# Molecular characterization of genomic segments of the Prospect Hill strain of Hantavirus and expression of regulatory proteins of human immunodeficiency virus.

 Title: Molecular characterization of genomic segments of the Prospect Hill strain of Hantavirus and expression of regulatory proteins of human immunodeficiency virus. Author: Parrington, Mark A. Abstract: Genomic analyses revealed Prospect Hill-1 (PH) virus has three RNA segments Large (L), Medium (M) and Small (S), like all Bunyaviridae, with relative molecular masses (M$\sb{\rm r}$) of 2.2 $\times$ 10$\sp6,$ 1.3 $\times$ 10$\sp6$ and 0.6 $\times$ 10$\sp6$ respectively. Complementary DNA representing the genomic M RNA segment of the PH virus was cloned and its nucleotide sequence determined. As with other Bunyaviridae the 3$\sp\prime$ and 5$\sp\prime$ termini are inversely complementary and could possibly allow the M RNA segment to form a circular structure. The PH virus M RNA segment has a single long open reading frame (ORF) in the viral complementary-sense RNA. This protein is the putative glycoprotein precursor that would be cleaved into the two viral envelope glycoproteins G1 and G2. The predicted gene product of the PH virus M segment was compared with the corresponding gene products of Hantaan virus, Sapporo rat virus strain SR-11 (SR) virus and Hallnas virus. There was 74% and 79% amino acid sequence similarity between the G1 and G2 proteins of PH virus and Hallnas virus respectively. In contrast, there was only 50% amino acid sequence similarity between the G1 proteins of PH virus and SR virus or Hantaan virus. However, the G2 proteins of SR virus and Hantaan virus were more closely related to the G2 protein of PH virus with amino acid sequence similarity of approximately 62%. Hydrophilicity plots of the four virus glycoproteins were very similar. The region of greatest hydrophilicity was conserved in the Hallnas virus, SR virus and Hantaan virus, and was located near the C-terminus of the G1 protein. In contrast, the region of greatest hydrophilicity in the PH virus glycoprotein precursor was located closer to the N-terminus of the G1 protein. Our data demonstrate that despite differences in the serotypic profiles and virulence of PH virus and Hallnas virus, their G1 and G2 proteins are closely related. Our data demonstrate that despite differences in the serotypic profiles and virulence of PH virus and Hallnas virus, their G1, G2 and N proteins are closely related. We conclude that PH virus and Hallnas virus may have evolved along a separate evolutionary pathway in the Hantavirus genus from SR virus and Hantaan virus. (Abstract shortened by UMI.) Date: 1991 URI: http://hdl.handle.net/10393/7744

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