Nipah virus 121791 Nipah virus disease Humans and pigs can be infected with the virus as well as hamsters which serve as an animal model of disease (Guillaume et al., 2004). Pteropid fruit bats are the primary reservoir of Nipah virus (Wiki: Nipah virus). Nipah virus was identified in 1999 when it caused an outbreak of neurological and respiratory disease on pig farms in peninsular Malaysia, resulting in 105 human deaths and the culling of one million pigs. In Singapore, 11 cases including one death occurred in abattoir workers exposed to pigs imported from the affected Malaysian farms. The Nipah virus has been classified by the Centers for Disease Control and Prevention as a Category C agent. The outbreak was originally mistaken for Japanese encephalitis (JE), however, physicians in the area noted that persons who had been vaccinated against JE were not protected, and the number of cases among adults was unusual. Symptoms of infection from the Malaysian outbreak were primarily encephalitic in humans and respiratory in pigs. Later outbreaks have caused respiratory illness in humans, increasing the likelihood of human-to-human transmission and indicating the existence of more dangerous strains of the virus. Based on seroprevalence data and virus isolations, the primary reservoir for Nipah virus was identified as Pteropid fruit bats including Pteropus vampyrus (Large Flying Fox) and Pteropus hypomelanus] (Small Flying-fox), both of which occur in Malaysia. The transmission of Nipah virus from flying foxes to pigs is thought to be due to an increasing overlap between bat habitats and piggeries in peninsular Malaysia. At the index farm, fruit orchards were in close proximity to the piggery, allowing the spillage of urine, faeces and partially eaten fruit onto the pigs. Retrospective studies demonstrate that viral spillover into pigs may have been occurring in Malaysia since 1996 without detection. During 1998, viral spread was aided by the transfer of infected pigs to other farms where new outbreaks occurred (Wiki: Nipah virus). Baboon Papio cynocephalus 9556 Bank vole Clethrionomys glareolus 447135 Bear Ursus americanus 9643 Birds Passeroidea 175121 Brown Trout Salmo trutta 8032 Buffalo Bison bison 9901 Carnivores Vulpes 9625 Cat Felis catus 9685 Catfishes Siluriformes 7995 Cattle Bos taurus 9913 Chicken Gallus gallus 9031 Chimpanzee Pan troglodytes 9598 chinchillas Chinchillidae 10150 Copper Pheasant Syrmaticus soemmerringii 9067 Deer Cervus elaphus 9860 Deer mouse Peromyscus maniculatus 10042 Dog Canis familiaris 9615 Ducks Anas 8835 Ferret Mustela putorius furo 9669 Fish Hyperotreti 117565 Gerbil Gerbillina 10045 Goat Capra hircus 9925 Gray wolf Canis lupus 9612 Guinea pig Cavia porcellus 10141 Hamster Mesocricetus auratus 10036 Horse Equus caballus 9796 Human Homo sapiens 9606 Macaque Macaca fascicularis 9541 Mongolian Gerbil Meriones unguiculatus 10047 Monkey Platyrrhini 9479 Mouse Mus musculus 10090 None None Parrot Psittacidae 9224 Pig Sus scrofa 9823 Rabbit Oryctolagus cuniculus 9986 Rainbow trout Oncorhynchus mykiss 8022 Rat Rattus 10114 Raven Corvus corax 56781 sei whale Balaenoptera borealis 9768 Sheep Ovis aries 9940 Squirrel Spermophilus richardsonii 37591 Tree shrew Tupaiidae 9393 Trouts, salmons & chars Salmoninae 504568 Turkey Meleagris gallopavo 9103 Vole Microtus ochrogaster 79684 Water buffalo Bubalus bubalis 391902 ALVAC-NiV-F VO_0004734 Recombinant vector vaccine Research Intramuscular injection (i.m.) Canarypox virus-based vaccine vectors carrying the fusion protein (ALVAC-F) (Weingartl et al., 2006). Intramuscular injection (i.m.) Recombinant vector construction Canarypox virus-based vaccine vectors carrying the gene for NiV glycoprotein (ALVAC-G) or the fusion protein (ALVAC-F) (Weingartl et al., 2006). Recombinant protein preparation Canarypox virus-based vaccine vectors carrying the gene for NiV glycoprotein (ALVAC-G) or the fusion protein (ALVAC-F) (Weingartl et al., 2006). Four pigs per group were intramuscularly challenged, with either with 10^8 PFU each or in combination of (ALVAC-NiV-G and ALVAC-NiV-F) (Weingartl et al., 2006). VO_0003057 The combined ALVAC-F/G vaccine induced the highest levels of neutralization antibodies (2,560); despite the low neutralizing antibody levels in the F vaccinees (160), all vaccinated animals appeared to be protected against challenge (Weingartl et al., 2006). The pigs were challenged with 2.5 x 10^5 PFU of NiV two weeks later (Weingartl et al., 2006). ALVAC-NiV-G VO_0004733 Recombinant vector vaccine Research Intramuscular injection (i.m.) Canarypox virus-based vaccine vectors carrying the gene for NiV glycoprotein (ALVAC-G) (Weingartl et al., 2006). Intramuscular injection (i.m.) Recombinant vector construction Canarypox virus-based vaccine vectors carrying the gene for NiV glycoprotein (ALVAC-G) or the fusion protein (ALVAC-F) (Weingartl et al., 2006). Recombinant protein preparation Canarypox virus-based vaccine vectors carrying the gene for NiV glycoprotein (ALVAC-G) or the fusion protein (ALVAC-F) (Weingartl et al., 2006). Four pigs per group were intramuscularly challenged, with either with 10^8 PFU each or in combination of (ALVAC-NiV-G and ALVAC-NiV-F) (Weingartl et al., 2006). VO_0003057 The combined ALVAC-F/G vaccine induced the highest levels of neutralization antibodies (2,560); despite the low neutralizing antibody levels in the F vaccinees (160), all vaccinated animals appeared to be protected against challenge (Weingartl et al., 2006). The pigs were challenged with 2.5 x 10^5 PFU of NiV two weeks later (Weingartl et al., 2006). HeV-sG-V Subunit vaccine Licensed Intramuscular injection (i.m.) Alhydrogel and CpG ODN 2006 adjuvants (Geisbert et al., 2021) The virus is stored at −80 °C P1 stock was obtained from CDC, p2 stock was prepared in Vero E6 cells and stored at University of Texas Medical Branch (UTMB) on 30 May 2011. The virus is stored at −80 °C, tested negative for mycoplasma and endotoxin.(Geisbert et al., 2021) Intramuscular injection (i.m.) HeV-sG recombinant antigen(Geisbert et al., 2021) licensed Nipah virus disease human vaccine Generic Unknown VO_0012169 Subunit vaccine Licensed A generic representation of subunit vaccines developed to prevent Nipah virus disease in humans, typically utilizing purified viral proteins such as the glycoprotein G to elicit protective immune responses. These vaccines are designed to provide immunity without the use of live virus, enhancing safety for recipients. NIpah Virus G and F Proteins Subunit Vaccine VO_0011407 Subunit vaccine Research Subcutaneous injection Subcutaneous injection Recombinant protein preparation Recombinant protein preparation For protection studies, inbred golden hamsters (Janvier, Le Fenest St. Isles, France) were vaccinated twice (1 month apart) with 107 PFU of vaccinia virus recombinants expressing either the G or F Nipah virus glycoprotein or with 5 × 106 of each of the recombinants when they were used for coimmunization (Guillaume et al., 2004). Hamsters immunized with F and G proteins were completely protected from lethal Nipah virus challenge (Guillaume et al., 2004). The animals were challenged 3 months after the last immunization with Nipah virus administered interperitoneally (Guillaume et al., 2004). Nipah Virus Vaccine rVSVΔG-NiVBG Recombinant vector vaccine Research recombinant vesicular stomatitis virus [Ref5938:Foster et al., 2022] Intramuscular injection (i.m.) A recombinant VSV-vectored vaccine rapidly protects nonhuman primates against lethal Nipah virus disease. (Foster et al., 2022) Intramuscular injection (i.m.) NiVB G protein Recombinant protein preparation (Foster et al., 2022) All survivors in study 1 and study 2 developed neutralizing antibodies beginning at 7 DPI. Interestingly, animals in study 2 exhibited higher neutralizing antibody titers than subjects in study 1, suggesting a stronger humoral response may be needed to control infection whenever the vaccine is administered at a shorter interval. None of the vector control nor specifically vaccinated animals that succumbed to NiV disease developed neutralizing antibodies. (Foster et al., 2022) For both studies, nine healthy, adult AGMs (African green monkey) were randomized into a group of six experimental animals and a group of three control animals. The six experimental animals were specifically vaccinated by intramuscular injection of 1 × 10^7 PFU of rVSV-ΔG-NiVBG, and control animals were vaccinated by intramuscular injection of 1 × 10^7 PFU of a nonspecific rVSVΔG-EBOV-GP vaccine. (Foster et al., 2022) All monkeys vaccinated with rVSV-ΔG-NiVBG 7 d prior to NiVB exposure were protected from lethal disease, while 67% of animals vaccinated 3 d before NiVB challenge survived. (Foster et al., 2022) For the first study, all nine AGMs were exposed 7 d after vaccination to 5 × 105 PFU of NiVB, with the dose being equally divided between intratracheal and the intranasal routes. For the second study, all AGMs were exposed 3 d after vaccination to 5 × 10^5 PFU of NiVB with the dose being equally divided between the intratracheal and the intranasal routes. (Foster et al., 2022) PHV02 Live recombinant vaccine Research Intramuscular injection (i.m.) PHV02 is a live, recombinant vaccine administered as a single intramuscular injection (Freeman and Levenson, 1966) Intramuscular injection (i.m.) rMV-Ed-G VO_0004714 Recombinant vector vaccine Research Intramuscular injection (i.m.) Recombinant measles virus (rMV) vaccine expressing NiV envelope glycoproteins (rMV-HL-G and rMV-Ed-G) (Yoneda et al., 2013). Intramuscular injection (i.m.) Recombinant vector construction A recombinant measles virus (rMV) vaccine expressing NiV envelope glycoproteins (rMV-HL-G and rMV-Ed-G) (Yoneda et al., 2013). 8-week-old golden hamsters were intraperitoneally immunized with 2×10^4 TCID50 of rMV-HL-G or rMV-Ed-G (Yoneda et al., 2013). VO_0003057 All hamsters vaccinated with rMV-HL-G or rMV-Ed-G showed complete protection. During the observation period (14 days after the challenge), all hamsters immunized with the recombinant MVs showed no clinical symptoms of the disease and survived (Yoneda et al., 2013). All hamsters were challenged intraperitoneally with 10^3 TCID50/animal of NiV (Yoneda et al., 2013). F fusion protein Nipah virus VO_0011314 8164021 8164022 AAF73956.1 CDD:306910 121791 ? fusion protein 5.9 56616.49 602 Fusion glycoprotein F0; pfam00523 >gi|8164021|gb|AF238466.1| Nipah virus fusion protein mRNA, complete cds AGGAGCCAAGCTCTTGCCTCGTTCAGAAGGTTAAACAAGCATTCTTACCATTGGATCAACAAAAGGATTG GTTTTATCGTCTAAGAAATTTATTGAAAGGCAAAGAAATTCCTGGTTTTATGTTGAATGAGGTGTATCAA ACTAAGGAGACCTTCTAACAGCCAGGTCATAGGAATATAAATAAAAATAAGAATAAAATTGATTCCATCG GAAGATTCATTTCAAGAAGTGATCAAATCAAAGCGGTTGGCAGACCTACCAATCATATACCACAAGACTC GACAATGGTAGTTATACTTGACAAGAGATGTTATTGTAATCTTTTAATATTGATTTTGATGATCTCGGAG TGTAGTGTTGGGATTCTACATTATGAGAAATTGAGTAAAATTGGACTTGTCAAAGGAGTAACAAGAAAAT ACAAGATTAAAAGCAATCCTCTCACAAAAGACATTGTTATAAAAATGATTCCGAATGTGTCGAACATGTC TCAGTGCACAGGGAGTGTCATGGAAAATTATAAAACACGATTAAACGGTATCTTAACACCTATAAAGGGA GCGTTAGAGATCTACAAAAACAACACTCATGACCTTGTCGGTGATGTGAGATTAGCCGGAGTTATAATGG CAGGAGTTGCTATTGGGATTGCAACCGCAGCTCAAATCACTGCAGGTGTAGCACTATATGAGGCAATGAA GAATGCTGACAACATCAACAAACTCAAAAGCAGCATTGAATCAACTAATGAAGCTGTCGTTAAACTTCAA GAGACTGCAGAAAAGACAGTCTATGTGCTGACTGCTCTACAGGATTACATTAATACTAATTTAGTACCGA CAATTGACAAGATAAGCTGCAAACAGACAGAACTCTCACTAGATCTGGCATTATCAAAGTACCTCTCTGA TTTGCTTTTTGTATTTGGCCCCAACCTTCAAGACCCAGTTTCTAATTCAATGACTATACAGGCTATATCT CAGGCATTCGGTGGAAATTATGAAACACTGCTAAGAACATTGGGTTACGCTACAGAAGACTTTGATGATC TTCTAGAAAGTGACAGCATAACAGGTCAAATCATCTATGTTGATCTAAGTAGCTACTATATAATTGTCAG GGTTTATTTTCCTATTCTGACTGAAATTCAACAGGCCTATATCCAAGAGTTGTTACCAGTGAGCTTCAAC AATGATAATTCAGAATGGATCAGTATTGTCCCAAATTTCATATTGGTAAGGAATACATTAATATCAAATA TAGAGATTGGATTTTGCCTAATTACAAAGAGGAGCGTGATCTGCAACCAAGATTATGCCACACCTATGAC CAACAACATGAGAGAATGTTTAACGGGATCGACTGAGAAGTGTCCTCGAGAGCTGGTTGTTTCATCACAT GTTCCCAGATTTGCACTATCTAACGGGGTTCTGTTTGCCAATTGCATAAGTGTTACATGTCAGTGTCAAA CAACAGGCAGGGCAATCTCACAATCAGGAGAACAAACTCTGCTGATGATTGACAACACCACCTGTCCTAC AGCCGTACTCGGTAATGTGATTATCAGCTTAGGGAAATATCTGGGGTCAGTAAATTATAATTCTGAAGGC ATTGCTATCGGTCCTCCAGTCTTTACAGATAAAGTTGATATATCAAGTCAGATATCCAGCATGAATCAGT CCTTACAACAGTCTAAGGACTATATCAAAGAGGCTCAACGACTCCTTGATACTGTTAATCCATCATTAAT AAGCATGTTGTCTATGATCATACTGTATGTATTATCGATCGCATCGTTGTGTATAGGGTTGATTACATTT ATCAGTTTTATCATTGTTGAGAAAAAGAGAAACACCTACAGCAGATTAGAGGATAGGAGAGTCAGACCTA CAAGCAGTGGGGATCTCTACTACATTGGGACATAGTGTATTCAGATTGATGAAATTATGTTAGAGAAATC AGAAAACTTCTGACTTTCAGAAATGGATTGTATACAATTAGTTAGATCATCCTGAATAATCGAGGTGAGA ACATTGCAACTATAAAATCAGATCATGTAAATAGTTGTAAAAAATTAAAAGCTTCTTTTAATTCTTTTGA ACAATAATTTAATTAATATATAACATATTCTCTCACACGAGCGCTAACCTATACACTCTCTACTAATATT TTATACTCATAATTAATGATATAATGACAAATAAGGATTCAAATTGGATTATGATATAGTTTCATACTAC AATAGCATTTCGACCAAGAAAATATCCTTACAATTATACAATGTACTTAACCGTGAATATGTAATTGATA ATTTCCCTTTAGAAATTTAATAAAAAA >AAF73956.1 fusion protein [Nipah henipavirus] MVVILDKRCYCNLLILILMISECSVGILHYEKLSKIGLVKGVTRKYKIKSNPLTKDIVIKMIPNVSNMSQ CTGSVMENYKTRLNGILTPIKGALEIYKNNTHDLVGDVRLAGVIMAGVAIGIATAAQITAGVALYEAMKN ADNINKLKSSIESTNEAVVKLQETAEKTVYVLTALQDYINTNLVPTIDKISCKQTELSLDLALSKYLSDL LFVFGPNLQDPVSNSMTIQAISQAFGGNYETLLRTLGYATEDFDDLLESDSITGQIIYVDLSSYYIIVRV YFPILTEIQQAYIQELLPVSFNNDNSEWISIVPNFILVRNTLISNIEIGFCLITKRSVICNQDYATPMTN NMRECLTGSTEKCPRELVVSSHVPRFALSNGVLFANCISVTCQCQTTGRAISQSGEQTLLMIDNTTCPTA VLGNVIISLGKYLGSVNYNSEGIAIGPPVFTDKVDISSQISSMNQSLQQSKDYIKEAQRLLDTVNPSLIS MLSMIILYVLSIASLCIGLITFISFIIVEKKRNTYSRLEDRRVRPTSSGDLYYIGT Protective antigen Hamsters were immunized subcutaneously with either 10^7 PFU of VV-NiV.G or VV-NiV.F expressing the G and F glycoproteins, respectively, or with the two combined. When the VV-NiV.F-vaccinated animals were challenged with Nipah virus 3 months after the last immunization (1,000 PFU/animal intraperitoneally), there was complete protection against mortality [Ref1375:Guillaume et al., 2004]. G glycoprotein Nipah henipavirus VO_0011313 920955 13559814 Nvgp5 AF212302 NP_112027 2VWD 121791 8709 11254 + attachment glycoprotein 8.36 62969.63 602 >NC_002728.1:8709-11254 Nipah virus, complete genome TAGGACCCAGGTCCATAACTCATTGGATACTTAACTGTATCTTTCTAAGCTATCACATATCAAAGGAGAG ATTGAATGCTTTTTTGGAGATCTAGATCATTACTATATGTGTCTCCTATAATCACATCATAGGAGTGAAC CATAATACACATCTTTGGGTAGGGGAAGGAAAGTATTGTTGACGTACTGATTGATCTGCTTGAGTCAAAT AATCAGTCATAACAATTCAAGAAAATGCCGGCAGAAAACAAGAAAGTTAGATTCGAAAATACTACTTCAG ACAAAGGGAAAATTCCTAGTAAAGTTATTAAGAGCTACTACGGAACCATGGACATTAAGAAAATAAATGA AGGATTATTGGACAGCAAAATATTAAGTGCTTTCAACACAGTAATAGCATTGCTTGGATCTATCGTGATC ATAGTGATGAATATAATGATCATCCAAAATTACACAAGATCAACAGACAATCAGGCCGTGATCAAAGATG CGTTGCAGGGTATCCAACAGCAGATCAAAGGGCTTGCTGACAAAATCGGCACAGAGATAGGGCCCAAAGT ATCACTGATTGACACATCCAGTACCATTACTATCCCAGCTAACATTGGGCTGTTAGGTTCAAAGATCAGC CAGTCGACTGCAAGTATAAATGAGAATGTGAATGAAAAATGCAAATTCACACTGCCTCCCTTGAAAATCC ACGAATGTAACATTTCTTGTCCTAACCCACTCCCTTTTAGAGAGTATAGGCCACAGACAGAAGGGGTGAG CAATCTAGTAGGATTACCTAATAATATTTGCCTGCAAAAGACATCTAATCAGATATTGAAGCCAAAGCTG ATTTCATACACTTTACCCGTAGTCGGTCAAAGTGGTACCTGTATCACAGACCCATTGCTGGCTATGGACG AGGGCTATTTTGCATATAGCCACCTGGAAAGAATCGGATCATGTTCAAGAGGGGTCTCCAAACAAAGAAT AATAGGAGTTGGAGAGGTACTAGACAGAGGTGATGAAGTTCCTTCTTTATTTATGACCAATGTCTGGACC CCACCAAATCCAAACACCGTTTACCACTGTAGTGCTGTATACAACAATGAATTCTATTATGTACTTTGTG CAGTGTCAACTGTTGGAGACCCTATTCTGAATAGCACCTACTGGTCCGGATCTCTAATGATGACCCGTCT AGCTGTGAAACCCAAGAGTAATGGTGGGGGTTACAATCAACATCAACTTGCCCTACGAAGTATCGAGAAA GGGAGGTATGATAAAGTTATGCCGTATGGACCTTCAGGCATCAAACAGGGTGACACCCTGTATTTTCCTG CTGTAGGATTTTTGGTCAGGACAGAGTTTAAATACAATGATTCAAATTGTCCCATCACGAAGTGTCAATA CAGTAAACCTGAAAATTGCAGGCTATCTATGGGGATTAGACCAAACAGCCATTATATCCTTCGATCTGGA CTATTAAAATACAATCTATCAGATGGGGAGAACCCCAAAGTTGTATTCATTGAAATATCTGATCAAAGAT TATCTATTGGATCTCCTAGCAAAATCTATGATTCTTTGGGTCAACCTGTTTTCTACCAAGCGTCATTTTC ATGGGATACTATGATTAAATTTGGAGATGTTCTAACAGTCAACCCTCTGGTTGTCAATTGGCGTAATAAC ACGGTAATATCAAGACCCGGGCAATCACAATGCCCTAGATTCAATACATGTCCAGAGATCTGCTGGGAAG GAGTTTATAATGATGCATTCCTAATTGACAGAATCAATTGGATAAGCGCGGGTGTATTCCTTGACAGCAA TCAGACCGCAGAAAATCCTGTTTTTACTGTATTCAAAGATAATGAAATACTTTATAGGGCACAACTGGCT TCTGAGGACACCAATGCACAAAAAACAATAACTAATTGTTTTCTCTTGAAGAATAAGATTTGGTGCATAT CATTGGTTGAGATATATGACACAGGAGACAATGTCATAAGACCCAAACTATTCGCGGTTAAGATACCAGA GCAATGTACATAAAAATCAACCTCATAATTTAATGGATTGATCTAATATAATGATAATAATCGTACAAAG ACATGTGATGTAAACAAAATTGTTGTAATTAAATAAGTCCTCAGCTGAATACTTTTTTAAGATTAGCAAT AGCATGTTTTTCCAGTTATTGGATAGTTGATAATATAATTCTGAAACTGGGTTAATAAATAATCTTGATC GGTGATCTTTGAGAACAATGATATCATATAGTTCATCAAGTGATAATCAATTCTTTATATGTACACTTTA GAGTATATTTTGAGACTTAGTATTTTCGGCCCGAATGTTAAATTTAATAGTTCATACATAACCTAAACTC AAGTTCTAAGCATAATGATAACAATTAATGCGAACTTGTCTTGATGTAAGGAAGATTTGATATTAACTGA GACTCCACTTGATATAGTAGAGCTGAATCTTGTAAATAAATTATAATGAATAGTTTATTCAAAGATTATC ATTCATATTAGTGTAAATTAAGAAAA >NP_112027.1 attachment glycoprotein [Nipah henipavirus] MPAENKKVRFENTTSDKGKIPSKVIKSYYGTMDIKKINEGLLDSKILSAFNTVIALLGSIVIIVMNIMII QNYTRSTDNQAVIKDALQGIQQQIKGLADKIGTEIGPKVSLIDTSSTITIPANIGLLGSKISQSTASINE NVNEKCKFTLPPLKIHECNISCPNPLPFREYRPQTEGVSNLVGLPNNICLQKTSNQILKPKLISYTLPVV GQSGTCITDPLLAMDEGYFAYSHLERIGSCSRGVSKQRIIGVGEVLDRGDEVPSLFMTNVWTPPNPNTVY HCSAVYNNEFYYVLCAVSTVGDPILNSTYWSGSLMMTRLAVKPKSNGGGYNQHQLALRSIEKGRYDKVMP YGPSGIKQGDTLYFPAVGFLVRTEFKYNDSNCPITKCQYSKPENCRLSMGIRPNSHYILRSGLLKYNLSD GENPKVVFIEISDQRLSIGSPSKIYDSLGQPVFYQASFSWDTMIKFGDVLTVNPLVVNWRNNTVISRPGQ SQCPRFNTCPEICWEGVYNDAFLIDRINWISAGVFLDSNQTAENPVFTVFKDNEILYRAQLASEDTNAQK TITNCFLLKNKIWCISLVEIYDTGDNVIRPKLFAVKIPEQCT Protective antigen Hamsters were immunized subcutaneously with either 107 PFU of VV-NiV.G or VV-NiV.F expressing the G and F glycoproteins, respectively, or with the two combined. When the VV-NiV.G-vaccinated animals were challenged with Nipah virus 3 months after the last immunization (1,000 PFU/animal intraperitoneally), there was complete protection against mortality [Ref1375:Guillaume et al., 2004]. Guillaume et al., 2004 journal Guillaume V, Contamin H, Loth P, Georges-Courbot MC, Lefeuvre A, Marianneau P, Chua KB, Lam SK, Buckland R, Deubel V, Wild TF 2004 78 2 834-840 Journal of virology Guillaume et al., 2006 journal Guillaume V, Contamin H, Loth P, Grosjean I, Courbot MC, Deubel V, Buckland R, Wild TF 2006 80 4 1972-1978 Journal of virology Weingartl et al., 2006 journal Weingartl HM, Berhane Y, Caswell JL, Loosmore S, Audonnet JC, Roth JA, Czub M 2006 80 16 7929-7938 Journal of virology Wiki: Nipah virus website http://en.wikipedia.org/wiki/Henipavirus Yoneda et al., 2013 journal Yoneda M, Georges-Courbot MC, Ikeda F, Ishii M, Nagata N, Jacquot F, Raoul H, Sato H, Kai C 2013 8 3 e58414 PloS one