Nucleocapsid protein gene of Junin arenavirus (cDNA sequence).
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Amino Acid Sequence↗
Biomedical subjects
V Romanowski
Publications and source records attributed to V Romanowski.
Complete sequence of the S RNA of lymphocytic choriomeningitis virus (WE strain) compared to that of Pichinde arenavirus.
Previous studies have reported that the 3' half of the small, S, RNA species of the WE strain of lymphocytic choriomeningitis (LCM) virus codes for the viral nucleoprotein in a subgenomic, viral-complementary, mRNA species (Romanowski, V. and Bishop, D.H.L. (1985) Virus Res. 2, 35-51). The complete sequence of the LCM-WE S RNA has now been obtained, indicating that the 5' half of the RNA codes for the viral glycoprotein precursor in a viral-sense sequence that does not overlap the N gene. It is concluded that, like Pichinde virus (Auperin, D. et al. (1984) J. Virol. 52, 897-904), LCM has an ambisense S RNA coding strategy. The LCM-WE S RNA is 3375 nucleotides in length, has a size of 1.14 X 10(6) Da and base composition of 26.1% A, 23.2% C, 21.5% G, 29.2% U. The 3' and 5' end sequences of the S RNA are complementary for some 30 nucleotides, depending on the arrangement. The non-coding regions at the two ends are 77 (5') and 60 (3') nucleotides long. The glycoprotein precursor has a primary amino acid size of 56293 Da and is rich in potential glycosylation sites as well as histidine and cysteine residues. It has both amino and carboxy proximal hydrophobic regions. The LCM-WE S RNA and predicted protein sequence data have been compared to those of Pichinde arena-virus. Extensive RNA and protein sequence homology exists for the two S RNA species, although the homology for the glycoprotein sequences of the two viruses (39%) is less than the 50% observed for the two viral nucleoproteins.
Amino Acid Sequence↗
Conserved sequences and coding of two strains of lymphocytic choriomeningitis virus (WE and ARM) and Pichinde arenavirus.
Analyses of the 3' end sequences of the small, S, and large, L, RNA species of lymphocytic choriomeningitis (LCM) virus isolates ARM and WE, and DNA clones of LCM-WE, have shown that there are extensive RNA sequence homologies between the 3' ends of the two RNA species of both LCM strains. Limited sequence data of DNA clones representing the LCM-WE L RNA species indicate that a gene product (presumably the minor 200 kdalton virion protein) is coded in a viral-complementary mRNA species. Sequence analyses of LCM-WE S DNA clones indicate that approximately 50% of the 2040 nucleotides representing the 3' half of the viral RNA species (and its encoded 558 amino acid gene product) are identical in type and position to those of Pichinde arenavirus (Auperin, D., et al. (1984a), Virology 134, 208-219). For Pichinde virus, it has been shown that the 3' proximal gene product (the nucleoprotein, N) is translated from a subgenomic, viral-complementary mRNA (Auperin et al., 1984a). Data have recently been obtained (Auperin, D., et al. (1984b) J. Virol., in press) that indicate that the Pichinde glycoprotein precursor, GPC, is coded in a viral-sense subgenomic mRNA species corresponding to the 5' half of the S RNA. The nucleotide sequence that immediately follows the N coding region of both LCM-WE and Pichinde viruses can be arranged in a hairpin configuration. In view of this, and if, like Pichinde virus, LCM has an ambisense S RNA coding strategy, then it is probable that the intergenic hairpins function as transcription terminators for the N and GPC mRNA species of both viruses.
Amino Acid Sequence↗
Analyses of the mRNA transcription processes of snowshoe hare bunyavirus S and M RNA species.
The time course of synthesis of snowshoe hare bunyavirus small (S)- and medium (M)-sized viral RNA (vRNA), viral cRNA (vcRNA), and mRNA species was analyzed by using single-stranded DNA probes representing the S- and M-coded gene products. In the presence of puromycin, an inhibitor of protein synthesis, the subgenomic S mRNA species were detected, but not full-length S vcRNA or S vRNA species. No M-related RNA species were identified in puromycin-treated cells. In the absence of puromycin, full-length M and S vRNA, S vcRNA, and subgenomic S mRNA species were observed, as well as apparently full-length M vcRNA species, presumably including the approximately similar-sized M mRNA species. The 5' ends of the S and M mRNA species have been shown to be heterogeneous and some 12 to 17 bases longer than the ends of their corresponding presumptive replicative vcRNA species, in agreement with an earlier report that they represent nonviral primer sequences (D. H. L. Bishop, M. E. Gay, and Y. Matsuoko, Nucleic Acids Res. 11:6409-6418, 1983). The 3' ends of the M and S mRNA species were found to be shorter by some 60 and 100 nucleotides, respectively, than those of their corresponding full-length vcRNA species. Comparison of the 3' noncoding regions of the S and M vcRNA species revealed that there are conserved sequences following the translation termination codons of the two RNA species. One of these conserved sequences is a pyrimidine-rich template sequence that is approximately 20 nucleotides beyond the deduced S mRNA transcription termination site.
Base Sequence↗
Sequencing studies of pichinde arenavirus S RNA indicate a novel coding strategy, an ambisense viral S RNA.
Analyses of the complete sequence of the 1.1 X 10(6)-dalton, small (S) RNA of the arenavirus Pichinde and virus-induced cellular RNA species have revealed that the viral nucleoprotein, N, is coded in a subgenomic, non-polyadenylated, virus-complementary mRNA corresponding to the 3' half of the viral RNA (Auperin et al., Virology 134:208-219, 1984). By contrast, a second S-coded product, presumably the viral glycoprotein precursor (GPC), is coded in a subgenomic, virus-sense mRNA corresponding to the 5' half of the RNA. Between the two genes is a unique RNA sequence that can be arranged in a hairpin configuration and may function as a transcription terminator for both genes. The term ambisense RNA is coined to describe this novel coding strategy of a viral RNA. The unique feature of the strategy is that the presumptive GPC mRNA and its translation product cannot be made until viral RNA replication has commenced. In addition, it allows the two subgenomic mRNA species to be regulated independently from each other or from other viral mRNA species. The implications of this strategy on possible mechanisms for the induction and maintenance of viral persistence, an important attribute of arenavirus infections, are discussed.
Arenaviridae↗
The formation of arenaviruses that are genetically diploid.
Analyses of RNA extracted from preparations of arenaviruses indicate that the relative molar proportions of the genomic L and S RNA species are frequently far from equal. In order to investigate the genetic significance of this observation temperature-sensitive (ts) mutants of two lymphocytic choriomeningitis (LCM) virus strains (ARM and WE) have been recovered and categorized into recombination groups (Groups I and II). Fingerprint analyses of wild-type progeny viruses obtained from dual infections with ARM Group II and WE Group I ts viruses indicate that they have L/S RNA genotypes of WE/ARM. It is concluded that the ARM Group II ts viruses have mutations in their L RNA species and that the WE Group I ts viruses have mutations in their S RNA species. Correspondingly it is deduced that the ARM Group I ts viruses have S RNA mutations and the WE Group II ts viruses mutations in their L RNA species. Cells coinfected with certain WE Group I mutants, or an ARM Group I and certain WE Group I ts mutants, have also yielded wild-type viruses. Fingerprint analyses have shown that the wild-type viruses obtained from the latter crosses are diploid with respect to their S RNA species. On subsequent passage these wild-type viruses shed high proportions of ts mutants. We interpret the data to indicate that the original Group I ts mutants that yielded the diploid viruses have mutations in different S RNA gene products so that the progeny produce plaques at the nonpermissive temperature by gene product complementation. No wild-type recombinant viruses have been obtained from crosses involving Pichinde and LCM ts mutants.
Arenaviruses, New World↗
[The study of protective properties of attenuated strain of Argentinian hemorrhagic fever].
Immunization of BALB/c, C57BL/6, CBA/calac mice with strain XJ44 of Argentine hemorrhagic fever resulted in changes of nonspecific immunity parameters, such as interferon, interleukin-1, tumor necrosis factor, and natural killers. The formation of a specific humoral and cellular immune response in BALB/c mice immunized with this strain has been demonstrated. Immunization of BALB/c mice with strain XJ44 protected the animals from infection with a heterogeneous strain Carvallo of Bolivian hemorrhagic fever.
Animals↗