Oligonucleotide probes synthesized using the published protein sequence for porcine pancreatic phospholipase A2 (PLA2; Puijk et al., 1977), were used to screen a cDNA library made from porcine pancreas. One resulting clone which encoded the entire porcine PLA2 enzyme was then used to screen various human cDNA and gene libraries. A 562-bp cDNA clone from human lung and two overlapping genomic clones encoding the identical transcript were obtained. These clones encoded a 126-residue peptide corresponding to human "pancreatic" PLA2. The gene spanned 4.9 kb and contained three introns of 1692, 800, and about 2650 bases, respectively. Hybridization of the human cDNA against blots of total human DNA detected the same set of fragments contained in both genomic clones and failed to detect more than one distinct gene. Under equivalent conditions, the same probe detected two discrete bands in cobra (Naja naja) genomic DNA. Apparently, there is a single or small number of identical human genes encoding "pancreatic" PLA2 which are transcribed also in lung tissue; human pancreatic PLA2 appeared more closely related at the nucleotide level to snake counterparts than to other reported human PLA2 enzyme forms.

Atrial extracts contain factors which induce potent natriuresis changes in renal haemodynamics, and relax pre-contracted vascular smooth muscle. Low-molecular-weight peptides which mimic these actions have now been purified by several groups, including ours (see accompanying paper), and higher-molecular-weight proteins with similar but less potent biological activities have also been identified and are presumed to be precursors. If released into the circulation, these peptides, collectively called atrial natriuretic factor (ANF), may play a significant part in blood-pressure homeostasis, regulation of extracellular fluid volume and as antagonists to the hypertensive effects of the renin-angiotensin system and other hormonal and neurotransmitter systems. We describe here the isolation and characterization of rat atrial cDNA clones which encode ANF. Nucleotide sequence analysis shows that auriculin corresponds to the 25 amino acids located close to the C-terminus of a 152-amino acid ANF precursor. Analysis of the in vitro translation products of precursor ANF mRNA suggests that multiple forms of the precursor may exist.

Rinderpest is a highly contagious ruminant viral disease manifested by a rapid course and greater than 90% mortality. Infectious vaccinia virus recombinants were constructed that express either the hemagglutinin or the fusion gene of rinderpest virus. All cattle vaccinated with either recombinant or with the combined recombinants produced neutralizing antibodies against rinderpest virus and were protected against the disease when challenged with more than 1000 times the lethal dose of the virus.

Peste des petits ruminants (PPR) is a viral disease of goats and sheep characterized by erosive stomatitis, enteritis, and pneumonia. The virus is a member of the family Paramyxoviridae and the genus Morbillivirus. The disease has high morbidity and mortality rates and has a substantial economic impact in developing countries. We have cloned and sequenced the cDNA of the nucleocapsid (N) gene of the Nigeria 75/1 strain of PPR virus (PPRV). A comparison of its nucleotide and deduced amino acid sequence with those of the N gene of the tissue culture-attenuated strain of PPRV was performed. A divergence of 8.9 and 5.0% was found at the nucleotide and amino acid level, respectively. A recombinant baculovirus that expresses the N protein in insect cells and larvae (Spodoptera frugiperda) was generated. The recombinant protein, characterized by Western blot analysis, was shown to have a molecular weight of 58 kDa and was recognized by anti-PPRV antibodies. The recombinant protein was used successfully as a coating antigen in an enzyme-linked immunosorbent assay for the serological diagnosis of PPRV.