Polyclonal Anti-ldiotypes Influence Macrophage Chemotaxis in Coxsackievirus-lnduced Murine Myocarditis

Paque, Ronald E.; Miller, R

doi:10.1002/jlb.45.1.79

Cited by 10 publications

(21 citation statements)

References 32 publications

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“…with 108 PFU of lethally UV-irradiated CVB3 virus in Freund's complete adjuvant, followed by weekly i.p. injections for at least 6 to 8 weeks of 107 PFU of virus (20)(21)(22)(23)(24). Syngeneic BALB/cJ donors of mouse anti-Ids were immunized subcutaneously with 50 ,ug of affinity column-purified, protein A-separated, anti-CVB3-purified IgG emulsified with Freund's complete adjuvant.…”

Section: Materlils and Methodsmentioning

confidence: 99%

“…Previous studies from our laboratory have suggested the participation of anti-idiotypic antibodies (anti-Ids) in the induction and expression of autoimmune myocarditis induced by the enterovirus coxsackievirus B3 (CVB3) in a murine model (20). The array of immunobiological effects of polyclonal or monoclonal anti-Ids has included inhibition of myocarditis by pretreatment and/or immunization with anti-Ids in susceptible hosts (20), suppression of in vitro T-cell or splenocyte proliferative responses (22), specific modulation of macrophage chemotaxis in vitro (21), release of the lymphokine migration inhibition factor from sensitized T cells (19), and ability to bind selectively to myocyte target cell molecules and/or mimic solubilized heart-associated antigens (23). Anti-Ids were also demonstrated to induce specific, antiviral T-cell immunity (20,22,23) and stimulate secondary B-cell responses in viral or anti-Id-primed animals (20,22).…”

mentioning

confidence: 99%

“…Anti-Ids were also demonstrated to induce specific, antiviral T-cell immunity (20,22,23) and stimulate secondary B-cell responses in viral or anti-Id-primed animals (20,22). The specificity of these anti-Ids was established with the demonstration of anti-anti-Ids (antibody 3) able to bind original CVB3 viral protein (VP) coat determinants (21).…”

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confidence: 99%

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Adoptively transferred anti-idiotype pulsed B cells mediate autoimmune myocarditis

Paque

Miller

1992

Infect Immun

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Syngeneic mice receiving adoptively transferred enriched B cells or splenocytes pulsed in vitro with polyclonal anti-idiotypic antibodies (anti-Ids) against anti-CVB3 virus antibodies developed coxsackievirus B3 antigenbinding and virus-neutralizing antibodies during a 30-day period, in addition to overt expression of autoimmune myocarditis. Adoptive transfer of anti-Id pulsed T cells resulted in delayed appearance and transient expression of antiviral antibodies, and antiviral antibodies were marginal to absent in syngeneic animals receiving anti-Id pulsed macrophage populations. Proliferation analysis of recipient splenocytes indicated lack of proliferative capacity in response to monoclonal or polyclonal anti-Ids and only marginal proliferative capacity in response to coxsackievirus B3 virus antigen(s). In vitro assessment of delayed hypersensitivity in recipient animals demonstrated some specific immunity to anti-Ids in recipients receiving splenocytes or T cells. Anti-Ids expressing mimicry for heart-associated and/or viral antigen(s) interacting with B cells or other accessory cells suggest an autoantibody or anti-Id triggering of B-cell-mediated mechanisms involved in the development of myocarditis.

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Section: Materlils and Methodsmentioning

confidence: 99%

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confidence: 99%

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Adoptively transferred anti-idiotype pulsed B cells mediate autoimmune myocarditis

Paque

Miller

1992

Infect Immun

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“…2,4-Dinitrophenol (DNP)ovalbumin was prepared by conjugation of 0.2 ml of dinitrofluorobenzene (DNFB) to 500 mg of ovalbumin (Sigma Chemical Co., St. Louis, Mo.) as described earlier (22,23). Briefly, ovalbumin was dissolved in 100 ml of 0.85 M saline with DNFB by stirring at 25°C for 30 min.…”

Section: Methodsmentioning

confidence: 99%

Polyclonal anti-idiotypic antibodies exhibit antigenic mimicry of limited type 1 fimbrial proteins of Escherichia coli

1990

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Polyclonal anti-idiotypic antibodies (anti-Ids)(fim) developed against idiotypes on antibodies (Ab-1s) that specifically bind structural, organelle fimbrial proteins of Escherichia coli were able to modulate immune function in anti-Id(fim)-immunized mice. Proliferation or suppression of splenic lymphoid cell responses by polyclonal anti-Ids in tissue culture appeared to be dose dependent. Anti-Ids were able to induce a dose-dependent T-cell-mediated immunity specific for type 1 fimbrial antigen(s) in immunized animals when assessed in vitro, but they failed to elicit in vivo positive ear-swelling skin reactions. Anti-Ids were unable to induce protective immunity against an in vivo infectious challenge with E. coli in anti-Id-immunized adult animals, but they stimulated a specific, secondary antibody response in anti-Id-challenged mice. Anti-Ids stimulated the development of anti-anti-Ids (Ab-3s) specifically binding a fimbrial antigen(s) and revealed the presence of antibody idiotypes binding E. coli adhesin proteins in the 27-to 29-kilodalton range. Results suggest discrete, but subtle, immunomodulatory effects of the anti-Ids and potential vaccinoid properties capable of stimulating a specific humoral and cellular response in vivo.

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“…The method for preparing F(ab):! fragments was performed as described by Paque & Miller (1989). Briefly, purified MAb prepared in 0.1 M sodium acetate (pH 7.2) was adjusted with 2 M acetic acid to pH 4.2 and kept at 37°C.…”

Section: Animals Female Lou Rats (Harlan Sprague Dawleymentioning

confidence: 99%

Anti-idiotype antibodies that mimic a conserved aquatic birnavirus epitope induce neutralizing antibodies and bind to fish cells with inhibition of virus replication

Sy¹,

Bl²

1996

Dis. Aquat. Org.

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Polyclonal anti-idiotype (anti-Id) antibodies were prepared in rats against a monoclonal antibody (MAb AS-1) which defines a highly conserved neutralization epitope on virion protein 2 (VP2) of Serogroup A aquatic birnaviruses. Anti-mouse IgG cross-reactive antibodies were removed from rat sera by adsorption to an affinity column of normal mouse IgG and further punfied by subsequent adsorption to and elution from an affinity column coupled with MAb AS-1. Confirmation that these anti-Id antibodies were directed against the paratope of MAb AS-1 and molecularly mimicked the virus epitope was demonstrated in a variety of assays. Anti-Id antibodies reacted in enzyme-linked immunosorbent assay (ELISA) with both whole MAb AS-1 IgG and F(ab);, fragments, but &d not react with 2 unrelated mouse IgGs or F(ab);, fragments. Anti-Id antibodies blocked binding of virus to MAb AS-1 in a dose-dependent manner with 100% inhibition at the highest concentration. Similarly, virus inhibited anti-Id/i&otype binding by 60 %. Furthermore, anti-Id antibodies inhibited the ability of MAb AS-1 to neutralize virus in plaque reduction assays. Anti-ld antibodies induced the production of virus neutralizing antibodies in mice. Anti-Id antibodies also were used to show that the AS-1 epitope is a presumptive cell attachment site on the virus which recognizes and binds to specific cell receptors Anti-Id antibodies were shown to bind to a variety of both salmonid and non-salmonid fish cell cultures. Pretreatment of fish cell cultures with virus inhibited (28 to 50%) binding of anti-ld antibodies. Treatment of fish cell cultures with anti-Id antibodies also resulted in a decrease (98%) in the yield of progeny virus compared with replication of the virus in untreated cells or cells treated with normal rat immunoglobulin.

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Polyclonal Anti-ldiotypes Influence Macrophage Chemotaxis in Coxsackievirus-lnduced Murine Myocarditis

Cited by 10 publications

References 32 publications

Adoptively transferred anti-idiotype pulsed B cells mediate autoimmune myocarditis

Adoptively transferred anti-idiotype pulsed B cells mediate autoimmune myocarditis

Polyclonal anti-idiotypic antibodies exhibit antigenic mimicry of limited type 1 fimbrial proteins of Escherichia coli

Anti-idiotype antibodies that mimic a conserved aquatic birnavirus epitope induce neutralizing antibodies and bind to fish cells with inhibition of virus replication

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