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F Fossiez

Publications and source records attributed to F Fossiez.

20 records · Page 2Linked to original sources

Nucleotide sequence of the polyhedrin gene of Euxoa scandens cytoplasmic polyhedrosis virus (EsCPV).

The double-stranded RNA genome of Euxoa scandens cytoplasmic polyhedrosis virus (EsCPV) was reversely transcribed to the double-stranded DNA and cloned into pIBI30. The complete nucleotide sequence of cloned genome segment 10, which encodes the virus polyhedrin polypeptide, was determined. The EsCPV polyhedrin gene consists of 881 bp and possesses an open reading frame that codes for a polypeptide of 269 amino acids (MW 30.1K), consistent with an apparent MW of 30K determined by SDS-PAGE for purified polyhedrin. The sequence is identical to that reported for the amino terminus of polyhedrin from the CPV of Orgyia pseudotsugata; however, no amino acid or nucleotide sequence homology was found between the EsCPV polyhedrin and that from Bombyx mori CPV (BmCPV) or several nuclear polyhedrosis viruses. The hydrophilic profiles and predicted secondary structures of both EsCPV and BmCPV polyhedrin show some similarities, mainly in the amino half of the polypeptides. These data should be helpful in identifying the domains responsible for the polyhedrin crystallizing properties.

Amino Acid Sequence↗

Generation and characterization of a human monoclonal autoantibody that acts as a high affinity interleukin-1 alpha specific inhibitor.

Interleukin-1 (IL-1) defines two polypeptides, IL-1 alpha and IL-1 beta, that possess a wide spectrum of biological effects. Two natural antagonists of IL-1 action have been characterized: the IL-1 receptor antagonist (IL-1Ra) and a soluble form of the type II IL-1 receptor. Neutralizing autoantibodies to IL-1 alpha have also been detected in sera of healthy individuals and patients with autoimmune or inflammatory diseases. To characterize such antibodies molecularly, we attempted to generate B cell clones producing anti-IL-1 alpha human monoclonal antibody (HuMAb) by combining Epstein-Barr virus-immortalization and CD40-activation of B lymphocytes from individuals with circulating anti-IL-1 alpha. We describe herein the generation and properties of a natural IgG4/kappa anti-IL-1 alpha monoclonal autoantibody, HuMAb X3, that bound specifically to human IL-1 alpha, but not to IL-1 beta and IL-1Ra, with a high affinity (Kd = 1.2 x 10(-10)M). HuMAb X3 inhibited IL-1 alpha binding to IL-1 receptors and neutralized biological activities of both recombinant and natural forms of IL-1 alpha. A recombinant form of HuMAb X3 was found to display identical specific IL-1 alpha antagonism. The presence of somatic mutations within X3 variable regions suggests an antigen-driven affinity maturation. This study extends the demonstration of the presence of high affinity neutralizing anti-IL-1 alpha autoantibodies that can function as a third type of IL-1 antagonist.

Amino Acid Sequence↗