The principal RNA species isolated from labeled preparations of the arenavirus Pichinde usually include a large viral RNA species L (apparent molecular weight = 3.2 x 106), and a smaller viral RNA species S (apparent molecular weight = 1.6 x 106). In addition, either little or considerable quantities of 28S rRNA as well as 18S rRNA can also be obtained in virus extracts, depending on the virus stock and growth conditions used to generate virus preparations. Similar RNA species have been identified in RNA extracted from Tacaribe and Tamiami arenavirus preparations. Oligonucleotide fingerprint analyses have confirmed the host ribosomal Qrigin of the 28S and 18S species. Such analyses have also indicated that the Pichinde viral L and S RNA species each contain unique nucleotide sequences. Viral RNA preparations isolated by conventional phenol-sodium dodecyl sulfate extraction often have much of their L and S RNA species in the form of aggregates as visualized by either electron microscopy or oligonucleotide fingerprinting of material recovered from the top of gels (run by using undenatured RNA preparations). Circular and linear RNA forms have also been seen in electron micrographs of undenatured RNA preparations, although denatured viral RNA preparations have yielded mostly linear RNA species with few RNA aggregates or circular forms. Analyses of the structural components of Pias 80S ribosomes of host cell origin (4, 5, 10, 20, chinde virus have established that there is a 21). The function of these ribosomes is unknown. major internal nucleocapsid protein N, (molec-In a recent set of analyses by Rawls and associular weight = 66,000), a large external glycoproates, it was shown that Pichinde virus grown in tein Gl (molecular weight = 64,000), a smaller cells that have temperature-sensitive ribosomes external glycoprotein G2 (molecular weight = yielded progeny virus particles that contained 38,000), as well as minor proteins of unknown thermolabile ribosomes (15). These progeny vifunction or location (23, 25). Tacaribe and Tamruses were capable of productively infecting cells iami viruses have a major nucleocapsid protein at temperatures that were nonpermissive for the N (molecular weights = 68,000 and 66,000, re-integrity of those ribosomes. spectively), a single glycoprotein size class G We have recently reported preliminary anal-(molecular weights = 42,000 and 44,000, respecyses of the RNA species of Pichinde virus preptively), as well as some minor protein species at arations grown from high-temperature-pasleast one of which (molecular weights = 79,000 saged, freshly cloned stocks (24, 25). It was and 77,000, respectively), is associated with the shown that for denatured viral RNA preparaviral nucleocapsids (11). For all three viruses the tions two major size classes of RNA were prespurified viral nucleocapsids have a convoluted, ent, L (apparent molecular weight = 3.2 x 106) beaded appearance (11, 25). For Tacaribe virus and S (apparent molecular weight = 1.6 x 106). the nucleocapsids are reported to be circular...

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The genome complexities of the principal intracellular viral complementary RNA species of the snowshoe hare bunyavirus have been analyzed by duplex analyses involving hybridization of complementary RNA to individual 32P-labeled viral RNA species (large, L; medium, M; and small, S), recovery of nucleaseresistant duplexes, and determination of the oligonucleotide fingerprints of the protected 32P-labeled viral sequences. The result for the M RNA (which codes for the glycoproteins Gl and G2; J. R. Gentsch and D. H. L. Bishop, J. Virol. 30:767-770, 1979) indicates that there is a single polycistronic M mRNA. Similar results were obtained for the L and S RNA species. In vitro translation studies with the S complementary RNA species of snowshoe hare virus as well as melted purified S duplexes substantiate earlier genetic and molecular studies (

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Pichinde virions grown in monolayers of BHK-21 cells were found to contain three major species of virion proteins as described previously (Ramos et al., J. Virol. 10:661-667, 1972). Two of the proteins were glycosylated (G1, molecular weight = 64,000; G2, molecular weight = 38,000) and were present in similar proportions on the outer surface of the virions. A third protein (N, molecular weight = 66,000) was not glycosylated and, in association with the viral RNA species, was the major protein component of the viral nucleocapsids. An estimate of the approximate number of molecules of these three major proteins per virion was made. Minor amounts of other proteins were also routinely observed in Pichinde virus preparations. None of the three major protein species were phosphorylated to any significant extent, nor did they contain sulfated components. Two virion RNA species (L and S), but no 18S rRNA species, were detected in Pichinde virus preparations obtained from infected BHK-21 cells.