Induction of T cell responses by chimeric bacterial proteins expressing several copies of a viral T cell epitope. (Q54648972)

2 June 2018

title

Induction of T cell responses by chimeric bacterial proteins expressing several copies of a viral T cell epitope. (English)

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2 June 2018

author

Pierre Martineau

2

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author name string

R Lo-Man

1

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M Hofnung

3

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C Leclerc

4

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language of work or name

English

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publication date

1 November 1993

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2 June 2018

European Journal of Immunology

published in

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2 June 2018

volume

23

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issue

11

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2 June 2018

page(s)

2998-3002

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2 June 2018

Interaction of an immunodominant epitope with Ia molecules in T-cell activation

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Peptide competition for antigen presentation

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The choice of T-cell epitopes utilized on a protein antigen depends on multiple factors distant from, as well as at the determinant site

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The molecular context of determinants within the priming antigen establishes a hierarchy of T cell induction: T cell specificities induced by peptides of beta-galactosidase vs. the whole antigen

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The effects of a flanking sequence on the immune response to a B and a T cell epitope from the fusion protein of measles virus

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Predominant naturally processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogeneous in size

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Efficient processing of an antigenic sequence for presentation by MHC class I molecules depends on its neighboring residues in the protein

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Flanking sequences influence the presentation of an endogenously synthesized peptide to cytotoxic T lymphocytes

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Presentation of viral antigen to class I major histocompatibility complex-restricted cytotoxic T lymphocyte. Recognition of an immunodominant influenza hemagglutinin site by cytotoxic T lymphocyte is independent of the position of the site in the he

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Expression of heterologous peptides at two permissive sites of the MalE protein: antigenicity and immunogenicity of foreign B-cell and T-cell epitopes

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Nonoverlapping T and B cell determinants on an hepatitis B surface antigen pre-S(2) region synthetic peptide

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Production in Escherichia coli and one-step purification of bifunctional hybrid proteins which bind maltose. Export of the Klenow polymerase into the periplasmic space

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Affinity chromatographic isolation of the periplasmic maltose binding protein ofEscherichia coli

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Identification of a T-cell epitope adjacent to neutralization antigenic site 1 of poliovirus type 1

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Efficient recognition by rat T cell clones of an epitope of mycobacterial hsp 65 inserted inEscherichia coli outer membrane protein PhoE

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T and B cell responses to chimeric proteins containing heterologous T helper epitopes inserted at different positions

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Immune responses to hybrid maltose-binding proteins

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Identifiers

DOI

10.1002/EJI.1830231141

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2 June 2018

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2 June 2018