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MeSH Review:

Henipavirus

Rodriguez, J.J. et al., Rodriguez, J.J. et al., Bossart, K.N. et al., Chan, Y.P. et al.

Rodriguez, Horvath, Bossart, Mungall, Crameri, Wang, Eaton, Broder,

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Disease relevance of Henipavirus

Inhibition of Henipavirus fusion and infection by heptad-derived peptides of the Nipah virus fusion glycoprotein [1].

High impact information on Henipavirus

These findings demonstrate a V protein-mediated IFN signal evasion mechanism that is a general property of the known Henipavirus species [2].
Mapping of domains responsible for nucleocapsid protein-phosphoprotein interaction of Henipaviruses [3].
Recent studies have shown that Henipavirus V proteins target STAT proteins by inducing the formation of cytoplasmically localized high molecular weight STAT-containing complexes [4].

References

Inhibition of Henipavirus fusion and infection by heptad-derived peptides of the Nipah virus fusion glycoprotein. Bossart, K.N., Mungall, B.A., Crameri, G., Wang, L.F., Eaton, B.T., Broder, C.C. Virol. J. (2005) [Pubmed]
Hendra virus V protein inhibits interferon signaling by preventing STAT1 and STAT2 nuclear accumulation. Rodriguez, J.J., Wang, L.F., Horvath, C.M. J. Virol. (2003) [Pubmed]
Mapping of domains responsible for nucleocapsid protein-phosphoprotein interaction of Henipaviruses. Chan, Y.P., Koh, C.L., Lam, S.K., Wang, L.F. J. Gen. Virol. (2004) [Pubmed]
Host evasion by emerging paramyxoviruses: Hendra virus and Nipah virus v proteins inhibit interferon signaling. Rodriguez, J.J., Horvath, C.M. Viral Immunol. (2004) [Pubmed]

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