Hantaan Virus: Identification of Virion Proteins

Elliott, Luanne H.; Kiley, Michael P.; McCormick, Joseph B.

doi:10.1099/0022-1317-65-8-1285

Cited by 53 publications

(29 citation statements)

References 23 publications

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“…wt.) which may represent the virion-associated polymerase Schmaljohn & Dalrymple, 1984;Elliott et al, 1984). Examination of the kinetics of synthesis of Hantaan virus proteins within infected cells revealed that at a high multiplicity of infection, viral polypeptides could first be detected at 6 h post-infection, quantitatively increased up to 24 h, then remained constant up to 56 h (Schmaljohn & Dalrymple, 1984).…”

Section: Introductionmentioning

confidence: 99%

Hantaan Virus Replication: Effects of Monensin, Tunicamycin and Endoglycosidases on the Structural Glycoproteins

Schmaljohn

Hasty

Rasmussen

et al. 1986

Journal of General Virology

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SUMMARYThe monovalent ionophore monensin, which interferes with cellular transport pathways, and the antibiotic tunicamycin, which prevents glycosylation of newly synthesized proteins, were used to examine Hantaan virus particle formation and polypeptide synthesis. Viral replication in the presence of either drug resulted in reduced antigen production as well as reduced yields of both intracellular and extracellular infectious virus. Analysis of viral polypeptides synthesized in the presence of the drugs suggested differential effects of monensin and tunicamycin on Hantaan virus. Although reduced levels of the three major structural proteins were detected with increasing concentrations of monensin, the electrophoretic migrations of the polypeptides synthesized were unaltered. In contrast, after tunicamycin treatment, G 1 was no longer detectable and G2 displayed both a quantitative reduction and an apparent molecular weight reduction of approximately 3000. Both G1 and G2 were sensitive to endoglycosidases H and F with resultant electrophoretic mobility shifts corresponding to molecular weights of approximately 7000 for G1 and 3000 for G2. Oligosaccharides appeared to be mostly, but not entirely, of the high-mannose type.

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Section: Introductionmentioning

confidence: 99%

Hantaan Virus Replication: Effects of Monensin, Tunicamycin and Endoglycosidases on the Structural Glycoproteins

Schmaljohn

Hasty

Rasmussen

et al. 1986

Journal of General Virology

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“…The S RNA segment encodes the nucleocapsid protein (N) and the M RNA segment encodes a glycoprotein precursor that is cleaved into the envelope glycoproteins G1 and G2 (Schmaljohn et al, 1986(Schmaljohn et al, , 1987Yoo & Kang, 1987b;Giebel et al, 1989;Stohwasser et al, 1990;Parrington & Kang, t990;Arikawa et al, 1990). The L segment is believed to encode the RNA polymerase (Elliott et al, 1984). The G1 and G2 proteins of Hantaan virus have been demonstrated to have neutralizing epitopes (Yamanishi et al, 1984;Dantas et al, 1986;Arikawa et al, 1989;Schmaljohn et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

Molecular Characterization of the Prospect Hill virus M RNA Segment: a Comparison with the M RNA Segments of Other Hantaviruses

Parrington

Lee²,

Kang³

1991

Journal of General Virology

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Complementary DNA representing the genomic M RNA segment of the Prospect Hill (PH) Hantavirus was cloned and its nucleotide sequence determined. The PH virus M RNA segment is 3707 nucleotides in length and has a long open reading frame in the viral complementary-sense RNA with a coding capacity of 1142 amino acids. The predicted gene product of the PH virus M segment was compared with the corresponding gene products of Hantaan virus strain 76-118 (Hantaan), Sapporo rat virus strain SR-11 (SR) and Puumala virus strain H~illn~is B 1 (H~lln~s). The amino acid sequence identities between the G1 and G2 proteins of PH virus and H~illn~is virus are respectively 74% and 79%. In contrast, the amino acid sequence similarities between the G 1 proteins of PH virus and SR virus or Hantaan virus are only 50%. However the G2 proteins of SR and Hantaan viruses were more closely related to the G2 protein of PH virus with amino acid sequence similarities of approximately 62%. The G1 proteins of all four viruses had three potential asparagine-linked glycosylation sites conserved and there was one conserved site in the G2 proteins. Hydrophilicity plots of the four virus glycoproteins were very similar. The region of greatest hydrophilicity was conserved in the H~illn~s, SR and Hantaan viruses, and was located near the C terminus of the G1 protein, whereas the region of greatest hydrophilicity in the PH virus glycoprotein precursor is located closer to the N terminus of the G1 protein. Our data demonstrate that despite differences in the serotypic profiles and virulence of PH and H~lln~s viruses, their G1 and G2 proteins are closely related. We conclude that PH and H~illn~is viruses may have evolved along a separate evolutionary pathway in the Hantavirus genus from that of SR and Hantaan viruses.

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“…Hantaviruses constitute a genus in the Bunyaviridae, a large family of viruses with more than 350 characterized members (6,22,24,32). In contrast to the arthropod-borne members of the other genera (Orthobunya-, Nairo-, Phlebo-, and Tospovirus), hantaviruses are rodent-borne (24).…”

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confidence: 99%

Electron Cryotomography of Tula Hantavirus Suggests a Unique Assembly Paradigm for Enveloped Viruses

Huiskonen

Hepojoki

Laurinmäki

et al. 2010

J Virol

126

169

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Hantaviruses (family Bunyaviridae) are rodent-borne emerging viruses that cause a serious, worldwide threat to human health. Hantavirus diseases include hemorrhagic fever with renal syndrome and hantavirus cardiopulmonary syndrome. Virions are enveloped and contain a tripartite single-stranded negative-sense RNA genome. Two types of glycoproteins, G N and G C , are embedded in the viral membrane and form protrusions, or "spikes." The membrane encloses a ribonucleoprotein core, which consists of the RNA segments, the nucleocapsid protein, and the RNA-dependent RNA polymerase. Detailed information on hantavirus virion structure and glycoprotein spike composition is scarce. Here, we have studied the structures of Tula hantavirus virions using electron cryomicroscopy and tomography. Three-dimensional density maps show how the hantavirus surface glycoproteins, membrane, and ribonucleoprotein are organized. The structure of the G N -G C spike complex was solved to 3.6-nm resolution by averaging tomographic subvolumes. Each spike complex is a square-shaped assembly with 4-fold symmetry. Spike complexes formed ordered patches on the viral membrane by means of specific lateral interactions. These interactions may be sufficient for creating membrane curvature during virus budding. In conclusion, the structure and assembly principles of Tula hantavirus exemplify a unique assembly paradigm for enveloped viruses.

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Hantaan Virus: Identification of Virion Proteins

Cited by 53 publications

References 23 publications

Hantaan Virus Replication: Effects of Monensin, Tunicamycin and Endoglycosidases on the Structural Glycoproteins

Hantaan Virus Replication: Effects of Monensin, Tunicamycin and Endoglycosidases on the Structural Glycoproteins

Molecular Characterization of the Prospect Hill virus M RNA Segment: a Comparison with the M RNA Segments of Other Hantaviruses

Electron Cryotomography of Tula Hantavirus Suggests a Unique Assembly Paradigm for Enveloped Viruses

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