Disease relevance of Hendra Virus

• The V proteins of Nipah virus and Hendra virus have been demonstrated to bind to cellular STAT1 and STAT2 proteins to form high-molecular-weight complexes that inhibit interferon (IFN)-induced antiviral transcription by preventing STAT nuclear accumulation [1].
• Recent examples of viruses that have crossed the species barrier from animal reservoirs to humans are hantavirus, haemorrhagic fever viruses, arboviruses, Nipah and Hendra viruses, avian influenza virus (AI), monkeypox virus, and the SARS-associated coronavirus (SARS-CoV) [2].
• The replication assay was also used to show that the N, P and L proteins of NiV recognize cis-acting sequences in the genomic termini of Hendra virus (HeV) but not measles virus [3].
• The nucleoprotein (N) gene of Hendra virus (HeV), an unclassified member of subfamily Paramyxovirinae in the family Paramyxoviridae previously known as equine morbillivirus, was cloned and sequenced [4].
• The FDLV and Sendai virus cluster in the phylogenetic analysis of L- and F-protein regarding the Paramyxovirus type species and Hendra virus and show the closest relationship [5].

High impact information on Hendra Virus

• Receptor binding, fusion inhibition, and induction of cross-reactive neutralizing antibodies by a soluble G glycoprotein of Hendra virus [6].
• Additionally, we found that purified human cathepsin L processed immunopurified Hendra virus F(0) into F(1) and F(2) fragments [7].
• To analyze the potential role of endocytosis in the processing and membrane fusion promotion of the Hendra virus F protein, mutation of tyrosine 525 to alanine (Hendra virus F Y525A) or phenylalanine (Hendra virus F Y525F) was performed [8].
• Although many paramyxovirus F proteins are proteolytically processed by the cellular protease furin at a multibasic cleavage motif, cleavage of the newly emerged Hendra virus F protein occurs by a previously unidentified cellular protease following a single lysine at residue 109 [7].
• Cathepsin L shRNA-expressing Vero cells transfected with pCAGGS-Hendra F demonstrated a nondetectable amount of cleavage of the Hendra virus F protein and significantly decreased membrane fusion activity [7].

Chemical compound and disease context of Hendra Virus

• RNA synthesis during infection by Hendra virus: an examination by quantitative real-time PCR of RNA accumulation, the effect of ribavirin and the attenuation of transcription [9].
• Reactivity of anti-Nipah virus monoclonal antibodies to formalin-fixed, paraffin-embedded lung tissues from experimental Nipah and Hendra virus infections [10].

Gene context of Hendra Virus

• Hendra virus V protein inhibits interferon signaling by preventing STAT1 and STAT2 nuclear accumulation [11].

References