Summary
Hendra virus (HENV) and Nipah virus (NIPV) are classified in the new genus Henipavirus , within the subfamily Paramyxovirinae, family Paramyxoviridae . The genetic and biological characteristics that differentiate henipaviruses from other members of the subfamily are summarized. Although they do not display neuraminidase and hemagglutination activities and in that regard resemble viruses in the genus Morbillivirus, several recent observations highlight similarities between henipaviruses and respiroviruses (genus Respirovirus in structure and replication strategy. First , three-dimensional modeling studies suggest that the external globular head domain of the HENV G protein resembles that of respiroviruses rather than morbilliviruses. Second, the pattern of transcriptional attenuation in HENV-infected cells resembles that observed with Sendai virus, a respirovirus, and differs from that found in cells infected with measles virus, a morbillivirus. Henipaviruses have a broad host range in vitro and in vivo, indicating wide distribution of cellular receptor molecules. The extensive host range has been confirmed in a quantitative in vitro cell-fusion assay using recombinant vaccinia viruses expressing the attachment and fusion proteins of HENV and NIPV. Cell lines of diverse origin and which are permissive in the in vitro cell fusion assay have been identified and the pattern of relative susceptibilities is the same for both HENV and NIPV, implying that both viruses use the same cell receptor. Protease treatment of permi ssive cells destroys their ability to fuse with cells expressing viral envelope glycoproteins. Virus overlay protein binding assay (VOPBA) and radio-immune precipitation assays confirm that both HENV and NIPV bind to membrane proteins in the 35&3x2013;50 kD range . Treatment of cell membrane proteins with N-glycosidase eliminates HeV binding activity in VOPBA whereas treatment with neuraminidase has no effect on binding. Thus preliminary evidence suggests that NIPV and HENV bind to the same glycoprotein receptor via a non-sialic acid-dependant mechanism.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Alkhatib G, Broder CC, Berger EA (1996) Cell type-specific fusion cofactors determine human immunodeficiency virus type 1 tropism for T-cell lines versus primary macrophages. J Virol 70: 5487–5494
Bagai SL, Lamb RA (1995) Quantitative measurement of paramyxovirus fusion: differences in requirements of glycoproteins between simian virus 5 and human parainfluenza virus 3 or Newcastle disease virus. J Virol 69: 6712–6719
Bossart KN, Wang LF, Eaton BT, Broder CC (2001) Functional expression and membrane fusion tropism of the envelope glycoproteins of Hendra virus. Virology 290: 121–135
Bossart KN, Wang LF, Flora MN, Chua KB, Lam SK, Eaton BT, Broder CC (2002) Membrane fusion tropism and heterotypic functional activities of the Nipah virus and Hendra virus envelope glycoproteins. J Virol 76: 11186–11198
Bowden TR, Westenberg M, Wang LF, Eaton BT, Boyle DB (2001) Molecular characterization of Menangle virus, a novel paramyxovirus which infects pigs, fruit bats, and humans. Virology 283: 358–373
Cattaneo R, Rebmann G, Baczko K, ter Meulen V, Billeter MA (1987) Altered ratios of measles virus transcripts in diseased human brains. Virology 160: 523–526
Chant K, Chan R, Smith M, Dwyer DE, Kirkland P (1998) Probable human infection with a newly described virus in the family Paramyxoviridae. Emerg Infect Dis 4: 273–275
Chua KB, Bellini WJ, Rota PA, Harcourt BH, Tamin A, Lam SK, Ksiazek TG, Rollin PE, Zaki SR, Shieh WJ, Goldsmith CS, Gubler DJ, Roehrig JT, Eaton BT, Gould AR, Olson J, Field H, Daniels P, Ling AE, Peters CJ, Anderson LJ, Mahy BWJ (2000) Nipah virus: A recently emergent deadly paramyxovirus. Science 288: 1432–1435
Chua KB, Wang LF, Lam SK, Eaton BT (2002) Full length genome sequence of Tioman virus, a novel paramyxovirus in the genus Ruhulavirus isolated from fruit bats in Malaysia. Arch Virol 147: 1323–1348
Harcourt BH, Tamin A, Ksiazek TG, Rollin PE, Anderson LJ, Bellini WJ, Rota PA (2000) Molecular characterization of Nipah virus, a newly emergent paramyxovirus. Virology 271: 334–349
Homann HE, Hofschneider PH, Neubert WJ (1990) Sendai virus gene expression in Iytically and persistently infected cells. Virology 177: 131–140
Jorgensen ED, Collins PL, Lomedico PT (1987) Cloning and nucleotide sequence of Newcastle disease virus hemagglutinin-neuraminidase mRNA: identification ofa putative sialic acid binding site. Virology 156: 12–24
Kato A, Kiyotani K, Hasan MK, Shioda T, Sakai Y, Yoshida T, Nagai Y (1999) Sendai virus gene start signals are not equivalent in reinitiation capacity: moderation at the fusion protein gene. J Virol 73: 9237–9246
Lamb RA, Kolakofsky D (2001) Paramyxoviridae: The viruses and their replication. In: Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (eds) Fields virology vol 1. Lippincott, Williams & Wilkins, Philadelphia, pp 1305–1340
Lamb RA, Mahy BW, Choppin PW (1976) The synthesis of Sendai virus polypeptides in infected cells. Virology 69: 116–131
Langedijk JP, Daus FJ, van Oirschot JT (1997) Sequence and structure alignment of Paramyxoviridae attachment proteins and discovery of enzymatic activity for a morbillivirus hemagglutinin. J Virol 71: 6155–6167
Loffler S, Lottspeich F, Lanza F, Azorsa DO, ter Meulen V, Schneider-Schaulies J (1997) CD9, a tetraspan transmembrane protein, render s cell s susceptible to canine distemper virus. J Virol 71: 42–49
Maisner A, Schneider-Schaulies J, Liszewski MK, Atkinson JP, Herrler G (1994) Binding of measles virus to membrane cofactor protein (CD46): importance of disulfide bonds and N-glyc ans for the receptor function. J Virol 68: 6299–6304
Markwell MA, Paulson JC (1980) Sendai virus utilizes specific sialyloligosaccharides as host cell receptor determinants. PNAS 77: 5693–5697
Mirza AM, Deng R, Iorio RM (1994) Site-directed mutagenesis of a conserved hexapeptide in the paramyxovirus hernagglutinin-neuraminidase glycoprotein: effects on antigenic structure and function. J Virol 68: 5093–5099
Murray K, Selleck P, Hooper P, Selleck P, Hyatt A, Gould A, Gleeson L, Westbury H, Hiley L, Selvey L, Rodwell B (1995) A morbilli virus that caused fatal disease in horses and humans. Science 268: 94–97
Naniche D, Varior-Krishnan G, Cervoni F, Wild F, Rossi B, Rabourdin-Cornbe C, Gerlier D (1993) Human membrane cofactor protein (CD46) acts as a cellular receptor for measles virus. J Virol 67: 6025–6032
Nussbaum O, Broder CC, Moss B, Stern LB, Rozenblatt S, Berger EA (1995) Functional and structural interactions between measles virus hemagglutinin and CD46. J Virol 69: 3341–3349
Reyes-Leyva J, Hernandez-Jauregui P, Montafio LF, Zenteno E (1993) The porcine paramyxovirus LPM specifically recognizes sialyl (alpha 2,3) lactose-containing structures. Arch Virol 133: 195–200
Tatsuo H, Ono N, Yanagi Y (2001) Morbilli viruses use signaling Iymphocyte activation molecules (CD150) as cellular receptors. J Virol 75: 5842–5850
Thomas SM, Lamb RA, Paterson RG (1988) Two mRNAs that differ by two nontemplated nucleotides encode the amino coterminal proteins P and V of the paramyxovirus SV5. Cell 54: 891–902
Wang L-F, Chua KB, Yu M, Eaton BT (2003) Genome diversity of emerging paramyxoviruses. Curr Genom 4: 263–273
Wang LF, Eaton BT (2001) Emerging paramyxoviruses. Infect Dis Rev 3: 52–69
Wang LF, Eaton BT (2002) Henipavirus (Paramyxoviridae, Paramyxovirinae). In: Tidona CA, Darai G (eds) The Springer index of viruses. Springer, Berlin Heidelberg New York Tokyo, pp 641–644
Wang LF, Harcourt BH, Yu M, Tamin A, Rota PA, Bellini WJ, Eaton BT (2001) Molecular biology of Hendra and Nipah viruses. Microb Infect 3: 279–287
Westbury HA (2000) Hendra virus disease in horses. Rev Sci Tech Office Int Epizoot 19: 151–159
Yu M, Hansson E, Langedijk JP, Eaton BT, Wang LF (1998) The attachment protein of Hendra virus has high structural similarity but limited primary sequence homology compared with viruses in the genus Paramyxo virus. Virology 251: 227–233
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2004 Springer-Verlag Wien
About this chapter
Cite this chapter
Eaton, B.T. et al. (2004). Henipaviruses: recent observations on regulation of transcription and the nature of the cell receptor. In: Calisher, C.H., Griffin, D.E. (eds) Emergence and Control of Zoonotic Viral Encephalitides. Archives of Virology. Supplementa, vol 18. Springer, Vienna. https://doi.org/10.1007/978-3-7091-0572-6_10
Download citation
DOI: https://doi.org/10.1007/978-3-7091-0572-6_10
Publisher Name: Springer, Vienna
Print ISBN: 978-3-211-20454-2
Online ISBN: 978-3-7091-0572-6
eBook Packages: Springer Book Archive