Characterization of glycoproteins of viruses causing hemorrhagic fever with renal syndrome (HFRS) using monoclonal antibodies

Dantas, Jose R.; Okuno, Yoshinobu; Asada, Hideo; Tamura, Manabu; Takahashi, Michiaki; Tanishita, Osamu; Takahashi, Yoshiyuki; Kurata, T; Yamanishi, Koichi

doi:10.1016/0042-6822(86)90058-9

Cited by 63 publications

(32 citation statements)

References 22 publications

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“…Of the two glycoproteins, the G2 protein was weakly crossreactive between the groups, while the G1 protein appeared to be the least cross-reactive. In a recent study using monoclonal antibodies raised against the G1 and G2 proteins of a Japanese hantavirus (Dantas et al, 1986) it was seen that both glycoproteins carried neutralizing epitopes. In cross-NTs with the 76-118 strain, only some of the anti-G2 monoclonal antibodies crossreacted.…”

Section: Short Communicationmentioning

confidence: 99%

Antigenic Relationship between Hantaviruses Analysed by Immunoprecipitation

Sheshberadaran

Niklasson

Tkachenko

1988

Journal of General Virology

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Section: Short Communicationmentioning

confidence: 99%

Antigenic Relationship between Hantaviruses Analysed by Immunoprecipitation

Sheshberadaran

Niklasson

Tkachenko

1988

Journal of General Virology

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“…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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“…Similarly, in the case of influenza virus and rotavirus, it was demonstrated that CTLs could cross-react with serologically distinct viruses and that cross-reactive anti-influenza virus CTLs mainly recognized viral nucleoprotein (Zweerink et al, 1977;Effros et al, 1977;Yewdell et al, 1985;Offit & Dudzik, 1988). For hantaviruses, which determinant is recognized by cross-reactive CTLs is not clear at this time, but it might be a viral ir~ternal antigen such as a nucleoprotein or polymerase, or a serotype-common viral surface antigen such as the domains related to haemagglutination activity (Dantas et al, 1986).…”

Section: Discussionmentioning

confidence: 99%

Cross-reactive Immunity among Different Serotypes of Virus Causing Haemorrhagic Fever with Renal Syndrome

Asada

Balachandra

Tamura

et al. 1989

Journal of General Virology

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SUMMARYSpleen cells primed by Prospect Hill (PH) or Puumala (Pu) virus could cross-react with Hantaan virus (HV) 76-118 strain-infected target cells after in vitro stimulation with HV-infected cells, although anti-PH or anti-Pu immune serum showed no crossreactive neutralizing (NT) activity to HV without complement. These results and our previous findings with cross-reactive cytotoxic T lymphocytes (CTLs) suggest that some epitopes recognized by CTLs might be common among the hantavirus genus, while the epitopes related to NT activity were mainly specific to each virus of this genus. Next, to evaluate the cross-reactive immunities demonstrated by in vitro study, we investigated the effect of transferring T lymphocytes and sera from BALB/c mice immunized with PH or Pu virus into nude mice before HV inoculation. Transferring T lymphocytes primed by PH or Pu virus reduced HV titres in lungs and spleens of nude mice, corresponding with the results of the in vitro CTL assays. Transferring anti-Pu immune serum also decreased HV titres in nude mice, which seemed to reflect complement-dependent NT activity. Moreover ICR mice previously immunized with PH or Pu virus showed resistance to challenge with a lethal dose of the HV KHF strain, indicating that cross-reactive immunity induced by PH or Pu virus could protect ICR mice against pathogenic HV infection.

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Characterization of glycoproteins of viruses causing hemorrhagic fever with renal syndrome (HFRS) using monoclonal antibodies

Cited by 63 publications

References 22 publications

Antigenic Relationship between Hantaviruses Analysed by Immunoprecipitation

Antigenic Relationship between Hantaviruses Analysed by Immunoprecipitation

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

Cross-reactive Immunity among Different Serotypes of Virus Causing Haemorrhagic Fever with Renal Syndrome

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