and is considered to have oncogenic and immune-modulating properties. Recently, we found conserved mutations in the BARF1 gene in NPC isolates. This study describes the expression and purification of NPC-derived BARF1 and analyzes humoral immune responses against prototype BARF1 (B95-8) and purified native hexameric BARF1 in sera of Indonesian NPC patients (n= 155) compared to healthy EBV-positive (n= 56) and EBV-negative (n= 16) individuals. BARF1 (B95-8) expressed inEscherichia coliand baculovirus, as well as BARF1-derived peptides, did not react with IgG or IgA antibodies in NPC. Purified native hexameric BARF1 protein isolated from culture medium was used in enzyme-linked immunosorbent assay (ELISA) and revealed relatively weak IgG and IgA responses in human sera, although it had strong antibody responses to other EBV proteins. Higher IgG reactivity was found in NPC patients (P= 0.015) than in regional Indonesian controls or EBV-negative individuals (P< 0.001). IgA responses to native BARF1 were marginal. NPC sera with the highest IgG responses to hexameric BARF1 in ELISA showed detectable reactivity with denatured BARF1 by immunoblotting. In conclusion, BARF1 has low immunogenicity for humoral responses and requires native conformation for antibody binding. The presence of antibodies against native BARF1 in the blood of NPC patients provides evidence that the protein is expressed and secreted as a hexameric protein in NPC patients.

Enzyme-linked immunosorbent assay for the detection of Epstein-Barr Virus-Induced Antigens and antibodies

1983 ◽  
Vol 63 (2) ◽  
pp. 171-185 ◽  
Author(s):  
Lars Sternås ◽  
Janos Luka ◽  
Bengt Kallin ◽  
Anders Rosén ◽  
Werner Henle ◽  
...  
Keyword(s):  
Immunosorbent Assay ◽  
Epstein Barr Virus ◽  
Enzyme Linked Immunosorbent Assay ◽  
Barr Virus ◽  
Epstein Barr

scholarly journals One percent of human circulating B lymphocytes are capable of producing the natural anti-Gal antibody

Blood ◽  
1993 ◽  
Vol 82 (8) ◽  
pp. 2485-2493 ◽  
Author(s):  
U Galili ◽  
F Anaraki ◽  
A Thall ◽  
C Hill-Black ◽  
M Radic
Keyword(s):  
B Lymphocytes ◽  
Blood Group ◽  
Enzyme Linked Immunosorbent Assay ◽  
Barr Virus ◽  
Effective System ◽  
Group A ◽  
Igh Gene Rearrangement ◽  
Epstein Barr ◽  
B Lymphoid ◽  
Group B

The natural anti-Gal antibody constitutes 1% of circulating IgG in humans and interacts specifically with the carbohydrate epitope Gal alpha 1–3Gal beta 1–4GlcNAc-R (the alpha-galactosyl epitope). In view of the unusually large amounts of this antibody in the serum, it was of interest to determine the proportion of circulating B lymphocytes capable of synthesizing anti-Gal. For this purpose, blood B lymphocytes were incubated with Epstein-Barr virus (EBV) and plated in microtiter wells. Proliferation of the EBV transformed B lymphocytes was readily visible after 3 weeks of incubation. The supernatants from wells containing proliferating B-lymphoid clones were assayed for anti-Gal by an agglutination assay with rabbit red blood cells and the specificity of the agglutinating antibodies was further confirmed by their interaction with synthetic oligosaccharides and by enzyme-linked immunosorbent assay with glycoproteins. Approximately 5% of the wells contained anti-Gal antibodies. Limiting dilution studies and IgH gene rearrangement patterns suggested that each well contained an average of five proliferating B-lymphoid clones. Thus, it is concluded that approximately 1% of circulating B lymphocytes are capable of producing anti-Gal. The proportion of anti-Gal--producing lymphoid clones exceeds by fourfold that of clones producing anti-blood group A or anti-blood group B antibodies. Individual anti-Gal clones display fine variations in their combining site, as indicated by their differential interaction with alpha-galactosyl epitopes on glycolipids and on N-linked carbohydrate chains of glycoproteins. The high frequency of precursor B lymphocytes capable of producing anti-Gal, found in every individual and the restricted specificity of this antibody to alpha-galactosyl epitopes, potentially makes anti-Gal--producing lymphocytes an effective system for studying human Ig genes involved in the natural immune response to structurally defined haptens.

Detection of Antibodies to Epstein-Barr Virus Antigens by Enzyme-Linked Immunosorbent Assay

1982 ◽  
Vol 146 (6) ◽  
pp. 734-740 ◽  
Author(s):  
Ralph F. Hopkins ◽  
Tracy J. Witmer ◽  
Russell H. Neubauer ◽  
Harvey Rabin
Keyword(s):  
Immunosorbent Assay ◽  
Epstein Barr Virus ◽  
Enzyme Linked Immunosorbent Assay ◽  
Barr Virus ◽  
Virus Antigens ◽  
Epstein Barr

Epstein-Barr virus-specific antibody response in cerebrospinal fluid and serum of patients with multiple sclerosis

2010 ◽  
Vol 16 (7) ◽  
pp. 883-887 ◽  
Author(s):  
Massimiliano Castellazzi ◽  
Carmine Tamborino ◽  
Alice Cani ◽  
Elena Negri ◽  
Eleonora Baldi ◽  
...  
Keyword(s):  
Multiple Sclerosis ◽  
Cerebrospinal Fluid ◽  
Neurological Disorders ◽  
Epstein Barr Virus ◽  
Serum Levels ◽  
Nuclear Antigen ◽  
Enzyme Linked Immunosorbent Assay ◽  
Barr Virus ◽  
Epstein Barr ◽  
Multiple Sclerosis Patients

Cerebrospinal fluid and serum levels and intrathecal synthesis of anti-Epstein—Barr virus (EBV) IgG were measured by enzyme-linked immunosorbent assay in 80 relapsing—remitting multiple sclerosis patients grouped according to clinical and magnetic resonance imaging (MRI) evidence of disease activity. Eighty patients with other inflammatory neurological disorders (OIND) and 80 patients with non-inflammatory neurological disorders (NIND) served as neurological controls. Cerebrospinal fluid concentrations were higher in OIND than in multiple sclerosis ( p < 0.0001) and NIND ( p < 0.01) for anti-viral-capsid-antigen (anti-VCA) IgG, in multiple sclerosis than in NIND ( p < 0.01) and in OIND than in NIND ( p < 0.05) for anti-EBV nuclear antigen-1 (EBNA-1) IgG. Serum levels were more elevated in OIND than in multiple sclerosis ( p < 0.05) and in MRI inactive than in MRI active multiple sclerosis ( p < 0.0001) for anti-VCA IgG, and in multiple sclerosis than in OIND and NIND ( p < 0.01) for anti-EBNA-1 IgG. Serum titres of anti-VCA and anti-EBNA-1 IgG were also positively ( p < 0.05) and inversely ( p < 0.001) correlated, respectively, with the Expanded Disability Status Scale. An intrathecal IgG production of anti-VCA and anti-EBNA-1 IgG, as indicated by Antibody Index, was present only in a limited number of multiple sclerosis patients and controls (range from 1.3 to 6.3%). These findings do not support a direct pathogenetic role of EBV-targeted humoral immune response in multiple sclerosis.

scholarly journals Interleukin 13 Is Secreted by and Stimulates the Growth of Hodgkin and Reed-Sternberg Cells

1999 ◽  
Vol 189 (12) ◽  
pp. 1939-1946 ◽  
Author(s):  
Ursula Kapp ◽  
Wen-Chen Yeh ◽  
Bruce Patterson ◽  
Andrew J. Elia ◽  
David Kägi ◽  
...  
Keyword(s):  
Cell Line ◽  
Cell Lines ◽  
Expression Patterns ◽  
Neutralizing Antibody ◽  
Enzyme Linked Immunosorbent Assay ◽  
Barr Virus ◽  
Non Hodgkin Lymphoma ◽  
Dependent Inhibition ◽  
Dose Dependent Inhibition ◽  
Epstein Barr

Gene expression patterns can provide vital clues to the pathogenesis of neoplastic diseases. We investigated the expression of 950 genes in Hodgkin's disease (HD) by analyzing differential mRNA expression using microarrays. In two independent microarray experiments, the HD-derived cell lines L428 and KMH2 were compared with an Epstein-Barr virus (EBV)-immortalized lymphoblastoid B cell line, LCL-GK. Interleukin (IL)-13 and IL-5 were found to be highly expressed in the HD-derived cell lines. Examination of IL-13 and IL-5 expression by Northern blot analysis and enzyme-linked immunosorbent assay confirmed these results and revealed the expression of IL-13 in a third HD-derived cell line, HDLM2. Control LCL and EBV-negative non-Hodgkin lymphoma–derived cell lines did not express IL-13. In situ hybridization of lymph node tissue from HD patients showed that elevated levels of IL-13 were specifically expressed by Hodgkin/Reed-Sternberg (H/RS) tumor cells. Treatment of a HD-derived cell line with a neutralizing antibody to IL-13 resulted in a dose-dependent inhibition of H/RS cell proliferation. These data suggest that H/RS cells produce IL-13 and that IL-13 plays an important role in the stimulation of H/RS cell growth, possibly by an autocrine mechanism. Modulation of the IL-13 signaling pathway may be a logical objective for future therapeutic strategies.

scholarly journals Development and Evaluation of an Epstein-Barr Virus (EBV) Immunoglobulin M Enzyme-Linked Immunosorbent Assay Based on the 18-Kilodalton Matrix Protein for Diagnosis of Primary EBV Infection

1998 ◽  
Vol 36 (11) ◽  
pp. 3359-3361 ◽  
Author(s):  
K. H. Chan ◽  
R. X. Luo ◽  
H. L. Chen ◽  
M. H. Ng ◽  
W. H. Seto ◽  
...  
Keyword(s):  
Immunosorbent Assay ◽  
Epstein Barr Virus ◽  
Matrix Protein ◽  
Immunoglobulin M ◽  
Enzyme Linked Immunosorbent Assay ◽  
Clinical Specimens ◽  
Barr Virus ◽  
Ebv Infection ◽  
Igm Elisa ◽  
Epstein Barr

A new immunoglobulin M (IgM) enzyme-linked immunosorbent assay (ELISA) based on the recombinant Epstein-Barr virus (EBV) matrix protein was developed. Compared to indirect immunofluorescence for the detection of IgM antibody to the EBV capsid antigen on clinical specimens, the sensitivity and specificity of the new IgM ELISA were 96 and 96%, respectively.

scholarly journals Production and nucleotide sequence of an inhibitory human IgM autoantibody directed against platelet glycoprotein Ia/IIa

Blood ◽  
1994 ◽  
Vol 84 (6) ◽  
pp. 1968-1974
Author(s):  
H Deckmyn ◽  
J Zhang ◽  
E Van Houtte ◽  
J Vermylen
Keyword(s):  
Platelet Aggregation ◽  
Cell Lines ◽  
Lupus Erythematosus ◽  
Gene Segment ◽  
Platelet Glycoprotein ◽  
Enzyme Linked Immunosorbent Assay ◽  
Germline Gene ◽  
Barr Virus ◽  
Epstein Barr ◽  
Human B Cell

Human B-cell lines were derived by limiting dilutions of Epstein-Barr virus (EBV) transformed peripheral B cells from a patient with an autoantibody against glycoprotein (GP)Ia/IIa, and manifesting defective collagen-induced platelet aggregation and a bleeding problem. Antibody- producing clones were selected for their reactivity with whole platelets or with affinity-purified GPIa/IIa by enzyme-linked immunosorbent assay (ELISA). One of these cell lines, selected for further evaluation, produced an IgM (E3G6) that interfered with platelet aggregation responses. Polymerase chain reaction (PCR) amplifications with two different sets of primers specific for human kappa-chains resulted in the rescue of a unique and identical sequence. The same was true for the mu-chain, from which it was concluded that the cell line was monoclonal. Further analysis showed that the kappa variable domain sequence is similar to the germline gene A30, to 2E7, an anti-GPIIb human autoantibody, and to HF2–1/17, a systemic lupus erythematosus (SLE)-associated broad-specificity human autoantibody. Thus, the specificity of our antibody, E3G6, appears to be determined by the mu-chain, the sequence of which is encoded by a VHIII gene segment strongly homologous to the germline gene DP-77, by a D gene that is not homologous to any of the germline D genes reported to date, and by JH4 gene segment that is germline. All four mutations versus DP- 77 are in CDRs, and result in amino acid substitutions, which implies that E3G6 may have been derived from an antigen-driven response.

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