The family Bunyaviridae is a large and diverse group of enveloped viruses with ribonucleic acid (RNA) genomes. The family consists of over 300 species that are divided into 5 genera. All bunyavirus genomes are comprised of three negative‐sense RNA segments, but they differ in their coding strategies to generate the structural and nonstructural proteins required for replication. Viruses are transmitted by infected vectors that include mosquitoes, phlebotomine flies, ticks and rodents. Bunyaviruses are distributed worldwide and are responsible for a variety of illnesses in human hosts ranging from mild to haemorrhagic fevers or fatal encephalitis. Thus, bunyaviruses are important infectious agents and vector control, precautionary measures, and education are needed to prevent future outbreaks in endemic areas.

Key Concepts

  • Bunyavirus replication occurs in the cytoplasm via a viral RNA‐dependent RNA polymerase.

  • All bunyavirus genomes consist of three negative‐sense RNA segments that encode for structural and/or nonstructural proteins.

  • Structural proteins are required for replication and nonstructural proteins generally play a role in evading host cellular responses.

  • Vectors that transmit bunyaviruses to humans include mosquitoes, phelobotomine flies, ticks and rodents.

  • Symptoms of bunyavirus infection include mild febrile illness, haemorrhagic fever and encephalitis.

  • Bunyaviruses can be found worldwide, so precautionary measures should be taken when travelling to endemic areas.

Keywords: orthobunyavirus; hantavirus; nairovirus; phlebovirus; tospovirus

Figure 1.

(a) Schematic representation of a bunyavirus particle. Virions are 80–120 nm in diameter. The spikes project approximately 5–10 nm above the viral lipid membrane and are composed of hetero‐oligomeric complexes of the glycoproteins, GN and GC (small inset). The three negative‐sense single‐stranded RNA genome segments – small (S), medium (M) and large (L) – are complexed with the N protein (shown in blue), forming ribonucleoprotein (RNPs) complexes. Complementary nucleotides at the 3′‐ and 5′ end of each genome segment undergo base pairing to form panhandle structures (magnified inset). The RNP complexes are likely incorporated into virions through interactions with the C‐terminal tails of the glycoproteins. (b) Ultrastructure of Qalyub virus, genus Nairovirus. Negative stain electron micrograph. Note knob‐like, irregular spikes. Reprinted with permission from Clerx et al., copyright 1981 Society for General Microbiology. (c) Ultrastructure of Crimean–Congo haemorrhagic fever virus, genus Nairovirus. Negative stain electron micrograph. Note dimpled or hollow cavities in spikes. Reproduced with permission from Ellis et al., copyright 1981 Springer. (d) Ultrastructure of Hantaan virus, genus Hantavirus. Negative stain electron micrograph. Note grid‐like arrangement of spikes on virions. Reproduced with permission from Martin et al., copyright 1985 Springer. Structure of Uukuniemi virus as determined by electron cryotomography. Shown are virions with spikes in tall (pH 7) conformation (e) and in flat (pH 6) conformation (f). Insets show close‐ups of the area indicated with dashed lines. Flat spikes have a barrel‐like appearance, whereas taller spikes have a more pointed appearance. The relationship between the five‐coordinated positions (indicated with a pentagon) and six‐coordinated positions (numbered 1–3) is consistent with T=12 triangulation. Bridging densities (indicated by arrows) are present between the spikes at every position and in both conformations. Isosurfaces were rendered at 1.5σ above the mean density. Reproduced with permission from Overby et al., copyright 2008 National Academy of Sciences, USA.

Figure 2.

Coding strategies of the small (S), medium (M) and large (L) genome segments of viruses in the family Bunyaviridae. Host‐derived transcriptional primers are found at the 5′‐termini of all messenger RNAs (mRNAs). These mRNA species are approximately 100 nucleotides shorter than vRNA at the 3′ end and are not polyadenylated. (a) Three different coding strategies have been described for S genome segments. Viruses in the Hantavirus and Nairovirus genera use a simple negative‐sense strategy to encode their nucleocapsid protein (N). Some hantaviruses also possess an overlapping reading frame within the coding sequence for N suggesting that they too may encode an NSS protein. Viruses in the Orthobunyavirus genus encode N and NSS in overlapping reading frames of the complementary RNA (cRNA). A single mRNA is believed to code for both proteins. Viruses in the Phlebovirus and Tospovirus genera use an ambisense strategy to encode their N in the viral cRNA and an NSS protein in the vRNA. (b) All viruses encode their envelope glycoproteins (GN and GC) in a continuous open reading frame in the cRNA. The GN/GC polyprotein precursor is cleaved cotranslationally. In the Hantavirus genus, viruses only encode the envelope glycoproteins whereas those in all other genera encode nonstructural (NSM) proteins as well. In the genera Orthobunyavirus and Nairovirus, NSM is encoded between GN and GC. Phleboviruses (with the exception of UUKV) encode an NSM located N‐terminally to GN and GC that is generated through utilization of an alternative translation initiation site. RVFV also encodes a 78‐kDa nonstructural protein that includes the sequence of both NSM and GN. Nairovirus (e.g. CCHFV) glycoproteins are generated from intermediate precursors termed PreGN and PreGC. In addition, nairoviruses encoded secreted nonstructural proteins at the N‐terminus of PreGN that are generated by endoproteolytic cleavage. Viruses in the Tospovirus genus encode an NSM protein, believed to be a ‘movement protein’ by ambisense coding. (c) Viruses in all genera encode a single protein (L polymerase) in the L segment cRNA. Diagrams are not drawn to scale.



Abraham G and Pattnaik AK (1983) Early RNA synthesis in Bunyamwera virus‐infected cells. Journal of General Virology 64(part 6): 1277–1290.

Altamura LA, Bertolotti‐Ciarlet A, Teigler J et al. (2007) Identification of a novel C‐terminal cleavage of Crimean‐Congo hemorrhagic fever virus PreGN that leads to generation of an NSM protein. Journal of Virology 81(12): 6632–6642.

Anderson GW Jr. and Smith JF (1987) Immunofelectron microscopy of Rift Valley fever viral morphogenesis in primary rat hepatocytes. Virology 161(1): 91–100.

Andersson I, Bladh L, Mousavi‐Jazi M et al. (2004) Human MxA protein inhibits the replication of Crimean‐Congo hemorrhagic fever virus. Journal of Virology 78(8): 4323–4329.

Bertolotti‐Ciarlet A, Smith J, Strecker K et al. (2005) Cellular localization and antigenic characterization of Crimean‐Congo hemorrhagic fever virus glycoproteins. Journal of Virology 79(10): 6152–6161.

Bieniasz PD (2006) Late budding domains and host proteins in enveloped virus release. Virology 344(1): 55–63.

Billecocq A, Spiegel M, Vialat P et al. (2004) NSs protein of Rift Valley fever virus blocks interferon production by inhibiting host gene transcription. Journal of Virology 78(18): 9798–9806.

Bird BH, Albarino CG and Nichol ST (2007) Rift Valley fever virus lacking NSm proteins retains high virulence in vivo and may provide a model of human delayed onset neurologic disease. Virology 362(1): 10–15.

Blakqori G, Delhaye S, Habjan M et al. (2007) La Crosse bunyavirus nonstructural protein NSs serves to suppress the type I interferon system of mammalian hosts. Journal of Virology 81(10): 4991–4999.

Blakqori G and Weber F (2005) Efficient cDNA‐based rescue of La Crosse bunyaviruses expressing or lacking the nonstructural protein NSs. Journal of Virology 79(16): 10420–10428.

Bridgen A and Elliott RM (1996) Rescue of a segmented negative‐strand RNA virus entirely from cloned complementary DNAs. Proceedings of the National Academy of Sciences of the USA 93(26): 15400–15404.

Clerx JP, Casals J and Bishop DH (1981) Structural characteristics of nairoviruses (genus Nairovirus, Bunyaviridae). Journal of General Virology 55(part 1): 165–178.

Donets MA, Chumakov MP, Korolev MB and Rubin SG (1977) Physicochemical characteristics, morphology and morphogenesis of virions of the causative agent of Crimean hemorrhagic fever. Intervirology 8(5): 294–308.

Ellis DS, Southee T, Lloyd G et al. (1981) Congo/Crimean haemorrhagic fever virus from Iraq 1979: I. Morphology in BHK21 cells. Archives of Virology 70(3): 189–198.

Ergonul O (2006) Crimean‐Congo haemorrhagic fever. Lancet Infectious Diseases 6(4): 203–214.

Ergonul O, Celikbas A, Baykam N, Eren S and Dokuzoguz B (2006a) Analysis of risk‐factors among patients with Crimean‐Congo haemorrhagic fever virus infection: severity criteria revisited. Clinical Microbiology and Infection 12(6): 551–554.

Ergonul O, Tuncbilek S, Baykam N, Celikbas A and Dokuzoguz B (2006b) Evaluation of serum levels of interleukin (IL)‐6, IL‐10, and tumor necrosis factor‐alpha in patients with Crimean‐Congo hemorrhagic fever. Journal of Infectious Diseases 193(7): 941–944.

Erickson BR, Deyde V, Sanchez AJ, Vincent MJ and Nichol ST (2006) N‐linked glycosylation of Gn (but not Gc) is important for Crimean Congo hemorrhagic fever virus glycoprotein localization and transport. Virology 361(2): 348–355.

Filone CM, Heise M, Doms RW and Bertolotti‐Ciarlet A (2006) Development and characterization of a Rift Valley fever virus cell‐cell fusion assay using alphavirus replicon vectors. Virology 356(1–2): 155–164.

Flick R, Flick K, Feldmann H and Elgh F (2003) Reverse genetics for Crimean‐Congo hemorrhagic fever virus. Journal of Virology 77(10): 5997–6006.

Fontana J, Lopez‐Montero N, Elliott RM, Fernandez JJ and Risco C (2008) The unique architecture of Bunyamwera virus factories around the Golgi complex. Cell Microbiology 10(10): 2012–2028.

Freiberg AN, Sherman MB, Morais MC, Holbrook MR and Watowich SJ (2008) Three‐dimensional organization of Rift Valley fever virus revealed by cryo‐electron tomography. Journal of Virology 82(21): 10341–10348.

Frias‐Staheli N, Giannakopoulos NV, Kikkert M et al. (2007) Ovarian tumor domain‐containing viral proteases evade ubiquitin‐ and ISG15‐dependent innate immune responses. Cell Host & Microbe 2(6): 404–416.

Garry CE and Garry RF (2004) Proteomics computational analyses suggest that the carboxyl terminal glycoproteins of Bunyaviruses are class II viral fusion protein (beta‐penetrenes). Theoretical Biology & Medical Modelling 1(1): 10.

Gavrilovskaya IN, Brown EJ, Ginsberg MH and Mackow ER (1999) Cellular entry of hantaviruses which cause hemorrhagic fever with renal syndrome is mediated by beta3 integrins. Journal of Virology 73(5): 3951–3959.

Gavrilovskaya IN, Shepley M, Shaw R, Ginsberg MH and Mackow ER (1998) beta3 Integrins mediate the cellular entry of hantaviruses that cause respiratory failure. Proceedings of the National Academy of Sciences of the USA 95(12): 7074–7079.

Gerrard SR, Bird BH, Albarino CG and Nichol ST (2007) The NSm proteins of Rift Valley fever virus are dispensable for maturation, replication and infection. Virology 359(2): 459–465.

Gerrard SR and Nichol ST (2006) Synthesis, proteolytic processing and complex formation of N‐terminally nested precursor proteins of the Rift Valley fever virus glycoproteins. Virology 357(2): 124–133.

Goldfarb LG, Chumakov MP, Myskin AA, Kondratenko VF and Reznikova OY (1980) An epidemiological model of Crimean hemorrhagic fever. American Journal of Tropical Medicine and Hygiene 29(2): 260–264.

Goldsmith CS, Elliott LH, Peters CJ and Zaki SR (1995) Ultrastructural characteristics of Sin Nombre virus, causative agent of hantavirus pulmonary syndrome. Archives of Virology 140(12): 2107–2122.

Hacker JK and Hardy JL (1997) Adsorptive endocytosis of California encephalitis virus into mosquito and mammalian cells: a role for G1. Virology 235(1): 40–47.

Haferkamp S, Fernando L, Schwarz TF, Feldmann H and Flick R (2005) Intracellular localization of Crimean‐Congo hemorrhagic fever (CCHF) virus glycoproteins. Virology Journal 2(1): 42.

Honig JE, Osborne JC and Nichol ST (2004) Crimean‐Congo hemorrhagic fever virus genome L RNA segment and encoded protein. Virology 321(1): 29–35.

ICTVdB (2006) Index of viruses: Bunyaviridae. In: Büchen‐Osmond C (ed.) ICTVdB: The Universal Virus Database, version 4. New York: Columbia University.

Ikegami T, Won S, Peters CJ and Makino S (2006) Rescue of infectious rift valley fever virus entirely from cDNA, analysis of virus lacking the NSs gene, and expression of a foreign gene. Journal of Virology 80(6): 2933–2940.

Jaaskelainen KM, Kaukinen P, Minskaya ES et al. (2007) Tula and Puumala hantavirus NSs ORFs are functional and the products inhibit activation of the interferon‐beta promoter. Journal of Medical Virology 79(10): 1527–1536.

Jacoby DR, Cooke C, Prabakaran I et al. (1993) Expression of the La Crosse M segment proteins in a recombinant vaccinia expression system mediates pH‐dependent cellular fusion. Virology 193(2): 993–996.

Jin M, Park J, Lee S et al. (2002) Hantaan virus enters cells by clathrin‐dependent receptor‐mediated endocytosis. Virology 294(1): 60–69.

Kaukinen P, Vaheri A and Plyusnin A (2003) Non‐covalent interaction between nucleocapsid protein of Tula hantavirus and small ubiquitin‐related modifier‐1, SUMO‐1. Virus Research 92(1): 37–45.

Kikkert M, Van Lent J, Storms M et al. (1999) Tomato spotted wilt virus particle morphogenesis in plant cells. Journal of Virology 73(3): 2288–2297.

Kinsella E, Martin SG, Grolla A et al. (2004) Sequence determination of the Crimean‐Congo hemorrhagic fever virus L segment. Virology 321(1): 23–28.

Kochs G, Janzen C, Hohenberg H and Haller O (2002) Antivirally active MxA protein sequesters La Crosse virus nucleocapsid protein into perinuclear complexes. Proceedings of the National Academy of Sciences of the USA 99(5): 3153–3158.

Kohl A, Clayton RF, Weber F et al. (2003) Bunyamwera virus nonstructural protein NSs counteracts interferon regulatory factor 3‐mediated induction of early cell death. Journal of Virology 77(14): 7999–8008.

Kormelink R, Storms M, Van Lent J, Peters D and Goldbach R (1994) Expression and subcellular location of the NSM protein of tomato spotted wilt virus (TSWV), a putative viral movement protein. Virology 200(1): 56–65.

Korolev MB, Donets MA, Rubin SG and Chumakov MP (1976) Morphology and morphogenesis of Crimean hemorrhagic fever virus. Archives of Virology 50(1–2): 169–172.

Krautkramer E and Zeier M (2008) Hantavirus causing hemorrhagic fever with renal syndrome enters from the apical surface and requires decay‐accelerating factor (DAF/CD55). Journal of Virology 82(9): 4257–4264.

Kuismanen E, Bang B, Hurme M and Pettersson RF (1984) Uukuniemi virus maturation: immunofluorescence microscopy with monoclonal glycoprotein‐specific antibodies. Journal of Virology 51(1): 137–146.

Kukkonen SK, Vaheri A and Plyusnin A (2004) Tula hantavirus L protein is a 250 kDa perinuclear membrane‐associated protein. Journal of General Virology 85(part 5): 1181–1189.

Lappin DF, Nakitare GW, Palfreyman JW and Elliott RM (1994) Localization of Bunyamwera bunyavirus G1 glycoprotein to the Golgi requires association with G2 but not with NSm. Journal of General Virology 75(part 12): 3441–3451.

Le May N, Dubaele S, Proietti De Santis L et al. (2004) TFIIH transcription factor, a target for the Rift Valley hemorrhagic fever virus. Cell 116(4): 541–550.

Le May N, Mansuroglu Z, Leger P et al. (2008) A SAP30 complex inhibits IFN‐beta expression in Rift Valley fever virus infected cells. PLoS Pathogens 4(1): e13.

Leonard VH, Kohl A, Hart TJ and Elliott RM (2006) Interaction of Bunyamwera Orthobunyavirus NSs protein with mediator protein MED8: a mechanism for inhibiting the interferon response. Journal of Virology 80(19): 9667–9675.

Li XD, Makela TP, Guo D et al. (2002) Hantavirus nucleocapsid protein interacts with the Fas‐mediated apoptosis enhancer Daxx. Journal of General Virology 83(part 4): 759–766.

Lowen AC, Noonan C, McLees A and Elliott RM (2004) Efficient bunyavirus rescue from cloned cDNA. Virology 330(2): 493–500.

Ludwig GV, Christensen BM, Yuill TM and Schultz KT (1989) Enzyme processing of La Crosse virus glycoprotein G1: a bunyavirus‐vector infection model. Virology 171(1): 108–113.

Maeda A, Lee BH, Yoshimatsu K et al. (2003) The intracellular association of the nucleocapsid protein (NP) of hantaan virus (HTNV) with small ubiquitin‐like modifier‐1 (SUMO‐1) conjugating enzyme 9 (Ubc9). Virology 305(2): 288–297.

Martin ML, Lindsey‐Regnery H, Sasso DR, McCormick JB and Palmer E (1985) Distinction between Bunyaviridae genera by surface structure and comparison with Hantaan virus using negative stain electron microscopy. Archives of Virology 86(1–2): 17–28.

Mir MA and Panganiban AT (2005) The hantavirus nucleocapsid protein recognizes specific features of the viral RNA panhandle and is altered in conformation upon RNA binding. Journal of Virology 79(3): 1824–1835.

Mir MA and Panganiban AT (2006) The bunyavirus nucleocapsid protein is an RNA chaperone: possible roles in viral RNA panhandle formation and genome replication. RNA (New York, NY) 12(2): 272–282.

Murphy FA, Harrison AK and Tzianabos T (1968) Electron microscopic observations of mouse brain infected with Bunyamwera group arboviruses. Journal of Virology 2(11): 1315–1325.

Murphy FA, Harrison AK and Whitfield SG (1973) Bunyaviridae: morphologic and morphogenetic similarities of Bunyamwera serologic supergroup viruses and several other arthropod‐borne viruses. Intervirology 1(4): 297–316.

Nakitare GW and Elliott RM (1993) Expression of the Bunyamwera virus M genome segment and intracellular localization of NSm. Virology 195(2): 511–520.

Novoa RR, Calderita G, Cabezas P, Elliott RM and Risco C (2005) Key Golgi factors for structural and functional maturation of Bunyamwera virus. Journal of Virology 79(17): 10852–10863.

Ogino M, Yoshimatsu K, Ebihara H et al. (2004) Cell fusion activities of Hantaan virus envelope glycoproteins. Journal of Virology 78(19): 10776–10782.

Overby AK, Pettersson RF, Grunewald K and Huiskonen JT (2008) Insights into bunyavirus architecture from electron cryotomography of Uukuniemi virus. Proceedings of the National Academy of Sciences of the USA 105(7): 2375–2379.

Overby AK, Pettersson RF and Neve EP (2007a) The glycoprotein cytoplasmic tail of Uukuniemi virus (Bunyaviridae) interacts with ribonucleoproteins and is critical for genome packaging. Journal of Virology 81(7): 3198–3205.

Overby AK, Popov V, Neve EP and Pettersson RF (2006) Generation and analysis of infectious virus‐like particles of Uukuniemi virus (Bunyaviridae): a useful system for studying bunyaviral packaging and budding. Journal of Virology 80(21): 10428–10435.

Overby AK, Popov VL, Pettersson RF and Neve EP (2007b) The cytoplasmic tails of Uukuniemi virus (Bunyaviridae) G(N) and G(C) glycoproteins are important for intracellular targeting and the budding of virus‐like particles. Journal of Virology 81(20): 11381–11391.

Papa A, Bino S, Velo E et al. (2006) Cytokine levels in Crimean‐Congo hemorrhagic fever. Journal of Clinical Virology 36(4): 272–276.

Patterson JL, Holloway B and Kolakofsky D (1984) La Crosse virions contain a primer‐stimulated RNA polymerase and a methylated cap‐dependent endonuclease. Journal of Virology 52(1): 215–222.

Patterson JL and Kolakofsky D (1984) Characterization of La Crosse virus small‐genome transcripts. Journal of Virology 49(3): 680–685.

Pekosz A and Gonzalez‐Scarano F (1996) The extracellular domain of La Crosse virus G1 forms oligomers and undergoes pH‐dependent conformational changes. Virology 225(1): 243–247.

Plassmeyer ML, Soldan SS, Stachelek KM, Martin‐Garcia J and Gonzalez‐Scarano F (2005) California serogroup Gc (G1) glycoprotein is the principal determinant of pH‐dependent cell fusion and entry. Virology 338(1): 121–132.

Plassmeyer ML, Soldan SS, Stachelek KM et al. (2007) Mutagenesis of the La Crosse virus glycoprotein supports a role for Gc (1066–1087) as the fusion peptide. Virology 358(2): 273–282.

Pollitt E, Zhao J, Muscat P and Elliott RM (2006) Characterization of Maguari Orthobunyavirus mutants suggests the nonstructural protein NSm is not essential for growth in tissue culture. Virology 348(1): 224–232.

Porterfield JS, Casals J, Chumakov MP et al. (1974) Bunyaviruses and Bunyaviridae. Intervirology 2(4): 270–272.

Ramanathan HN, Chung DH, Plane SJ et al. (2007) Dynein‐dependent transport of the hantaan virus nucleocapsid protein to the endoplasmic reticulum‐Golgi intermediate compartment. Journal of Virology 81(16): 8634–8647.

Ramanathan HN and Jonsson CB (2008) New and Old World hantaviruses differentially utilize host cytoskeletal components during their life cycles. Virology 374(1): 138–150.

Ravkov EV and Compans RW (2001) Hantavirus nucleocapsid protein is expressed as a membrane‐associated protein in the perinuclear region. Journal of Virology 75(4): 1808–1815.

Ravkov EV, Nichol ST and Compans RW (1997) Polarized entry and release in epithelial cells of Black Creek Canal virus, a New World hantavirus. Journal of Virology 71(2): 1147–1154.

Ravkov EV, Nichol ST, Peters CJ and Compans RW (1998) Role of actin microfilaments in Black Creek Canal virus morphogenesis. Journal of Virology 72(4): 2865–2870.

Ronka H, Hilden P, Von Bonsdorff CH and Kuismanen E (1995) Homodimeric association of the spike glycoproteins G1 and G2 of Uukuniemi virus. Virology 211(1): 241–250.

Rwambo PM, Shaw MK, Rurangirwa FR and DeMartini JC (1996) Ultrastructural studies on the replication and morphogenesis of Nairobi sheep disease virus, a Nairovirus. Archives of Virology 141(8): 1479–1492.

Salanueva IJ, Novoa RR, Cabezas P et al. (2003) Polymorphism and structural maturation of Bunyamwera virus in Golgi and post‐Golgi compartments. Journal of Virology 77(2): 1368–1381.

Sanchez AJ, Vincent MJ, Erickson BR and Nichol ST (2006) Crimean‐Congo hemorrhagic fever virus glycoprotein precursor is cleaved by furin‐like and SKI‐1 proteases to generate a novel 38‐kilodalton glycoprotein. Journal of Virology 80(1): 514–525.

Sanchez AJ, Vincent MJ and Nichol ST (2002) Characterization of the glycoproteins of Crimean‐Congo hemorrhagic fever virus. Journal of Virology 76(14): 7263–7275.

Schmaljohn CS and LeDuc JW (1999) Bunyaviridae. In: Mahy BWJ and Collier L (eds) Topley and Wilson's Microbiology and Microbial Infections, vol. 2, pp. 601–628. London: Edward Arnold.

Schmaljohn CS and Nichol ST (2007) Bunyaviridae. In: Knipe DM and Howley PM (eds) Fields Virology, 5th edn, pp. 1741–1789. Philadelphia: Lippincott Williams & Wilkins.

Shi X, Brauburger K and Elliott RM (2005) Role of N‐linked glycans on Bunyamwera virus glycoproteins in intracellular trafficking, protein folding, and virus infectivity. Journal of Virology 79(21): 13725–13734.

Shi X, Kohl A, Leonard VH et al. (2006) Requirement of the N‐terminal region of Orthobunyavirus nonstructural protein NSm for virus assembly and morphogenesis. Journal of Virology 80(16): 8089–8099.

Soellick T, Uhrig JF, Bucher GL, Kellmann JW and Schreier PH (2000) The movement protein NSm of tomato spotted wilt tospovirus (TSWV): RNA binding, interaction with the TSWV N protein, and identification of interacting plant proteins. Proceedings of the National Academy of Sciences of the USA 97(5): 2373–2378.

Soldan SS, Plassmeyer ML, Matukonis MK and Gonzalez‐Scarano F (2005) La Crosse virus nonstructural protein NSs counteracts the effects of short interfering RNA. Journal of Virology 79(1): 234–244.

Storms MM, Kormelink R, Peters D, Van Lent JW and Goldbach RW (1995) The nonstructural NSm protein of tomato spotted wilt virus induces tubular structures in plant and insect cells. Virology 214(2): 485–493.

Swanepoel R, Gill DE, Shepherd AJ et al. (1989) The clinical pathology of Crimean‐Congo hemorrhagic fever. Reviews of Infectious Diseases 11(suppl. 4): S794–S800.

Swanepoel R, Shepherd AJ, Leman PA et al. (1987) Epidemiologic and clinical features of Crimean‐Congo hemorrhagic fever in southern Africa. American Journal of Tropical Medicine and Hygiene 36(1): 120–132.

Thomas D, Blakqori G, Wagner V et al. (2004) Inhibition of RNA polymerase II phosphorylation by a viral interferon antagonist. Journal of Biological Chemistry 279(30): 31471–31477.

Tischler ND, Gonzalez A, Perez‐Acle T, Rosemblatt M and Valenzuela PD (2005) Hantavirus Gc glycoprotein: evidence for a class II fusion protein. Journal of General Virology 86(part 11): 2937–2947.

Vincent MJ, Sanchez AJ, Erickson BR et al. (2003) Crimean‐Congo hemorrhagic fever virus glycoprotein proteolytic processing by subtilase SKI‐1. Journal of Virology 77(16): 8640–8649.

Weber F, Bridgen A, Fazakerley JK et al. (2002) Bunyamwera bunyavirus nonstructural protein NSs counteracts the induction of alpha/beta interferon. Journal of Virology 76(16): 7949–7955.

Whitfield AE, Ullman DE and German TL (2004) Expression and characterization of a soluble form of tomato spotted wilt virus glycoprotein GN. Journal of Virology 78(23): 13197–13206.

Whitfield AE, Ullman DE and German TL (2005) Tomato spotted wilt virus glycoprotein G(C) is cleaved at acidic pH. Virus Research 110(1–2): 183–186.

Wichmann D, Grone HJ, Frese M et al. (2002) Hantaan virus infection causes an acute neurological disease that is fatal in adult laboratory mice. Journal of Virology 76(17): 8890–8899.

Won S, Ikegami T, Peters CJ and Makino S (2007) NSm protein of Rift Valley fever virus suppresses virus‐induced apoptosis. Journal of Virology 81(24): 13335–13345.

Further Reading

Clements AC, Pfeiffer DU, Martin V and Otte MJ (2007) A Rift Valley fever atlas for Africa. Preventive Veterinary Medicine 82: 72–82.

Ergonul O (2008) Treatement of Crimean‐Congo hemorrhagic fever. Antiviral Research 78: 125–131.

Jonson CB, Hooper J and Mertz G (2008) Treatement of hantavirus pulmonary syndrome. Antiviral Research 78: 162–169.

Martin V, Chevalier V, Ceccato P et al. (2008) The impact of climate change on the epidemiology and control of Rift Valley fever. Revue Scientifique Et Technique 27: 413–426.

Morikawa S, Saijo M and Kurane I (2007) Recent progress in molecular biology of Crimean‐Congo hemorrhagic fever. Comparative Immunology, Microbiology and Infectious Diseases 30: 375–389.

Vaheri A, Vapalahti O and Plyusnin A (2008) How to diagnose hantavirus infections and detect them in rodents and insectivores. Reviews in Medical Virology 18: 277–288.

Vorou R, Pierroutsakos IN and Maltezou HC (2007) Crimean‐Congo hemorrhagic fever. Current Opinion in Infectious Diseases 20: 495–500.

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Taylor, Shannon L, Altamura, Louis A, and Schmaljohn, Connie S(Mar 2009) Bunyaviridae. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1002/9780470015902.a0001012.pub2]