Henipavirus RNA in African Bats

Drexler, Jan Felix; Corman, Victor M.; Gloza‐Rausch, Florian; Seebens, Antje; Annan, Augustina; Ipsen, Anne; Kruppa, Thomas; Müller, Marcel A.; Kalko, Elisabeth K. V.; Adu‐Sarkodie, Yaw; Oppong, Samuel; Drosten, Christian

doi:10.1371/journal.pone.0006367

Cited by 198 publications

(178 citation statements)

References 42 publications

Supporting

Mentioning

151

Contrasting

Unclassified

Order By: Relevance

“…Nevertheless, in addition to these countries, the virus has been detected in fruit bats or the bats were seropsitive to NiV antibodies from Cambodia [79], Thailand [90], Indonesia [81], India [23,99], Madagascar in Southern Africa [41] and Ghana in West Africa [22,37]. P. giganteus is the only Pteropus species present in Bangladesh [59].…”

Section: Historical Backgroundmentioning

confidence: 99%

Nipah virus infection: current scenario

et al. 2013

View full text Add to dashboard Cite

show abstract

Section: Historical Backgroundmentioning

confidence: 99%

Nipah virus infection: current scenario

et al. 2013

View full text Add to dashboard Cite

show abstract

“…Hendra virus (HeV), 3 the first known member of the genus Henipavirus within the Paramyxoviridae family, emerged in 1994 as the causative agent of a sudden outbreak of acute respiratory disease in horses in Brisbane, Australia. Nipah virus (NiV), the second known member of the genus Henipavirus, came to light as the etiologic agent of an outbreak of respiratory and central nervous system disease in pigs and humans in Malaysia in 1998 through 1999.…”

mentioning

confidence: 99%

“…Currently this genus contains two virus species and a number of strains isolated from humans, bats, horses, and pigs over a wide geographic area and during a period of 10 years. Notably, henipaviruses have recently also been found outside of Australia and Asia, thus extending the number of endemic regions of one of the most pathogenic virus genera known in humans (3). The susceptibility of humans, the wide host range, and interspecies transmission, together with the absence of therapeutic agents, led to the classification of HeV and NiV as biosecurity level 4 (BSL4) pathogens (4).…”

mentioning

confidence: 99%

Characterization of the Interactions between the Nucleoprotein and the Phosphoprotein of Henipavirus

Habchi

Blangy

Mamelli

et al. 2011

Journal of Biological Chemistry

165

View full text Add to dashboard Cite

The Henipavirus genome is encapsidated by the nucleoprotein (N) within a helical nucleocapsid that recruits the polymerase complex via the phosphoprotein (P). In a previous study, we reported that in henipaviruses, the N-terminal domain of the phosphoprotein and the C-terminal domain of the nucleoprotein (N TAIL ) are both intrinsically disordered. Here we show that Henipavirus N TAIL domains are also disordered in the context of full-length nucleoproteins. We also report the cloning, purification, and characterization of the C-terminal X domains (P XD ) of Henipavirus phosphoproteins. Using isothermal titration calorimetry, we show that N TAIL and P XD form a 1:1 stoichiometric complex that is stable under NaCl concentrations as high as 1 M and has a K D in the M range. Using far-UV circular dichroism and nuclear magnetic resonance, we show that P XD triggers an increase in the ␣-helical content of N TAIL . Using fluorescence spectroscopy, we show that P XD has no impact on the chemical environment of a Trp residue introduced at position 527 of the Henipavirus N TAIL domain, thus arguing for the lack of stable contacts between the C termini of N TAIL and P XD . Finally, we present a tentative structural model of the N TAIL -P XD interaction in which a short, order-prone region of N TAIL (␣-MoRE; amino acids 473-493) adopts an ␣-helical conformation and is embedded between helices ␣2 and ␣3 of P XD , leading to a relatively small interface dominated by hydrophobic contacts. The present results provide the first detailed experimental characterization of the N-P interaction in henipaviruses and designate the N TAIL -P XD interaction as a valuable target for rational antiviral approaches.

show abstract

“…Human cases of NiV infection in these areas have been associated with higher mortality rates of up to Ͼ75%, along with both food-borne and person-to-person transmission (16,31,36,37,46). Serologic and nucleic acid evidence of henipavirus infection, along with a few cases of virus isolation, among various bat species has been reported across a wide geographic range from Oceania and Australia, China, and Southern Asia to Africa (5,13,26,27,30,35,36,45,61,67). Although no connection to human disease occurrence has been reported, these observations suggest a potential threat of henipavirus spillovers in these regions.…”

mentioning

confidence: 99%

Biochemical, Conformational, and Immunogenic Analysis of Soluble Trimeric Forms of Henipavirus Fusion Glycoproteins

Chan

Lu²,

Dutta

et al. 2012

J Virol

View full text Add to dashboard Cite

The henipaviruses, Hendra virus (HeV) and Nipah virus (NiV), are paramyxoviruses discovered in the mid-to late 1990s that possess a broad host tropism and are known to cause severe and often fatal disease in both humans and animals. HeV and NiV infect cells by a pH-independent membrane fusion mechanism facilitated by their attachment (G) and fusion (F) glycoproteins. Here, several soluble forms of henipavirus F (sF) were engineered and characterized. Recombinant sF was produced by deleting the transmembrane (TM) and cytoplasmic tail (CT) domains and appending a glycosylphosphatidylinositol (GPI) anchor signal sequence followed by GPI-phospholipase D digestion, appending a trimeric coiled-coil (GCNt) domain (sF GCNt ), or deleting the TM, CT, and fusion peptide domain. These sF glycoproteins were produced as F 0 precursors, and all were apparent stable trimers recognized by NiV-specific antisera. Surprisingly, however, only the GCNt-appended constructs (sF GCNt ) could elicit cross-reactive henipavirus-neutralizing antibody in mice. In addition, sF GCNt constructs could be triggered in vitro by protease cleavage and heat to transition from an apparent prefusion to postfusion conformation, transitioning through an intermediate that could be captured by a peptide corresponding to the C-terminal heptad repeat domain of F. The pre-and postfusion structures of sF GCNt and non-GCNt-appended sF could be revealed by electron microscopy and were distinguishable by F-specific monoclonal antibodies. These data suggest that only certain sF constructs could serve as potential subunit vaccine immunogens against henipaviruses and also establish important tools for further structural, functional, and diagnostic studies on these important emerging viruses.

show abstract

Henipavirus RNA in African Bats

Cited by 198 publications

References 42 publications

Nipah virus infection: current scenario

Nipah virus infection: current scenario

Characterization of the Interactions between the Nucleoprotein and the Phosphoprotein of Henipavirus

Biochemical, Conformational, and Immunogenic Analysis of Soluble Trimeric Forms of Henipavirus Fusion Glycoproteins

Contact Info

Product

Resources

About