Contribution of defined amino acid residues to the immunogenicity of recombinant Escherichia coli heat-stable enterotoxin fusion proteins

Autor: Maurice Der Vartanian, Isabelle Batisson
Přispěvatelé: Laboratoire Microorganismes : Génome et Environnement (LMGE), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Centre National de la Recherche Scientifique (CNRS)-Université d'Auvergne - Clermont-Ferrand I (UdA), Laboratoire de microbiologie, Institut National de la Recherche Agronomique (INRA), Université Blaise Pascal - Clermont-Ferrand 2 (UBP)-Université d'Auvergne - Clermont-Ferrand I (UdA)-Centre National de la Recherche Scientifique (CNRS), Unité de Microbiologie (MIC), Batisson, Isabelle
Jazyk: angličtina
Rok vydání: 2000
Předmět:
MESH: Rabbits
MESH: Escherichia coli Proteins
Enterotoxin
MESH: Amino Acid Sequence
MESH: Adhesins
Escherichia coli
medicine.disease_cause
Mice
Enterotoxins
MESH: Immunogenetics
MESH: Antibodies
Bacterial
MESH: Enterotoxins
Heat-stable enterotoxin
MESH: Animals
Peptide sequence
MESH: Bacterial Proteins
chemistry.chemical_classification
Adhesins
Escherichia coli
MESH: Escherichia coli
Immunogenicity
Escherichia coli Proteins
Bacterial
Antibodies
Bacterial
Adhesins
MESH: Amino Acid Substitution
MESH: Glycine
Amino acid
[SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology
Rabbits
Recombinant Fusion Proteins
Bacterial Toxins
Molecular Sequence Data
Glycine
Biology
Microbiology
Antibodies
MESH: Fimbriae
Bacterial
Fimbriae
Bacterial Proteins
Leucine
[SDV.BBM] Life Sciences [q-bio]/Biochemistry
Molecular Biology
Genetics
medicine
Escherichia coli
Immunogenetics
MESH: Recombinant Fusion Proteins
Animals
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
Amino Acid Sequence
Antigens
[SDV.MP] Life Sciences [q-bio]/Microbiology and Parasitology
Molecular Biology
MESH: Mice
Antigens
Bacterial
MESH: Molecular Sequence Data
Toxin
Fusion protein
MESH: Leucine
chemistry
Amino Acid Substitution
MESH: Bacterial Toxins
Fimbriae
Bacterial
MESH: Antigens
Bacterial
Zdroj: FEMS Microbiology Letters
FEMS Microbiology Letters, Wiley-Blackwell, 2000, 192 (2), pp.223-9
FEMS Microbiology Letters, 2000, 192 (2), pp.223-9
ISSN: 0378-1097
1574-6968
Popis: International audience; We investigated whether the toxicity-associated receptor-binding domain of the non-immunogenic Escherichia coli heat-stable enterotoxin (STh) as a fusion with a carrier protein and the inclusion of an appropriate spacer are critical factors for eliciting antibody responses against the native toxin. The immunological properties of three toxic and one non-toxic fusion proteins, consisting of STh N-terminally joined to the C-terminus of the major subunit ClpG of E. coli CS31A fimbriae, were compared. In contrast to the non-toxic hybrid STh with glycine and leucine simultaneously substituted for the receptor-interacting Pro(13) and Ala(14) amino acids, the toxic chimeras responded by producing high serum levels of anti-STh antibodies in immunized animals. On the other hand, only the toxic ClpG-STh construct with the natural peptide 47KSGPESM(53) of Pro-STh as spacer stimulated STh-neutralizing responses against both native toxin and enterotoxigenic live E. coli cells. Altogether, these findings suggest a close relationship between conformational similarity to the native structure of STh and the ability to elicit specific antibody responses against STh.
Databáze: OpenAIRE
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