Variable region cDNA sequences and characterization of murine anti-human interferon γ receptor monoclonal antibodies that inhibit receptor binding by interferon γ

Bridges, Angela; Birch, Ashley; Williams, Gwyneth; Aguet, Michel; Schlatter, Daniel; Huber, Walter; Garotta, Gianni

doi:10.1016/0161-5890(95)00114-x

Cited by 3 publications

(2 citation statements)

References 37 publications

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“…Analysis of the sequences revealed that the MAbs used different germ line family sequences for V H , V, and J but the same germ line family for J H ( Table 1). Comparison of these heavy-and light-chain rearranged V region sequences to similar sequences found in the GenBank database has shown that the V region rearrangement events encode various immunoglobulin binding specificities ranging from double-stranded DNA to protein epitopes (3,4,22,(26)(27)(28)30).…”

Section: Sequencing Of Mab Variable Domainsmentioning

confidence: 99%

Specificity and Diversity of Antibodies toMycobacterium tuberculosisArabinomannan

Navoa¹,

Laal

Pirofski³

et al. 2003

Clin Vaccine Immunol

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Arabinomannan (AM) is a polysaccharide antigen of the mycobacterial capsule. However, it is uncertain whether AM constitutes an immunologically distinct fraction of Mycobacterium tuberculosis. In this study, we analyzed the repertoire and specificity of antibodies to AM by using AM-binding murine monoclonal antibodies (MAbs) and human serum samples. Murine MAbs were found to be diverse in their specificity to AM and cross-reactivity with other arabinose-containing mycobacterial polysaccharides, with MAb 9d8 binding exclusively to AM. Human antibodies to AM were detected in serum samples from patients with pulmonary tuberculosis (TB), as well as in those from healthy, purified protein derivative-negative controls, with significantly higher titers among patients. The binding of human antibodies to AM was inhibited by MAb 9d8 in three patients with TB but not in controls. MAb 5c11, which recognizes other mycobacterial arabinosecontaining carbohydrates in addition to AM, inhibited the binding of serum samples from 75% of patients and 76% of controls. Analysis of human antibodies with murine MAbs to human V H determinants demonstrated diversity among antibodies to AM with qualitative and quantitative differences compared with antibodies to lipoarabinomannan. In summary, our study suggests that antibodies to AM are diverse and heterogeneous with respect to antigen recognition and V H determinant expression, with human serum samples containing different subsets of antibodies to AM with the specificities of AM-binding murine MAbs. One MAb and a subset of human antibodies bind AM specifically, suggesting that this polysaccharide is antigenically distinct and is expressed in human infection.

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Section: Sequencing Of Mab Variable Domainsmentioning

confidence: 99%

Specificity and Diversity of Antibodies toMycobacterium tuberculosisArabinomannan

Navoa¹,

Laal

Pirofski³

et al. 2003

Clin Vaccine Immunol

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show abstract

“…The epitopes recognized by the other mAb's (GIR94, GIR208, 21/31.1, 177.1, and IRγ2) have not yet been mapped. The epitope recognized by A6 has been investigated extensively in recent years by sitedirected mutagenesis and crystallography (37)(38)(39)(40)(41)(42). A6 recognizes a conformational epitope stabilized by Cys 63 (38).…”

mentioning

confidence: 99%

In a novel form of IFN-γ receptor 1 deficiency, cell surface receptors fail to bind IFN-γ

Jouanguy¹,

Dupuis²,

Pallier³

et al. 2000

J. Clin. Invest.

150

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Neutralizing epitopes on the extracellular interferon γ receptor (IFNγR) α-chain characterized by homolog scanning mutagenesis and X-ray crystal structure of the A6 Fab-IFNγR 1-108 complex 1 1Edited by R. Huber

Sogabe

Stuart

Henke

et al. 1997

Journal of Molecular Biology

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Variable region cDNA sequences and characterization of murine anti-human interferon γ receptor monoclonal antibodies that inhibit receptor binding by interferon γ

Cited by 3 publications

References 37 publications

Specificity and Diversity of Antibodies toMycobacterium tuberculosisArabinomannan

Specificity and Diversity of Antibodies toMycobacterium tuberculosisArabinomannan

In a novel form of IFN-γ receptor 1 deficiency, cell surface receptors fail to bind IFN-γ

Neutralizing epitopes on the extracellular interferon γ receptor (IFNγR) α-chain characterized by homolog scanning mutagenesis and X-ray crystal structure of the A6 Fab-IFNγR 1-108 complex 1 1Edited by R. Huber

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