Abstract
Influenza, a serious illness of humans and domesticated animals, has been studied intensively for many years. It therefore provides an example of how much we can learn from detailed studies of an infectious disease and of how even the most intensive scientific research leaves further questions to answer. This introduction is written for researchers who have become interested in one of these unanswered questions, but who may not have previously worked on influenza. To investigate these questions, researchers must not only have a firm grasp of relevant methods and protocols; they must also be familiar with the basic details of our current understanding of influenza. This article therefore briefly covers the burden of disease that has driven influenza research, summarizes how our thinking about influenza has evolved over time, and sets out key features of influenza viruses by discussing how we classify them and what we understand of their replication. It does not aim to be comprehensive, as any researcher will read deeply into the specific areas that have grasped their interest. Instead, it aims to provide a general summary of how we came to think about influenza in the way we do now, in the hope that the reader’s own research will help us to understand it better.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Nee S, Smith JM (1990) The evolutionary biology of molecular parasites. Parasitology 100(Suppl):S5–S18
Isaacs A, Lindenmann J (1957) Virus interference. I. The interferon. Proc R Soc London B Biol Sci 147(927):258–267
Isaacs A, Lindenmann J, Valentine RC (1957) Virus interference. II. Some properties of interferon. Proc R Soc London B Biol Sci 147(927):268–273
Jensen KE, Davenport FM, Hennessy AV, Francis T Jr (1956) Characterization of influenza antibodies by serum absorption. J Exp Med 104(2):199–209
Davenport FM, Hennessy AV, Francis T Jr (1953) Epidemiologic and immunologic significance of age distribution of antibody to antigenic variants of influenza virus. J Exp Med 98(6):641–656
Wang P, Palese P, O'Neill RE (1997) The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal. J Virol 71(3):1850–1856
Shinya K, Ebina M, Yamada S, Ono M, Kasai N, Kawaoka Y (2006) Avian flu: influenza virus receptors in the human airway. Nature 440(7083):435–436. https://doi.org/10.1038/440435a
Townsend AR, Rothbard J, Gotch FM, Bahadur G, Wraith D, McMichael AJ (1986) The epitopes of influenza nucleoprotein recognized by cytotoxic T lymphocytes can be defined with short synthetic peptides. Cell 44(6):959–968
Benson RA, Lawton JC, MacLeod MK (2017) T cell response in the lung following influenza virus infection. Methods Mol Biol 1591:235–248. https://doi.org/10.1007/978-1-4939-6931-9_17
Field J, Nikawa J, Broek D, MacDonald B, Rodgers L, Wilson IA, Lerner RA, Wigler M (1988) Purification of a RAS-responsive adenylyl cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method. Mol Cell Biol 8(5):2159–2165
Carrat F, Vergu E, Ferguson NM, Lemaitre M, Cauchemez S, Leach S, Valleron AJ (2008) Time lines of infection and disease in human influenza: a review of volunteer challenge studies. Am J Epidemiol 167(7):775–785. https://doi.org/10.1093/aje/kwm375
Hirve S, Newman LP, Paget J, Azziz-Baumgartner E, Fitzner J, Bhat N, Vandemaele K, Zhang W (2016) Influenza seasonality in the tropics and subtropics - when to vaccinate? PLoS One 11(4):e0153003. https://doi.org/10.1371/journal.pone.0153003
Lemaitre M, Carrat F (2010) Comparative age distribution of influenza morbidity and mortality during seasonal influenza epidemics and the 2009 H1N1 pandemic. BMC Infect Dis 10:162. https://doi.org/10.1186/1471-2334-10-162
Taubenberger JK, Morens DM (2006) 1918 influenza: the mother of all pandemics. Emerg Infect Dis 12(1):15–22. https://doi.org/10.3201/eid1201.050979
Office C (2017) National risk register of civil emergencies – 2017 edition. https://www.gov.uk/government/publications/national-risk-register-of-civil-emergencies-2017-edition
Morens DM, Taubenberger JK (2010) Historical thoughts on influenza viral ecosystems, or behold a pale horse, dead dogs, failing fowl, and sick swine. Influenza Other Respir Viruses 4(6):327–337. https://doi.org/10.1111/j.1750-2659.2010.00148.x
Daly JM, MacRae S, Newton JR, Wattrang E, Elton DM (2011) Equine influenza: a review of an unpredictable virus. Vet J 189(1):7–14. https://doi.org/10.1016/j.tvjl.2010.06.026
Vincent A, Awada L, Brown I, Chen H, Claes F, Dauphin G, Donis R, Culhane M, Hamilton K, Lewis N, Mumford E, Nguyen T, Parchariyanon S, Pasick J, Pavade G, Pereda A, Peiris M, Saito T, Swenson S, Van Reeth K, Webby R, Wong F, Ciacci-Zanella J (2014) Review of influenza A virus in swine worldwide: a call for increased surveillance and research. Zoonoses Public Health 61(1):4–17. https://doi.org/10.1111/zph.12049
Francis T Jr (1953) Influenza: the new acquaintance. Ann Intern Med 39(2):203–221
Honigsbaum M (2014) Pre-modern influenza. In: A history of the great influenza pandemics: death, panic and hysteria 1890–1920. I.B. Taurus & Co Ltd., London, pp 13–31
Lowen AC, Steel J (2014) Roles of humidity and temperature in shaping influenza seasonality. J Virol 88(14):7692–7695. https://doi.org/10.1128/JVI.03544-13
Taubenberger JK, Hultin JV, Morens DM (2007) Discovery and characterization of the 1918 pandemic influenza virus in historical context. Antivir Ther 12(4 Pt B):581–591
Honigsbaum M (2014) ‘An epidemic started by telegraph’: news, sensation and science. In: A history of the great influenza pandemics: death, panic and hysteria 1890–1920. I.B. Taurus & Co Ltd., London, pp 32–81
Honigsbaum M (2014) ‘An inexpressible dread’: influenza, nervousness and psychosis. In: A history of the great influenza pandemics: death, panic and hysteria 1890–1920. I.B. Taurus & Co Ltd., London, pp 82–117
Morens DM, Taubenberger JK, Fauci AS (2008) Predominant role of bacterial pneumonia as a cause of death in pandemic influenza: implications for pandemic influenza preparedness. J Infect Dis 198(7):962–970. https://doi.org/10.1086/591708
McCullers JA (2014) The co-pathogenesis of influenza viruses with bacteria in the lung. Nat Rev Microbiol 12(4):252–262. https://doi.org/10.1038/nrmicro3231
Radetsky P (1991) The invisible invaders: the story of the emerging age of viruses. Little, Brown & Company, USA
Shope RE (1931) Swine influenza: III. Filtration experiments and etiology. J Exp Med 54(3):373–385
Dochez AR, Mills KC, Kneeland Y (1933) Studies of the etiology of influenza. Proc Soc Exp Biol Med 30(8):1017–1022
Smith W, Andrewes CH, Laidlaw PP (1933) A virus obtained from influenza patients. Lancet 2:66–68
Boos J, August MJ (2013) Of mice and men: animal models of viral infection. In: To catch a virus. ASM Press, Washington, DC, pp 23–50
Gaush CR, Smith TF (1968) Replication and plaque assay of influenza virus in an established line of canine kidney cells. Appl Microbiol 16(4):588–594
Gaush CR, Hard WL, Smith TF (1966) Characterization of an established line of canine kidney cells (MDCK). Proc Soc Exp Biol Med 122(3):931–935
Green IJ (1962) Serial propagation of influenza B (Lee) virus in a transmissible line of canine kidney cells. Science 138(3536):42–43
Adams MJ, Lefkowitz EJ, King AMQ, Harrach B, Harrison RL, Knowles NJ, Kropinski AM, Krupovic M, Kuhn JH, Mushegian AR, Nibert M, Sabanadzovic S, Sanfacon H, Siddell SG, Simmonds P, Varsani A, Zerbini FM, Gorbalenya AE, Davison AJ (2017) Changes to taxonomy and the international code of virus classification and nomenclature ratified by the international committee on taxonomy of viruses (2017). Arch Virol 162(8):2505–2538. https://doi.org/10.1007/s00705-017-3358-5
Andrewes CH, Bang FB, Burnet FM (1955) A short description of the myxovirus group (influenza and related viruses). Virology 1(2):176–184
Burnet FM (1951) Mucoproteins in relation to virus action. Physiol Rev 31(2):131–150
Hirst GK (1941) The agglutination of red cells by allantoic fluid of chick embryos infected with influenza virus. Science 94(2427):22–23. https://doi.org/10.1126/science.94.2427.22
Waterson AP (1962) Two kinds of myxovirus. Nature 193:1163–1164
A revision of the system of nomenclature for influenza viruses: a WHO memorandum (1980). Bull World Health Organ 58(4):585–591
Webster RG, Bean WJ, Gorman OT, Chambers TM, Kawaoka Y (1992) Evolution and ecology of influenza A viruses. Microbiol Rev 56(1):152–179
Horm VS, Gutierrez RA, Nicholls JM, Buchy P (2012) Highly pathogenic influenza A(H5N1) virus survival in complex artificial aquatic biotopes. PLoS One 7(4):e34160. https://doi.org/10.1371/journal.pone.0034160
Tong S, Li Y, Rivailler P, Conrardy C, Castillo DA, Chen LM, Recuenco S, Ellison JA, Davis CT, York IA, Turmelle AS, Moran D, Rogers S, Shi M, Tao Y, Weil MR, Tang K, Rowe LA, Sammons S, Xu X, Frace M, Lindblade KA, Cox NJ, Anderson LJ, Rupprecht CE, Donis RO (2012) A distinct lineage of influenza A virus from bats. Proc Natl Acad Sci U S A 109(11):4269–4274. https://doi.org/10.1073/pnas.1116200109
Tong S, Zhu X, Li Y, Shi M, Zhang J, Bourgeois M, Yang H, Chen X, Recuenco S, Gomez J, Chen LM, Johnson A, Tao Y, Dreyfus C, Yu W, McBride R, Carney PJ, Gilbert AT, Chang J, Guo Z, Davis CT, Paulson JC, Stevens J, Rupprecht CE, Holmes EC, Wilson IA, Donis RO (2013) New world bats harbor diverse influenza A viruses. PLoS Pathog 9(10):e1003657. https://doi.org/10.1371/journal.ppat.1003657
Wang M, Veit M (2016) Hemagglutinin-esterase-fusion (HEF) protein of influenza C virus. Protein Cell 7(1):28–45. https://doi.org/10.1007/s13238-015-0193-x
Hause BM, Ducatez M, Collin EA, Ran Z, Liu R, Sheng Z, Armien A, Kaplan B, Chakravarty S, Hoppe AD, Webby RJ, Simonson RR, Li F (2013) Isolation of a novel swine influenza virus from Oklahoma in 2011 which is distantly related to human influenza C viruses. PLoS Pathog 9(2):e1003176. https://doi.org/10.1371/journal.ppat.1003176
Ferguson L, Olivier AK, Genova S, Epperson WB, Smith DR, Schneider L, Barton K, McCuan K, Webby RJ, Wan XF (2016) Pathogenesis of influenza D virus in cattle. J Virol 90(12):5636–5642. https://doi.org/10.1128/JVI.03122-15
White SK, Ma W, McDaniel CJ, Gray GC, Lednicky JA (2016) Serologic evidence of exposure to influenza D virus among persons with occupational contact with cattle. J Clin Virol 81:31–33. https://doi.org/10.1016/j.jcv.2016.05.017
Hutchinson EC, Charles PD, Hester SS, Thomas B, Trudgian D, Martinez-Alonso M, Fodor E (2014) Conserved and host-specific features of influenza virion architecture. Nat Commun 5:4816. https://doi.org/10.1038/ncomms5816
Rota PA, Wallis TR, Harmon MW, Rota JS, Kendal AP, Nerome K (1990) Cocirculation of two distinct evolutionary lineages of influenza type B virus since 1983. Virology 175(1):59–68
Dudas G, Bedford T, Lycett S, Rambaut A (2015) Reassortment between influenza B lineages and the emergence of a coadapted PB1-PB2-HA gene complex. Mol Biol Evol 32(1):162–172. https://doi.org/10.1093/molbev/msu287
Vijaykrishna D, Holmes EC, Joseph U, Fourment M, Su YC, Halpin R, Lee RT, Deng YM, Gunalan V, Lin X, Stockwell TB, Fedorova NB, Zhou B, Spirason N, Kuhnert D, Boskova V, Stadler T, Costa AM, Dwyer DE, Huang QS, Jennings LC, Rawlinson W, Sullivan SG, Hurt AC, Maurer-Stroh S, Wentworth DE, Smith GJ, Barr IG (2015) The contrasting phylodynamics of human influenza B viruses. elife 4:e05055. https://doi.org/10.7554/eLife.05055
Brooke CB (2017) Population diversity and collective interactions during influenza virus infection. J Virol 91(22):e01164. https://doi.org/10.1128/JVI.01164-17
Kilbourne ED (1968) Recombination of influenza a viruses of human and animal origin. Science 160(3823):74–76. https://doi.org/10.1126/science.160.3823.74
Kilbourne ED (1969) Future influenza vaccines and the use of genetic recombinants. Bull World Health Organ 41(3):643–645
Blazejewska P, Koscinski L, Viegas N, Anhlan D, Ludwig S, Schughart K (2011) Pathogenicity of different PR8 influenza A virus variants in mice is determined by both viral and host factors. Virology 412(1):36–45. https://doi.org/10.1016/j.virol.2010.12.047
Stuart-Harris CH (1939) A neurotropic strain of human influenza virus. Lancet 1:497–499
Schulman JL, Palese P (1977) Virulence factors of influenza A viruses: WSN virus neuraminidase required for plaque production in MDBK cells. J Virol 24(1):170–176
Goto H, Kawaoka Y (1998) A novel mechanism for the acquisition of virulence by a human influenza A virus. Proc Natl Acad Sci U S A 95(17):10224–10228
Goto H, Wells K, Takada A, Kawaoka Y (2001) Plasminogen-binding activity of neuraminidase determines the pathogenicity of influenza A virus. J Virol 75(19):9297–9301. https://doi.org/10.1128/JVI.75.19.9297-9301.2001
Sun X, Tse LV, Ferguson AD, Whittaker GR (2010) Modifications to the hemagglutinin cleavage site control the virulence of a neurotropic H1N1 influenza virus. J Virol 84(17):8683–8690. https://doi.org/10.1128/JVI.00797-10
Kilbourn ED, Schulman JL, Schild GC, Schloer G, Swanson J, Bucher D (1971) Correlated studies of a recombinant influenza-virus vaccine. 1. Derivation and characterization of virus and vaccine. J Infect Dis 124(5):449–462. https://doi.org/10.1093/infdis/124.5.449
Hutchinson EC, Fodor E (2013) Transport of the influenza virus genome from nucleus to nucleus. Viruses 5(10):2424–2446. https://doi.org/10.3390/v5102424
Webster RG, Yakhno M, Hinshaw VS, Bean WJ, Murti KG (1978) Intestinal influenza: replication and characterization of influenza viruses in ducks. Virology 84(2):268–278
Ciminski K, Thamamongood T, Zimmer G, Schwemmle M (2017) Novel insights into bat influenza A viruses. J Gen Virol 98(10):2393–2400. https://doi.org/10.1099/jgv.0.000927
Rogers GN, Paulson JC (1983) Receptor determinants of human and animal influenza virus isolates: differences in receptor specificity of the H3 hemagglutinin based on species of origin. Virology 127(2):361–373
Ito T, Couceiro JN, Kelm S, Baum LG, Krauss S, Castrucci MR, Donatelli I, Kida H, Paulson JC, Webster RG, Kawaoka Y (1998) Molecular basis for the generation in pigs of influenza A viruses with pandemic potential. J Virol 72(9):7367–7373
Lakadamyali M, Rust MJ, Babcock HP, Zhuang X (2003) Visualizing infection of individual influenza viruses. Proc Natl Acad Sci U S A 100(16):9280–9285. https://doi.org/10.1073/pnas.0832269100
Huotari J, Helenius A (2011) Endosome maturation. EMBO J 30(17):3481–3500. https://doi.org/10.1038/emboj.2011.286
Stauffer S, Feng Y, Nebioglu F, Heilig R, Picotti P, Helenius A (2014) Stepwise priming by acidic pH and a high K+ concentration is required for efficient uncoating of influenza A virus cores after penetration. J Virol 88(22):13029–13046. https://doi.org/10.1128/JVI.01430-14
Lan Y, Zhang Y, Dong L, Wang D, Huang W, Xin L, Yang L, Zhao X, Li Z, Wang W, Li X, Xu C, Yang L, Guo J, Wang M, Peng Y, Gao Y, Guo Y, Wen L, Jiang T, Shu Y (2010) A comprehensive surveillance of adamantane resistance among human influenza A virus isolated from mainland China between 1956 and 2009. Antivir Ther 15(6):853–859. https://doi.org/10.3851/IMP1656
Nelson MI, Simonsen L, Viboud C, Miller MA, Holmes EC (2009) The origin and global emergence of adamantane resistant A/H3N2 influenza viruses. Virology 388(2):270–278. https://doi.org/10.1016/j.virol.2009.03.026
White J, Kartenbeck J, Helenius A (1982) Membrane fusion activity of influenza virus. EMBO J 1(2):217–222
Su WC, Chen YC, Tseng CH, Hsu PW, Tung KF, Jeng KS, Lai MM (2013) Pooled RNAi screen identifies ubiquitin ligase itch as crucial for influenza A virus release from the endosome during virus entry. Proc Natl Acad Sci U S A 110(43):17516–17521. https://doi.org/10.1073/pnas.1312374110
Gschweitl M, Ulbricht A, Barnes CA, Enchev RI, Stoffel-Studer I, Meyer-Schaller N, Huotari J, Yamauchi Y, Greber UF, Helenius A, Peter M (2016) A SPOPL/Cullin-3 ubiquitin ligase complex regulates endocytic trafficking by targeting EPS15 at endosomes. elife 5:e13841. https://doi.org/10.7554/eLife.13841
Banerjee I, Miyake Y, Nobs SP, Schneider C, Horvath P, Kopf M, Matthias P, Helenius A, Yamauchi Y (2014) Influenza A virus uses the aggresome processing machinery for host cell entry. Science 346(6208):473–477. https://doi.org/10.1126/science.1257037
Rudnicka A, Yamauchi Y (2016) Ubiquitin in influenza virus entry and innate immunity. Viruses 8(10). https://doi.org/10.3390/v8100293
Eisfeld AJ, Neumann G, Kawaoka Y (2015) At the centre: influenza A virus ribonucleoproteins. Nat Rev Microbiol 13(1):28–41. https://doi.org/10.1038/nrmicro3367
Fodor E (2013) The RNA polymerase of influenza a virus: mechanisms of viral transcription and replication. Acta Virol 57(2):113–122
Hale BG, Albrecht RA, Garcia-Sastre A (2010) Innate immune evasion strategies of influenza viruses. Future Microbiol 5(1):23–41. https://doi.org/10.2217/fmb.09.108
Weber-Gerlach M, Weber F (2016) To conquer the host, influenza virus is packing it in: interferon-antagonistic strategies beyond NS1. J Virol 90(19):8389–8394. https://doi.org/10.1128/JVI.00041-16
Kash JC, Tumpey TM, Proll SC, Carter V, Perwitasari O, Thomas MJ, Basler CF, Palese P, Taubenberger JK, Garcia-Sastre A, Swayne DE, Katze MG (2006) Genomic analysis of increased host immune and cell death responses induced by 1918 influenza virus. Nature 443(7111):578–581. https://doi.org/10.1038/nature05181
Zhou J, Wang D, Gao R, Zhao B, Song J, Qi X, Zhang Y, Shi Y, Yang L, Zhu W, Bai T, Qin K, Lan Y, Zou S, Guo J, Dong J, Dong L, Zhang Y, Wei H, Li X, Lu J, Liu L, Zhao X, Li X, Huang W, Wen L, Bo H, Xin L, Chen Y, Xu C, Pei Y, Yang Y, Zhang X, Wang S, Feng Z, Han J, Yang W, Gao GF, Wu G, Li D, Wang Y, Shu Y (2013) Biological features of novel avian influenza A (H7N9) virus. Nature 499(7459):500–503. https://doi.org/10.1038/nature12379
Bruce EA, Digard P, Stuart AD (2010) The Rab11 pathway is required for influenza A virus budding and filament formation. J Virol 84(12):5848–5859. https://doi.org/10.1128/JVI.00307-10
Amorim MJ, Bruce EA, Read EK, Foeglein A, Mahen R, Stuart AD, Digard P (2011) A Rab11- and microtubule-dependent mechanism for cytoplasmic transport of influenza A virus viral RNA. J Virol 85(9):4143–4156. https://doi.org/10.1128/JVI.02606-10
Momose F, Sekimoto T, Ohkura T, Jo S, Kawaguchi A, Nagata K, Morikawa Y (2011) Apical transport of influenza A virus ribonucleoprotein requires Rab11-positive recycling endosome. PLoS One 6(6):e21123. https://doi.org/10.1371/journal.pone.0021123
Eisfeld AJ, Kawakami E, Watanabe T, Neumann G, Kawaoka Y (2011) RAB11A is essential for transport of the influenza virus genome to the plasma membrane. J Virol 85(13):6117–6126. https://doi.org/10.1128/JVI.00378-11
de Castro Martin IF, Fournier G, Sachse M, Pizarro-Cerda J, Risco C, Naffakh N (2017) Influenza virus genome reaches the plasma membrane via a modified endoplasmic reticulum and Rab11-dependent vesicles. Nat Commun 8(1):1396. https://doi.org/10.1038/s41467-017-01557-6
Vale-Costa S, Alenquer M, Sousa AL, Kellen B, Ramalho J, Tranfield EM, Amorim MJ (2016) Influenza A virus ribonucleoproteins modulate host recycling by competing with Rab11 effectors. J Cell Sci 129(8):1697–1710. https://doi.org/10.1242/jcs.188409
Hengrung N, El Omari K, Serna Martin I, Vreede FT, Cusack S, Rambo RP, Vonrhein C, Bricogne G, Stuart DI, Grimes JM, Fodor E (2015) Crystal structure of the RNA-dependent RNA polymerase from influenza C virus. Nature 527(7576):114–117. https://doi.org/10.1038/nature15525
Thierry E, Guilligay D, Kosinski J, Bock T, Gaudon S, Round A, Pflug A, Hengrung N, El Omari K, Baudin F, Hart DJ, Beck M, Cusack S (2016) Influenza polymerase can adopt an alternative configuration involving a radical repacking of PB2 domains. Mol Cell 61(1):125–137. https://doi.org/10.1016/j.molcel.2015.11.016
Reich S, Guilligay D, Pflug A, Malet H, Berger I, Crepin T, Hart D, Lunardi T, Nanao M, Ruigrok RW, Cusack S (2014) Structural insight into cap-snatching and RNA synthesis by influenza polymerase. Nature 516(7531):361–366. https://doi.org/10.1038/nature14009
Pflug A, Guilligay D, Reich S, Cusack S (2014) Structure of influenza A polymerase bound to the viral RNA promoter. Nature 516(7531):355–360. https://doi.org/10.1038/nature14008
Dadonaite B, Vijayakrishnan S, Fodor E, Bhella D, Hutchinson EC (2016) Filamentous influenza viruses. J Gen Virol 97(8):1755–1764. https://doi.org/10.1099/jgv.0.000535
Rolfes M, Foppa I, Garg S, Flannery B, Brammer L, James A. Singleton (2016) Estimated influenza illnesses, medical visits, hospitalizations, and deaths averted by vaccination in the United States. https://www.cdc.gov/flu/about/disease/2015-16.htm. Accessed 8 Dec 2017
The 20th Century Mortality Files (2011) https://data.gov.uk/dataset/the_20th_century_mortality_files. Accessed 7 Nov 2017
The 21st century mortality files - deaths dataset, England and Wales (2017) https://www.ons.gov.uk/peoplepopulationandcommunity/birthsdeathsandmarriages/deaths/datasets/the21stcenturymortalityfilesdeathsdataset. Accessed 12 Oct 2017
The 21st century mortality files - population dataset, England and Wales (2017) https://www.ons.gov.uk/peoplepopulationandcommunity/populationandmigration/populationestimates/datasets/the21stcenturymortalityfilespopulationdataset. Accessed 12 Oct 2017
Vijayakrishnan S, Loney C, Jackson D, Suphamungmee W, Rixon FJ, Bhella D (2013) Cryotomography of budding influenza a virus reveals filaments with diverse morphologies that mostly do not bear a genome at their distal end. PLoS Pathog 9(6):e1003413
Long JC, Fodor E (2016) The PB2 subunit of the influenza a virus RNA polymerase is imported into the mitochondrial matrix. J Virol 90(19):8729–8738. https://doi.org/10.1128/JVI.01384-16
Author information
Authors and Affiliations
Corresponding authors
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer Science+Business Media, LLC, part of Springer Nature
About this protocol
Cite this protocol
Hutchinson, E.C., Yamauchi, Y. (2018). Understanding Influenza. In: Yamauchi, Y. (eds) Influenza Virus. Methods in Molecular Biology, vol 1836. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-8678-1_1
Download citation
DOI: https://doi.org/10.1007/978-1-4939-8678-1_1
Published:
Publisher Name: Humana Press, New York, NY
Print ISBN: 978-1-4939-8677-4
Online ISBN: 978-1-4939-8678-1
eBook Packages: Springer Protocols