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E M Zhou

Publications and source records attributed to E M Zhou.

31 records · Page 2Linked to original sources

Comparison of Freund's adjuvant and TiterMax in inducing anti-idiotype to idiotypic antibodies against pseudorabies virus antigens.

Freund's adjuvant (FA) and TiterMax (TM) were compared for their effectiveness in the induction of the anti-idiotypic antibodies (anti-Id or Ab2) in pigs, goats and mice against swine polyclonal anti-pseudorabies virus (PRV) antibodies (Ab1) by sequential immunization procedures. Both adjuvants had similar effects on inducing anti-swine immunoglobulin antibodies in the animals. However, high levels of the anti-Id were only generated in animals that received FA. Serological characterization of the anti-Id antisera indicated that internal image anti-Id (Ab2 beta) was generated that recognized shared idiotype (IdX) on the antibodies to PRV. The internal image Ab2 was capable of blocking the anti-PRV antibodies from binding to the PRV antigens, and their interaction with anti-PRV antibodies could be inhibited by PRV antigens.

Animals↗

Internal image rabbit anti-idiotypic antibody detects sheep antibodies to the bluetongue virus core protein VP7.

BACKGROUND: Rabbit polyclonal anti-idiotypic antibodies (anti-Id) were generated against three murine monoclonal antibodies (MAbs) specific for the group-specific antigen VP7 of bluetongue virus (BTV) by the sequential immunization method. It was demonstrated by serological tests that part of the anti-Id possesses the characteristics of internal image anti-Id. By affinity purification against the individual MAbs, the internal image anti-Id, designated RAb2-A, was isolated and identified as specific for the MAb, M1875. OBJECTIVES: To examine the ability of RAb2-A to detect sheep anti-VP7 antibodies by recognition of the common idiotype (Idx). STUDY DESIGN: Affinity-purified RAb2-A IgG, along with VP7, was applied on the solid-phase of ELISA plate and the membrane for Western blot analysis to detect anti-VP7 antibodies from sheep that were immunized with VP7 or were experimentally infected with BTV. An inhibition ELISA was employed to determine whether sheep anti-VP7 and M1875 recognize the same or similar epitope(s). RESULTS: RAb2-A recognised the Idx on anti-VP7 antibodies from sheep that were either immunized with VP7 or experimentally infected with BTV. Specificity of the reaction was confirmed by the observation that RAb2-A did not react with normal sheep serum or sheep antibodies against epizootic haemorrhagic disease of deer virus, a bluetongue-related disease virus in the Orbivirus genus. CONCLUSION: The ability of RAb2-A to detect anti-VP7 antibodies through recognition of the Idx suggests that RAb2-A can be used as a probe to detect anti-BTV antibodies.

Animals↗

Anti-idiotypic antibody as potential serodiagnostic reagent for detection of bluetongue virus infection.

Polyclonal anti-idiotypic antibodies (anti-Ids) were generated by the sequential immunization of rabbits with three mouse monoclonal antibodies (MAb1s) specific for a major bluetongue virus (BTV) protein, VP7. The anti-Ids, designated RAb2s, recognized idiotopes which were located within or near the antigen-combining sites of the MAb1s and were associated with both heavy and light chains of MAb1s. RAb2s inhibited the MAb1s from binding to BTV antigens, and their interaction with MAb1s was inhibited by BTV antigens. By recognizing the common idiotopes, RAb2s detected anti-BTV antibodies from bovine antisera; their interaction was also partially inhibited by BTV antigens. These results indicated that RAb2s recognized the common idiotopes on anti-VP7 antibodies obtained from mice and cattle and that at least a portion of RAb2s were internal-image anti-Ids that functionally mimicked VP7. RAb2s may be used to substitute for the tissue culture-derived viral antigen in currently used serological assays for the detection of antibodies to BTV.

Animals↗

Regulation of levels of serum antibodies to ryegrass pollen allergen Lol pIV by an internal image anti-idiotypic monoclonal antibody.

A murine monoclonal anti-idiotypic antibody (anti-Id), designated B1/1, was produced against an idiotope of a murine antibody (mAb91), which recognizes the epitope, site A, of allergen Lol pIV, one of the major groups of allergens in ryegrass (Lolium perenne) pollen. The ability of B1/1 to modulate the antibody responses to Lol pIV was investigated in murine model systems. In the first system, B1/1-keyhole limpet haemocyanin (KLH) conjugate was administered to treat three different strains of mice (C57BL/6, BALB/c and C3H). In the second and third model systems, a solution of B1/1 in phosphate-buffered saline (PBS) was used to treat syngeneic BALB/c mice at various doses and time intervals, respectively. The treatment with either form of B1/1, administered at doses ranging from 100 ng to 100 micrograms mouse, resulted in a reduction of the levels of the antibodies to Lol pIV. In particular, the level of IgE antibodies to Lol pIV was greatly reduced. The administration of a single intravenous (i.v.) injection of a solution of B1/1 8 weeks prior to the challenge with Lol pIV was still effective in reducing the level of antibodies to the allergen. Moreover, the level of antibodies to Lol pIV that expressed the idiotope mAb91 was also markedly decreased. By contrast, it was observed that the level of antibodies to Lol pIV in mice pretreated with B1/1 in PBS at a dose of 10 ng/mouse increased (albeit slightly) compared to that in mice treated with control mAb. These experimental models lend themselves for investigating the mechanism(s) by which an anti-Id modulates antibody responses to a grass pollen allergen.

Allergens↗

Anti-idiotypic antibodies generated by sequential immunization detect the shared idiotype on antibodies to pseudorabies virus antigens.

Anti-idiotypic antibodies (anti-Id or Ab2) were generated in Balb/c mice against either mouse monoclonal or swine polyclonal antibodies (Ab1) to pseudorabies virus (PRV) antigens by conventional and sequential immunization methods. In the conventional method, one antibody preparation was repeatedly injected into the animals, whereas three anti-PRV antibody preparations were used alternately for the sequential immunization procedure. Anti-Ids were serologically characterized for possession of the Ab2s that detect shared idiotype (IdX) on antibodies to PRV antigens. Only the Ab2s that were generated by the sequential immunization method recognized the IdX present on murine and swine antibodies to PRV. The sequential immunization method described herein was anticipated to be helpful for generating virus specific Ab2s as candidates for serodiagnostic reagents or vaccines.

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A murine monoclonal anti-idiotypic antibody detects a common idiotope on human, mouse and rabbit antibodies to allergen Lol p IV.

A syngeneic mouse monoclonal anti-idiotypic antibody (anti-Id), designated as B1/1, was generated against a monoclonal antibody (MoAb 91) specific for Ryegrass pollen allergen Lol p IV. This anti-Id recognized an idiotope (Id) that was also present on other monoclonal antibodies with the same specificity as MoAb 91. Observations that (i) the anti-Id inhibited the binding of MoAb 91 to Lol p IV and (ii) the Id-anti-Id interaction could be inhibited by Lol p IV indicated that the Id was located within or near the antigen combining site. These properties served to characterize B1/1 as an internal image anti-Id. Evidence that an immune response in different species to Lol p IV elicits the formation of antibodies which express a common Id was provided by the observations that (i) the Id-anti-Id interactions could be inhibited by mouse, human and rabbit antisera to Lol p IV and (ii) the binding of these antisera to Lol p IV could be inhibited by the anti-Id. Interestingly, the internal image anti-Id B1/1 also recognized an Id on a monoclonal antibody which was directed to an epitope of Lol p IV, different from that recognized by MoAb 91.

Allergens↗

Administration of noninternal image monoclonal anti-idiotypic antibodies induces idiotype-restricted responses specific for human immunodeficiency virus envelope glycoprotein epitopes.

A mouse monoclonal anti-idiotypic antibody (anti-Id), designated MC1, was generated against chimpanzee antibodies specific for a synthetic peptide corresponding to a native epitope associated with gp41 of human immunodeficiency virus (HIV). This anti-Id recognized a shared idiotope/idiotype (Id) on a second chimpanzee anti-gp41 peptide preparation but failed to detect this Id on rabbit and mouse anti-gp41 peptide antibodies induced by immunization with the gp41 synthetic peptide. The chimpanzee Id-MC1 reaction was not inhibited by either synthetic peptide or recombinant gp160 suggesting that MC1 exhibits noninternal image, Ab-2 alpha-like characteristics. Immunization of syngeneic Balb/c mice with MC1 induced an antigen-positive (Ag+) response capable of binding the synthetic peptide, recombinant gp160, and gp41, whereas MC1-immunized rabbits did not produce any detectable anti-peptide and/or anti-HIV envelope glycoprotein antibody response. The MC1-induced anti-Id response (Ab-3) in both mice and rabbits expressed a similar Id with the Ab-1, which is not normally expressed in the anti-gp41 peptide antibody response induced by the nominal antigen in Balb/c mice and in rabbits. Together, these studies indicate that a mouse monoclonal anti-Id of the Ab-2 alpha class can induce an anti-HIV response specific for a gp41 epitope defined by a synthetic peptide, which does not cross species barriers.

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Strategies for developing vaccines against acquired immunodeficiency syndrome.

There exists an abundance of literature on the prospects for developing vaccines against the etiologic viral agent of acquired immunodeficiency syndrome (AIDS). Excellent reviews from a variety of investigators are available on this subject. It is our intention to review the literature relative to potential strategies for developing a successful AIDS vaccine and to impart some of our concerns on the different types of vaccine that are being tested. We have also focused on some vaccine strategies that have not received much attention in previous review articles. Finally, the role of animal models in assessing vaccine safety and efficacy against AIDS has been briefly described.

Acquired Immunodeficiency Syndrome↗

Immune response to human immunodeficiency virus. In vivo administration of anti-idiotype induces an anti-gp160 response specific for a synthetic peptide.

Anti-idiotypic antibodies (anti-Id) to chimpanzee antibodies directed against a synthetic peptide corresponding to a native epitope associated with gp41 of human immunodeficiency virus (HIV) envelope glycoprotein were produced in rabbits. The peptide was analogous to amino acid sequences 735 to 752 from the human T cell leukemia virus-IIIB isolate of HIV. Characteristics of the anti-Id preparation included: 1) detection of a shared determinant present on a second chimpanzee and one of three rabbit antibody preparations directed against the synthetic peptide, 2) failure to recognize an idiotype (Id) in BALB/c mouse antisera to the peptide, and 3) partial inhibition of the homologous chimpanzee Id preparation from binding either peptide or a recombinant HIV gp160 preparation. Immunization of BALB/c mice with the anti-Id induced an antipeptide response which bound a recombinant gp160 preparation without subsequent peptide or gp160 exposure. The anti-gp160 containing sera from mice immunized with anti-Id were able to inhibit the Id-anti-Id reaction indicating that an Id-positive antibody response was induced. This Id is not normally expressed in the murine anti-gp 160 immune response to the synthetic peptide and suggests that this anti-Id may activate normally silent clones. This study indicates that Id networks may be operational during the immune response to HIV epitopes. Alternatively, anti-Id may be useful in altering the serologic characteristics of an antibody response to HIV and may offer potential for modulating the immune response in this viral infection.

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Evaluation of a competitive ELISA for detection of antibodies against avian influenza virus nucleoprotein.

A competitive enzyme-linked immunosorbent assay (C-ELISA) employing a baculovirus-expressed recombinant nucleoprotein and a monoclonal antibody was developed for the detection of antibodies to type A influenza virus nucleoprotein. The performance of the C-ELISA was evaluated by testing 756 chickens, 1123 turkeys, 707 emus, and 1261 ostriches, for a total of 3847 serum samples. Relative to the agar gel immunodiffusion (AGID) test, the C-ELISA had a sensitivity of 100% for all four species. The C-ELISA's sensitivity relative to the hemagglutination-inhibition (HI) test results was 100% for chicken, turkey, and emu and 96.2% for the ostrich serum samples. More than 90% of the AGID-negative/C-ELISA-positive serum samples were found positive by HI for at least one influenza serotype. The specificity of C-ELISA relative to AGID ranged from 85.5% to 99.8% for sera collected from these species. These results indicated that the C-ELISA was more sensitive and more specific than the AGID test and as sensitive and as specific as the HI test. The C-ELISA has the potential to replace the AGID test for screening sera from avian species, including ratites, for detection of antibodies to type A influenza virus.

Animals↗

Evaluation of antibody responses of emus (Dromaius novaehollandiae) to avian influenza virus infection.

Emu antibody responses to avian influenza virus (AIV) infection were evaluated by the competitive enzyme-linked immunosorbent assay (C-ELISA), agar gel immunodiffusion (AGID) and hemagglutination inhibition (HI) tests. All birds infected with AIV H5N1, H5N3, or H7N7 developed antinucleoprotein (NP) antibodies as early as 7 days postinfection as detected by the C-ELISA. The responses lasted 49 days for the emus receiving H5N3 and at least 56 days for emus receiving the other two viruses. By evaluating 50 emu field serum samples, the C-ELISA was found more sensitive than the AGID test for the detection of anti-NP antibodies. This study indicates that emus experimentally infected with AIV developed antibody responses that can be detected by C-ELISA, AGID, and HI tests. The results from this and our previous studies demonstrate the use of the C-ELISA as a substitute for the AGID test in a routine serodiagnostic screening for detection of antibodies to AIV infection in multiple avian species.

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