Plasmodium falciparum: molecular analysis of a putative protective antigen, the thermostable 96-kDa protein.

A group of three Plasmodium falciparum antigens of distinct pI, migrating with an apparent MW of 96 kDa has been previously identified as a target of protective immunity both in humans and in monkeys (Jouin et al. 1987, Dubois et al. 1987).

The polymorphic 11.1 locus of Plasmodium falciparum.

Clone pPF11.1 encodes a Plasmodium falciparum antigen expressed during the intraerythrocytic cycle and containing tandem repeats of a 9 amino acid unit. We report here an analysis of the genomic region specific for 11.

Karyotype comparison between P. chabaudi and P. falciparum: analysis of a P. chabaudi cDNA containing sequences highly repetitive in P. falciparum.

The molecular karyotypes of P. chabaudi and P. falciparum have been compared by pulse field gradient electrophoresis.

Characterisation of P. falciparum antigenic determinants isolated from a genomic expression library by differential antibody screening.

A genomic expression library of P.falciparum has been differentially screened with a number of immune sera. The response of 9 clones to the various sera is presented, together with the DNA sequence encoding the epitopes.

Human antisera detect a Plasmodium falciparum genomic clone encoding a nonapeptide repeat.

Plasmodium falciparum causes malaria infections in its human host. Its wide distribution in tropical countries is a major world health problem. Before a vaccine can be produced, the identification and characterization of parasite antigens is necessary.

Cloning of cDNAS that code for Plasmodium chabaudi antigens of the erythrocytic forms and cross-hybridize with P. falciparum.

Several Plasmodium chabaudi antigens are synthesized and the corresponding mRNAs are detected by cell-free translation only during specific stages of the erythrocytic cycle. Ring stage mRNA was used to construct a cDNA library in the plasmid vector pBR 322. The library was screened by differential hybridization with cDNA specific for ring stage parasites or schizonts.

Two regions of the bifunctional protein aspartokinase I- homoserine dehydrogenase I are connected by a short hinge.

Four proteases differing in their specificity, i.e. subtilisin, trypsin, alpha-chymotrypsin and V8 staphylococcal protease, cleave the bifunctional protein Escherichia coli aspartokinase I-homoserine dehydrogenase I (composed of 820 residues) producing an active homoserine dehydrogenase fragment.

Mechanism of allosteric activation of glycogen phosphorylase probed by the reactivity of essential arginine residues. Identification of an arginine residue involved in the binding of glucose 1-phosphate.

We have previously reported the physicochemical and kinetic properties of glycogen phosphorylase modified by arginine-specific reagent under different conditions [Dreyfus, M., Vandenbunder, B., & Buc, H.

Nucleotide sequence of the thrA gene of Escherichia coli.

The thrA gene of Escherichia coli codes for a single polypeptide chain having two enzymatic activities required for the biosynthesis of threonine, aspartokinase I and homoserine dehydrogenase I. This gene was cloned in a bacterial plasmid and its complete nucleotide sequence was established. It contains 2460 base pairs that encode for a polypeptide chain of 820 amino acids.

The primary structure of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I. Site of limited proteolytic cleavage by subtilisin.

The sequence of the first 25 residues of the homoserine dehydrogenase fragment, produced by limited proteolysis of aspartokinase I-homoserine dehydrogenase I with substilisin, has been determined. The sequence of a cyanogen bromide peptide (CB5, 59 residues), isolated from the entire protein, is also presented. Residues 1 to 18 of the subtilisin homoserine dehydrogenase fragment match the sequence 42 to 59 of peptide CB5.