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Journal articles on the topic 'Influenza B virus'

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Published: 4 June 2021

Last updated: 2 February 2022

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1

McCullers, Jonathan A., Sergio Facchini, P. Joan Chesney, and Robert G. Webster. "Influenza B Virus Encephalitis." Clinical Infectious Diseases 28, no. 4 (April 1999): 898–900. http://dx.doi.org/10.1086/515214.

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2

FRANK, ARTHUR L., LARRY H. TABER, and CHERYL M. PORTER. "INFLUENZA B VIRUS REINFECTION." American Journal of Epidemiology 125, no. 4 (April 1987): 576–86. http://dx.doi.org/10.1093/oxfordjournals.aje.a114571.

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3

Osterhaus, A. D. "Influenza B Virus in Seals." Science 288, no. 5468 (May 12, 2000): 1051–53. http://dx.doi.org/10.1126/science.288.5468.1051.

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4

Mao, Steve. "Stressed out by influenza virus." Science 362, no. 6412 (October 18, 2018): 301.2–301. http://dx.doi.org/10.1126/science.362.6412.301-b.

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5

Nakajima, S., F. Nishikawa, K. Nakamura, H. Nakao, and K. Nakajima. "Reinfection with influenza B virus in children: analysis of the reinfection influenza B viruses." Epidemiology and Infection 113, no. 1 (August 1994): 103–12. http://dx.doi.org/10.1017/s0950268800051517.

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SUMMARYInfluenza B virus reinfection in Japanese children was studied epidemi-ologically during 1979–91 and virologically during 1985–91. During this investigation, there were four epidemics caused by influenza B viruses, each of which accompanied antigenic drift. Between the epidemics in 1987/88 and 1989/90, the viruses changed drastically, both genetically and antigenically. The minimum rate of reinfection with influenza B virus during the whole period was 3–25% depending on the influenza seasons. The antigens of primary and reinfection strains of influenza B virus isolated from 18 children during 1985–90, which covered three epidemic periods, were studied by haemagglutination inhibition tests. The results showed that the viruses isolated in the 1984/85 and 1987/88 influenza seasons, which belonged to the same lineage, were antigenically close, and reinfection occurred with these viruses. The results of amino-acid analysis of the HA1 polypeptide of these viruses corresponded with those of antigenic analysis. There were no specific amino-acid changes shared by the primary infection and reinfection influenza B viruses; the patients were infected with the viruses epidemic at that time.

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6

Wanitchang, Asawin, Jaraspim Narkpuk, Peera Jaru-ampornpan, Juggagarn Jengarn, and Anan Jongkaewwattana. "Inhibition of influenza A virus replication by influenza B virus nucleoprotein: An insight into interference between influenza A and B viruses." Virology 432, no. 1 (October 2012): 194–203. http://dx.doi.org/10.1016/j.virol.2012.06.016.

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7

Bodewes, Rogier, Danny Morick, Gerrie de Mutsert, Nynke Osinga, Theo Bestebroer, Stefan van der Vliet, Saskia L. Smits, et al. "Recurring Influenza B Virus Infections in Seals." Emerging Infectious Diseases 19, no. 3 (March 2013): 511–12. http://dx.doi.org/10.3201/eid1903.120965.

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8

Nogales, Aitor, Irene Rodríguez-Sánchez, Kristen Monte, Deborah J. Lenschow, Daniel R. Perez, and Luis Martínez-Sobrido. "Replication-competent fluorescent-expressing influenza B virus." Virus Research 213 (February 2016): 69–81. http://dx.doi.org/10.1016/j.virusres.2015.11.014.

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9

&NA;. "Sialidase inhibitors: influenza B virus resistance emerges." Inpharma Weekly &NA;, no. 1582-1583 (April 2007): 14. http://dx.doi.org/10.2165/00128413-200715820-00038.

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10

Kugelberg, Elisabeth. "Promoting B cell responses to influenza virus." Nature Reviews Immunology 14, no. 5 (April 7, 2014): 283. http://dx.doi.org/10.1038/nri3662.

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11

Flandorfer, Astrid, Adolfo García-Sastre, Christopher F. Basler, and Peter Palese. "Chimeric Influenza A Viruses with a Functional Influenza B Virus Neuraminidase or Hemagglutinin." Journal of Virology 77, no. 17 (September 1, 2003): 9116–23. http://dx.doi.org/10.1128/jvi.77.17.9116-9123.2003.

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ABSTRACT Reassortment of influenza A and B viruses has never been observed in vivo or in vitro. Using reverse genetics techniques, we generated recombinant influenza A/WSN/33 (WSN) viruses carrying the neuraminidase (NA) of influenza B virus. Chimeric viruses expressing the full-length influenza B/Yamagata/16/88 virus NA grew to titers similar to that of wild-type influenza WSN virus. Recombinant viruses in which the cytoplasmic tail or the cytoplasmic tail and the transmembrane domain of the type B NA were replaced with those of the type A NA were impaired in tissue culture. This finding correlates with reduced NA content in virions. We also generated a recombinant influenza A virus expressing a chimeric hemagglutinin (HA) protein in which the ectodomain is derived from type B/Yamagata/16/88 virus HA, whereas both the cytoplasmic and the transmembrane domains are derived from type A/WSN virus HA. This A/B chimeric HA virus did not grow efficiently in MDCK cells. However, after serial passage we obtained a virus population that grew to titers as high as wild-type influenza A virus in MDCK cells. One amino acid change in position 545 (H545Y) was found to be responsible for the enhanced growth characteristics of the passaged virus. Taken together, we show here that the absence of reassortment between influenza viruses belonging to different A and B types is not due to spike glycoprotein incompatibility at the level of the full-length NA or of the HA ectodomain.

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12

Rotteveel, F. T. M., E. Braakman, B. Robbe, and C. J. Lucas. "Recognition of influenza virus-infected B-cell lines by human influenza virus-specific CTL." Cellular Immunology 111, no. 2 (February 1988): 473–81. http://dx.doi.org/10.1016/0008-8749(88)90110-4.

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13

Tan, Jessica, Guha Asthagiri Arunkumar, and Florian Krammer. "Universal influenza virus vaccines and therapeutics: where do we stand with influenza B virus?" Current Opinion in Immunology 53 (August 2018): 45–50. http://dx.doi.org/10.1016/j.coi.2018.04.002.

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14

To, Janet, and Jaume Torres. "Viroporins in the Influenza Virus." Cells 8, no. 7 (June 29, 2019): 654. http://dx.doi.org/10.3390/cells8070654.

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Influenza is a highly contagious virus that causes seasonal epidemics and unpredictable pandemics. Four influenza virus types have been identified to date: A, B, C, and D, where only A–C are known to infect humans. Influenza A (IAV) and B (IBV) viruses are responsible for seasonal influenza epidemics in humans and are responsible for up to a billion flu infections annually. The M2 protein is present in all influenza types and belongs to the class of viroporins (i.e., small proteins that form ion channels that increase membrane permeability in virus-infected cells). In influenza A and B, AM2 and BM2 are predominantly proton channels, although they also show some permeability to monovalent cations. In contrast, M2 proteins in influenza C (ICV) and D (IDV), CM2 and DM2, appear to be especially selective for chloride ions, with possibly some permeability to protons. These differences point to different biological roles for M2 in types A and B versus C and D, which is also reflected in their sequences. AM2 is by far the best characterized viroporin, and mechanistic details and rationale of its acid activation, proton selectivity, unidirectionality and relative low conductance are just beginning to be understood. The present review summarizes the biochemical and structural aspects of influenza viroporins and discusses the most relevant aspects of function, inhibition and interaction with the host.

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15

Ñamendys-Silva, Silvio A., María O. González-Herrera, Julia Texcocano-Becerra, and Angel Herrera-Gómez. "Acute Respiratory Distress Syndrome Caused by Influenza B Virus Infection in a Patient with Diffuse Large B-Cell Lymphoma." Case Reports in Medicine 2011 (2011): 1–4. http://dx.doi.org/10.1155/2011/647528.

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Influenza B virus infections are less common than infections caused by influenza A virus in critically ill patients, but similar mortality rates have been observed for both influenza types. Pneumonia caused by influenza B virus is uncommon and has been reported in pediatric patients and previously healthy adults. Critically ill patients with pneumonia caused by influenza virus may develop acute respiratory distress syndrome. We describe the clinical course of a critically ill patient with diffuse large B-cell lymphoma nongerminal center B-cell phenotype who developed acute respiratory distress syndrome caused by influenza B virus infection. This paper emphasizes the need to suspect influenza B virus infection in critically ill immunocompromised patients with progressive deterioration of cardiopulmonary function despite treatment with antibiotics. Early initiation of neuraminidase inhibitor and the implementation of guidelines for management of severe sepsis and septic shock should be considered.

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16

Ping, Jihui, Tiago J. S. Lopes, Gabriele Neumann, and Yoshihiro Kawaoka. "Development of high-yield influenza B virus vaccine viruses." Proceedings of the National Academy of Sciences 113, no. 51 (December 5, 2016): E8296—E8305. http://dx.doi.org/10.1073/pnas.1616530113.

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The burden of human infections with influenza A and B viruses is substantial, and the impact of influenza B virus infections can exceed that of influenza A virus infections in some seasons. Over the past few decades, viruses of two influenza B virus lineages (Victoria and Yamagata) have circulated in humans, and both lineages are now represented in influenza vaccines, as recommended by the World Health Organization. Influenza B virus vaccines for humans have been available for more than half a century, yet no systematic efforts have been undertaken to develop high-yield candidates. Therefore, we screened virus libraries possessing random mutations in the six “internal” influenza B viral RNA segments [i.e., those not encoding the major viral antigens, hemagglutinin (HA) and neuraminidase NA)] for mutants that confer efficient replication. Candidate viruses that supported high yield in cell culture were tested with the HA and NA genes of eight different viruses of the Victoria and Yamagata lineages. We identified combinations of mutations that increased the titers of candidate vaccine viruses in mammalian cells used for human influenza vaccine virus propagation and in embryonated chicken eggs, the most common propagation system for influenza viruses. These influenza B virus vaccine backbones can be used for improved vaccine virus production.

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17

Wanitchang, Asawin, Phonphimon Wongthida, and Anan Jongkaewwattana. "Influenza B virus M2 protein can functionally replace its influenza A virus counterpart in promoting virus replication." Virology 498 (November 2016): 99–108. http://dx.doi.org/10.1016/j.virol.2016.08.016.

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18

Gao, Qinshan, Edward W. A. Brydon, and Peter Palese. "A Seven-Segmented Influenza A Virus Expressing the Influenza C Virus Glycoprotein HEF." Journal of Virology 82, no. 13 (April 30, 2008): 6419–26. http://dx.doi.org/10.1128/jvi.00514-08.

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ABSTRACT Influenza viruses are classified into three types: A, B, and C. The genomes of A- and B-type influenza viruses consist of eight RNA segments, whereas influenza C viruses only have seven RNAs. Both A and B influenza viruses contain two major surface glycoproteins: the hemagglutinin (HA) and the neuraminidase (NA). Influenza C viruses have only one major surface glycoprotein, HEF (hemagglutinin-esterase fusion). By using reverse genetics, we generated two seven-segmented chimeric influenza viruses. Each possesses six RNA segments from influenza virus A/Puerto Rico/8/34 (PB2, PB1, PA, NP, M, and NS); the seventh RNA segment encodes either the influenza virus C/Johannesburg/1/66 HEF full-length protein or a chimeric protein HEF-Ecto, which consists of the HEF ectodomain and the HA transmembrane and cytoplasmic regions. To facilitate packaging of the heterologous segment, both the HEF and HEF-Ecto coding regions are flanked by HA packaging sequences. When introduced as an eighth segment with the NA packaging sequences, both viruses are able to stably express a green fluorescent protein (GFP) gene, indicating a potential use for these viruses as vaccine vectors to carry foreign antigens. Finally, we show that incorporation of a GFP RNA segment enhances the growth of seven-segmented viruses, indicating that efficient influenza A viral RNA packaging requires the presence of eight RNA segments. These results support a selective mechanism of viral RNA recruitment to the budding site.

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19

Wang, Qinghua, Feng Cheng, Mingyang Lu, Xia Tian, and Jianpeng Ma. "Crystal Structure of Unliganded Influenza B Virus Hemagglutinin." Journal of Virology 82, no. 6 (January 9, 2008): 3011–20. http://dx.doi.org/10.1128/jvi.02477-07.

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ABSTRACT Here we report the crystal structure of hemagglutinin (HA) from influenza B/Hong Kong/8/73 (B/HK) virus determined to 2.8 Å. At a sequence identity of ∼25% to influenza A virus HAs, B/HK HA shares a similar overall structure and domain organization. More than two dozen amino acid substitutions on influenza B virus HAs have been identified to cause antigenicity alteration in site-specific mutants, monoclonal antibody escape mutants, or field isolates. Mapping these substitutions on the structure of B/HK HA reveals four major epitopes, the 120 loop, the 150 loop, the 160 loop, and the 190 helix, that are located close in space to form a large, continuous antigenic site. Moreover, a systematic comparison of known HA structures across the entire influenza virus family reveals evolutionarily conserved ionizable residues at all regions along the chain and subunit interfaces. These ionizable residues are likely the structural basis for the pH dependence and sensitivity to ionic strength of influenza HA and hemagglutinin-esterase fusion proteins.

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20

Hatta, Masato, Hideo Goto, and Yoshihiro Kawaoka. "Influenza B Virus Requires BM2 Protein for Replication." Journal of Virology 78, no. 11 (June 1, 2004): 5576–83. http://dx.doi.org/10.1128/jvi.78.11.5576-5583.2004.

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ABSTRACT The BM2 protein of influenza B virus functions as an ion channel, which is suggested to be important for virus uncoating in endosomes of virus-infected cells. Because direct support for this function is lacking, whether BM2 plays an essential role in the viral life cycle remains unknown. We therefore attempted to generate BM2 knockout viruses by reverse genetics. Mutant viruses possessing M segments with the mutated initiation codon of BM2 protein at the stop-start pentanucleotide were viable and still expressed BM2. The introduction of multiple stop codons and a one-nucleotide deletion downstream of the stop-start pentanucleotide, in addition to disablement of the BM2 initiation codon, failed to generate viable mutant viruses, but the mutant M segments still expressed proteins that reacted with the BM2 peptide antiserum. To completely abolish BM2 expression, we generated a mutant M gene whose BM2 open reading frame was deleted. Although this mutant was not able to replicate in normal MDCK cells, it did replicate in a cell line that we established which constitutively expresses BM2. Furthermore, a virus possessing the mutant M gene lacking the BM2 open reading frame and a mutant NA gene containing the BM2 open reading frame instead of the NA open reading frame underwent multiple cycles of replication in MDCK cells, with exogenous sialidase used to supplement the deleted viral sialidase activity. These findings demonstrate that the BM2 protein is essential for influenza B virus replication.

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21

Mäkelä, Sanna M., Pamela Österlund, Veera Westenius, Sinikka Latvala, Michael S. Diamond, Michael Gale, and Ilkka Julkunen. "RIG-I Signaling Is Essential for Influenza B Virus-Induced Rapid Interferon Gene Expression." Journal of Virology 89, no. 23 (September 16, 2015): 12014–25. http://dx.doi.org/10.1128/jvi.01576-15.

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ABSTRACTInfluenza B virus causes annual epidemics and, along with influenza A virus, accounts for substantial disease and economic burden throughout the world. Influenza B virus infects only humans and some marine mammals and is not responsible for pandemics, possibly due to a very low frequency of reassortment and a lower evolutionary rate than that of influenza A virus. Influenza B virus has been less studied than influenza A virus, and thus, a comparison of influenza A and B virus infection mechanisms may provide new insight into virus-host interactions. Here we analyzed the early events in influenza B virus infection and interferon (IFN) gene expression in human monocyte-derived macrophages and dendritic cells. We show that influenza B virus induces IFN regulatory factor 3 (IRF3) activation and IFN-λ1 gene expression with faster kinetics than does influenza A virus, without a requirement for viral protein synthesis or replication. Influenza B virus-induced activation of IRF3 required the fusion of viral and endosomal membranes, and nuclear accumulation of IRF3 and viral NP occurred concurrently. In comparison, immediate early IRF3 activation was not observed in influenza A virus-infected macrophages. Experiments with RIG-I-, MDA5-, and RIG-I/MDA5-deficient mouse fibroblasts showed that RIG-I is the critical pattern recognition receptor needed for the influenza B virus-induced activation of IRF3. Our results show that innate immune mechanisms are activated immediately after influenza B virus entry through the endocytic pathway, whereas influenza A virus avoids early IRF3 activation and IFN gene induction.IMPORTANCERecently, a great deal of interest has been paid to identifying the ligands for RIG-I under conditions of natural infection, as many previous studies have been based on transfection of cells with different types of viral or synthetic RNA structures. We shed light on this question by analyzing the earliest step in innate immune recognition of influenza B virus by human macrophages. We show that influenza B virus induces IRF3 activation, leading to IFN gene expression after viral RNPs (vRNPs) are released into the cytosol and are recognized by RIG-I receptor, meaning that the incoming influenza B virus is already able to activate IFN gene expression. In contrast, influenza A (H3N2) virus failed to activate IRF3 at very early times of infection, suggesting that there are differences in innate immune recognition between influenza A and B viruses.

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22

Voeten, J. T. M., J. Groen, D. van Alphen, E. C. J. Claas, R. de Groot, A. D. M. E. Osterhaus, and G. F. Rimmelzwaan. "Use of Recombinant Nucleoproteins in Enzyme-Linked Immunosorbent Assays for Detection of Virus-Specific Immunoglobulin A (IgA) and IgG Antibodies in Influenza Virus A- or B-Infected Patients." Journal of Clinical Microbiology 36, no. 12 (1998): 3527–31. http://dx.doi.org/10.1128/jcm.36.12.3527-3531.1998.

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The nucleoprotein genes of influenza virus A/Netherlands/018/94 (H3N2) and influenza virus B/Harbin/7/94 were cloned into the bacterial expression vector pMalC to yield highly purified recombinant influenza virus A and B nucleoproteins. With these recombinant influenza nucleoproteins, enzyme-linked immunosorbent assays (ELISAs) were developed for the detection of influenza virus A- and B-specific immunoglobulin A (IgA) and IgG serum antibodies. Serum samples were collected at consecutive time points after the onset of clinical symptoms from patients with confirmed influenza virus A or B infections. Nucleoprotein-specific IgA antibodies were detected in 41.2% of influenza virus A-infected patients and in 66.7% of influenza virus B-infected patients on day 6 after the onset of clinical symptoms. In serum samples taken on day 21 (influenza virus A-infected patients) or day 28 (influenza virus B-infected patients), nucleoprotein-specific IgA antibodies could be detected in 58.8 and 58.3% of influenza virus A- and B-infected patients, respectively. At the same time, IgG antibody rises were detected in 88.2% of influenza virus A-infected patients and in 95.8% of influenza virus B-infected patients. On comparison, hemagglutination inhibition assays detected antibody titer rises in 81.3 and 72.7% of patients infected with influenza viruses A and B, respectively. In contrast to the detection of nucleoprotein-specific IgG antibodies or hemagglutination-inhibiting antibodies, the detection of nucleoprotein-specific IgA antibodies does not require paired serum samples and therefore can be considered an attractive alternative for the rapid serological diagnosis of influenza.

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23

Huber, Victor C., Loren H. Kleimeyer, and Jonathan A. McCullers. "Live, attenuated influenza virus (LAIV) vehicles are strong inducers of immunity toward influenza B virus." Vaccine 26, no. 42 (October 2008): 5381–88. http://dx.doi.org/10.1016/j.vaccine.2008.07.086.

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24

Shen, Ching-Fen, Tzong-Shiann Ho, Shih-Min Wang, Yu-Ting Liao, Yu-Shiang Hu, Huey-Pin Tsai, and Shun-Hua Chen. "The cellular immunophenotype expression of influenza A virus and influenza B virus infection in children." Clinical Immunology 219 (October 2020): 108548. http://dx.doi.org/10.1016/j.clim.2020.108548.

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25

Lam, Jonathan H., and Nicole Baumgarth. "The Multifaceted B Cell Response to Influenza Virus." Journal of Immunology 202, no. 2 (January 7, 2019): 351–59. http://dx.doi.org/10.4049/jimmunol.1801208.

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26

TROENDLE, JANE F., GAIL J. DEMMLER, W. PAUL GLEZEN, MILTON FINEGOLD, and MICHAEL J. ROMANO. "Fatal influenza B virus pneumonia in pediatric patients." Pediatric Infectious Disease Journal 11, no. 2 (February 1992): 117–21. http://dx.doi.org/10.1097/00006454-199202000-00011.

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27

Hoffmann, E., K. Mahmood, C. F. Yang, R. G. Webster, H. B. Greenberg, and G. Kemble. "Rescue of influenza B virus from eight plasmids." Proceedings of the National Academy of Sciences 99, no. 17 (August 9, 2002): 11411–16. http://dx.doi.org/10.1073/pnas.172393399.

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28

Peltola, Ville, Thedi Ziegler, and Olli Ruuskanen. "Influenza A and B Virus Infections in Children." Clinical Infectious Diseases 36, no. 3 (February 2003): 299–305. http://dx.doi.org/10.1086/345909.

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29

Rothaeusler, Kristina, and Nicole Baumgarth. "B-cell fate decisions following influenza virus infection." European Journal of Immunology 40, no. 2 (February 2010): 366–77. http://dx.doi.org/10.1002/eji.200939798.

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30

Shen, Jun, Brian D. Kirk, Jianpeng Ma, and Qinghua Wang. "Diversifying selective pressure on influenza B virus hemagglutinin." Journal of Medical Virology 81, no. 1 (November 21, 2008): 114–24. http://dx.doi.org/10.1002/jmv.21335.

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31

Tamez, Rebecca L., Whitney V. Tan, John T. O'Malley, Karen R. Broder, Maria C. Garzon, Philip LaRussa, and Christine T. Lauren. "Influenza B virus infection and Stevens-Johnson syndrome." Pediatric Dermatology 35, no. 1 (December 28, 2017): e45-e48. http://dx.doi.org/10.1111/pde.13370.

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32

Paul Glezen, W. "Editorial Commentary: Changing Epidemiology of Influenza B Virus." Clinical Infectious Diseases 59, no. 11 (August 19, 2014): 1525–26. http://dx.doi.org/10.1093/cid/ciu668.

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33

Vianello, F. A., S. Osnaghi, E. A. Laicini, G. P. Milani, G. Tardini, A. M. Cappellari, G. Lunghi, C. V. Agostoni, and E. F. Fossali. "Optic neuritis associated with influenza B virus meningoencephalitis." Journal of Clinical Virology 61, no. 3 (November 2014): 463–65. http://dx.doi.org/10.1016/j.jcv.2014.09.010.

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34

Chen, Rubing, and Edward C. Holmes. "The Evolutionary Dynamics of Human Influenza B Virus." Journal of Molecular Evolution 66, no. 6 (May 27, 2008): 655–63. http://dx.doi.org/10.1007/s00239-008-9119-z.

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35

Demers, Andrew, Zhiguang Ran, Qiji Deng, Dan Wang, Brody Edman, Wuxun Lu, and Feng Li. "Palmitoylation is required for intracellular trafficking of influenza B virus NB protein and efficient influenza B virus growth in vitro." Journal of General Virology 95, no. 6 (June 1, 2014): 1211–20. http://dx.doi.org/10.1099/vir.0.063511-0.

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All influenza viruses bud and egress from lipid rafts within the apical plasma membrane of infected epithelial cells. As a result, all components of progeny virions must be transported to these lipid rafts for assembly and budding. Although the mechanism of transport for other influenza proteins has been elucidated, influenza B virus (IBV) glycoprotein NB subcellular localization and transport are not understood completely. To address the aforementioned properties of NB, a series of trafficking experiments were conducted. Here, we showed that NB co-localized with markers specific for the endoplasmic reticulum (ER) and Golgi region. The data from chemical treatment of NB-expressing cells by Brefeldin A, a fungal antibiotic and a known chemical inhibitor of the protein secretory pathway, further confirmed that NB is transported through the ER–Golgi pathway as it restricted NB localization to the perinuclear region. Using NB deletion mutants, the hydrophobic transmembrane domain was identified as being required for NB transport to the plasma membrane. Furthermore, palmitoylation was also required for transport of NB to the plasma membrane. Systematic mutation of cysteines to serines in NB demonstrated that cysteine 49, likely in a palmitoylated form, is also required for transport to the plasma membrane. Surprisingly, further analysis demonstrated that in vitro replication of NBC49S mutant virus was delayed relative to the parental IBV. The results demonstrated that NB is the third influenza virus protein to have been shown to be palmitoylated and together these findings may aid in future studies aimed at elucidating the function of NB.

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36

Green, Robin. "When “B” becomes “A”: the emerging threat of influenza B virus." African Journal of Thoracic and Critical Care Medicine 25, no. 4 (December 6, 2019): 156. http://dx.doi.org/10.7196/sarj.2019.v25i4.038.

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37

Sharma, Lokesh, Andre Rebaza, and Charles S. Dela Cruz. "When “B” becomes “A”: the emerging threat of influenza B virus." European Respiratory Journal 54, no. 2 (August 2019): 1901325. http://dx.doi.org/10.1183/13993003.01325-2019.

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38

Yasui, Hisako, Junko Kiyoshima, Tetuji Hori, and Kan Shida. "Protection against Influenza Virus Infection of Mice Fed Bifidobacterium breve YIT4064." Clinical Diagnostic Laboratory Immunology 6, no. 2 (March 1, 1999): 186–92. http://dx.doi.org/10.1128/cdli.6.2.186-192.1999.

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ABSTRACT Mice fed Bifidobacterium breve YIT4064 and immunized orally with influenza virus were more strongly protected against influenza virus infection of the lower respiratory tract than ones immunized with influenza virus only. The number of mice with enhanced anti-influenza virus immunoglobulin G (IgG) in serum upon oral administration of B. breve YIT4064 and oral immunization with influenza virus was significantly greater than that upon oral immunization with influenza virus only. These findings demonstrated that the oral administration of B. breve YIT4064 increased anti-influenza virus IgG antibodies in serum and protected against influenza virus infection. The oral administration of B. breve YIT4064 may enhance antigen-specific IgG against various pathogenic antigens taken orally and induce protection against various virus infections.

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39

Laursen, Nick S., Robert H. E. Friesen, Xueyong Zhu, Mandy Jongeneelen, Sven Blokland, Jan Vermond, Alida van Eijgen, et al. "Universal protection against influenza infection by a multidomain antibody to influenza hemagglutinin." Science 362, no. 6414 (November 1, 2018): 598–602. http://dx.doi.org/10.1126/science.aaq0620.

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Broadly neutralizing antibodies against highly variable pathogens have stimulated the design of vaccines and therapeutics. We report the use of diverse camelid single-domain antibodies to influenza virus hemagglutinin to generate multidomain antibodies with impressive breadth and potency. Multidomain antibody MD3606 protects mice against influenza A and B infection when administered intravenously or expressed locally from a recombinant adeno-associated virus vector. Crystal and single-particle electron microscopy structures of these antibodies with hemagglutinins from influenza A and B viruses reveal binding to highly conserved epitopes. Collectively, our findings demonstrate that multidomain antibodies targeting multiple epitopes exhibit enhanced virus cross-reactivity and potency. In combination with adeno-associated virus–mediated gene delivery, they may provide an effective strategy to prevent infection with influenza virus and other highly variable pathogens.

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Kiseleva, Irina, Elena Krutikova, Ekaterina Stepanova, Svetlana Donina, Maria Pisareva, Vera Krivitskaya, Andrey Rekstin, Erin Grace Sparrow, Guido Torelli, and Larisa Rudenko. "Cross-Protective Efficacy of Monovalent Live Influenza B Vaccines against Genetically Different Lineages of B/Victoria and B/Yamagata in Ferrets." BioMed Research International 2018 (August 30, 2018): 1–11. http://dx.doi.org/10.1155/2018/9695628.

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Background.Currently, two genetic lineages of influenza B virus, B/Victoria and B/Yamagata, are cocirculating in humans in various countries. This situation has raised a question regarding the possibility of cross-protection between B components of live attenuated influenza vaccine (LAIV) belonging to different lineages. This study aimed to assess in naïve ferrets the potential protective activity of monovalent B-LAIVs against challenge with homologous and heterologous wild-type (WT) influenza B viruses.Methods.Groups of seronegative female ferrets 5-6 months of age were given one dose of monovalent LAIV based on B/Victoria or B/Yamagata lineage virus. Ferrets were challenged 21 days later with B/Victoria or B/Yamagata WT virus. Ferrets were monitored closely for clinical signs and morbidity outcomes including febrile response, body weight loss, nasal symptoms, and level of activity one week prior to vaccination and for three days following vaccination/challenge. Nasal washes were collected three days after vaccination/challenge. Samples of lung tissue were taken three days after challenge. All samples were analyzed for the presence of challenge virus by culturing in embryonated chicken eggs and real-time polymerase chain reaction. Antibody response to vaccination was assessed by routine hemagglutination inhibition assay and microneutralization test.Results.Vaccination led to intensive production of specific neutralizing and antihemagglutinating antibodies to vaccine virus, protected ferrets from homologous challenge infection, and significantly reduced clinical signs and replication of homologous challenge virus. In contrast, cross-lineage serum antibodies were not detected. However, ferrets vaccinated with monovalent B-LAIV had a significantly lower level of heterologous challenge virus in the respiratory tract than those given challenge virus only.Conclusions.Monovalent B-LAIV has the potential to be cross-protective against infection with genetically different influenza lineages. Further studies are required to confirm this effect.

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Nolte, Frederick S., Lori Gauld, and Susan B. Barrett. "Direct Comparison of Alere i and cobas Liat Influenza A and B Tests for Rapid Detection of Influenza Virus Infection." Journal of Clinical Microbiology 54, no. 11 (August 31, 2016): 2763–66. http://dx.doi.org/10.1128/jcm.01586-16.

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We compared two rapid, point-of care nucleic acid amplification tests for detection of influenza A and B viruses (Alere i [Alere] and cobas Liat [Roche Diagnostics]) with the influenza A and B virus test components of the FilmArray respiratory panel (BioFire Diagnostics) using 129 respiratory specimens collected in universal viral transport medium (80 influenza A virus and 16 influenza B virus positive) from both adult and pediatric patients. The sensitivities of the Alere test were 71.3% for influenza A virus and 93.3% for influenza B virus, with specificities of 100% for both viruses. The sensitivities and specificities of the Liat test were 100% for both influenza A and B viruses. The poor sensitivity of the Alere test for detection of influenza A virus was likely due to a study set that included many low-positive samples that were below its limit of detection.

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Ghebremedhin, B., I. Engelmann, W. König, and B. König. "Comparison of the performance of the rapid antigen detection actim Influenza A&B test and RT-PCR in different respiratory specimens." Journal of Medical Microbiology 58, no. 3 (March 1, 2009): 365–70. http://dx.doi.org/10.1099/jmm.0.004358-0.

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Nowadays, influenza antigen detection test kits are used most frequently to detect influenza A or B virus to establish the diagnosis of influenza rapidly and initiate appropriate therapy. This study was conducted to evaluate the performance of the actim Influenza A&B test (Medix Biochemica). Overall, 473 respiratory specimens were analysed in the actim Influenza A&B test and the results were compared with those from an RT-PCR assay; 461 of these samples originated from paediatric patients aged 7 weeks to 6.5 years either with influenza-related symptoms or from the intensive care unit, and 12 samples originated from adults with underlying lung or haematological diseases. Diagnosis of influenza A or B virus could be established using the actim Influenza A&B test (9/473 samples for influenza A virus and 6/473 for influenza B virus). RT-PCR revealed 23 patients with influenza virus (13/473 for influenza A virus and 10/473 for influenza B virus). The sensitivity and specificity of the actim Influenza A&B test were 65 and 100 % compared with the RT-PCR assay. However, 32 external quality assessment samples containing seven different strains of influenza A subtypes H1N1 and H3N2 and the avian H5N1 were detected correctly by the actim Influenza A&B test. No cross-reactivity to a range of bacterial, fungal and other viral pathogens was observed. In conclusion, the actim Influenza A&B test is reliable for positive results due to its high specificity. Nevertheless, negative results from this test need to be confirmed by a more sensitive assay because of the low sensitivity observed with diagnostic samples.

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Kim, Yun Hee, Hyun Soo Kim, Sung Hwan Cho, and Sang Heui Seo. "Influenza B Virus Causes Milder Pathogenesis and Weaker Inflammatory Responses in Ferrets Than Influenza A Virus." Viral Immunology 22, no. 6 (December 2009): 423–30. http://dx.doi.org/10.1089/vim.2009.0045.

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Tung, Chang-Shung, Joshua L. Goodman, Henry Lu, and Catherine A. Macken. "Homology model of the structure of influenza B virus HA1." Journal of General Virology 85, no. 11 (November 1, 2004): 3249–59. http://dx.doi.org/10.1099/vir.0.80021-0.

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Influenza B virus is one of two types of influenza virus that cause substantial morbidity and mortality in humans, the other being influenza A virus. The inability to provide lasting protection to humans against influenza B virus infection is due, in part, to antigenic drift of the viral surface glycoprotein, haemagglutinin (HA). Studies of the antigenicity of the HA of influenza B virus have been hampered by lack of knowledge of its structure. To address this gap, two possible models have been inferred for this structure, based on two known structures of the homologous HA of the influenza A virus (subtypes H3 and H9). Statistical, structural and functional analyses of these models suggested that they matched important details of experimental observations and did not differ from each other in any substantive way. These models were used to investigate two HA sites at which viral variants appeared to carry a selective advantage. It was found that each of these sites coevolved with nearby sites to compensate for either size or charge changes.

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Wu, Yuet, Wenwei Tu, Kwok-Tai Lam, Kin-Hung Chow, Pak-Leung Ho, Yi Guan, Joseph S. Malik Peiris, and Yu-Lung Lau. "Lethal Coinfection of Influenza Virus and Streptococcus pneumoniae Lowers Antibody Response to Influenza Virus in Lung and Reduces Numbers of Germinal Center B Cells, T Follicular Helper Cells, and Plasma Cells in Mediastinal Lymph Node." Journal of Virology 89, no. 4 (November 26, 2014): 2013–23. http://dx.doi.org/10.1128/jvi.02455-14.

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ABSTRACTSecondaryStreptococcus pneumoniaeinfection after influenza is a significant clinical complication resulting in morbidity and sometimes mortality. Prior influenza virus infection has been demonstrated to impair the macrophage and neutrophil response to the subsequent pneumococcal infection. In contrast, how a secondary pneumococcal infection after influenza can affect the adaptive immune response to the initial influenza virus infection is less well understood. Therefore, this study focuses on how secondary pneumococcal infection after influenza may impact the humoral immune response to the initial influenza virus infection in a lethal coinfection mouse model. Compared to mice infected with influenza virus alone, mice coinfected with influenza virus followed by pneumococcus had significant body weight loss and 100% mortality. In the lung, lethal coinfection significantly increased virus titers and bacterial cell counts and decreased the level of virus-specific IgG, IgM, and IgA, as well as the number of B cells, CD4 T cells, and plasma cells. Lethal coinfection significantly reduced the size and weight of spleen, as well as the number of B cells along the follicular developmental lineage. In mediastinal lymph nodes, lethal coinfection significantly decreased germinal center B cells, T follicular helper cells, and plasma cells. Adoptive transfer of influenza virus-specific immune serum to coinfected mice improved survival, suggesting the protective functions of anti-influenza virus antibodies. In conclusion, coinfection reduced the B cell response to influenza virus. This study helps us to understand the modulation of the B cell response to influenza virus during a lethal coinfection.IMPORTANCESecondary pneumococcal infection after influenza virus infection is an important clinical issue that often results in excess mortality. Since antibodies are key mediators of protection, this study aims to examine the antibody response to influenza virus and demonstrates that lethal coinfection reduced the B cell response to influenza virus. This study helps to highlight the complexity of the modulation of the B cell response in the context of coinfection.

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Scott, Paul D., Bo Meng, Anthony C. Marriott, Andrew J. Easton, and Nigel J. Dimmock. "Defective interfering influenza A virus protects in vivo against disease caused by a heterologous influenza B virus." Journal of General Virology 92, no. 9 (September 1, 2011): 2122–32. http://dx.doi.org/10.1099/vir.0.034132-0.

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Influenza A and B viruses are major human respiratory pathogens that contribute to the burden of seasonal influenza. They are both members of the family Orthomyxoviridae but do not interact genetically and are classified in different genera. Defective interfering (DI) influenza viruses have a major deletion of one or more of their eight genome segments, which renders them both non-infectious and able to interfere in cell culture with the production of infectious progeny by a genetically compatible, homologous virus. It has been shown previously that intranasal administration of a cloned DI influenza A virus, 244/PR8, protects mice from various homologous influenza A virus subtypes and that it also protects mice from respiratory disease caused by a heterologous virus belonging to the family Paramyxoviridae. The mechanisms of action in vivo differ, with homologous and heterologous protection being mediated by probable genome competition and type I interferon (IFN), respectively. In the current study, it was shown that 244/PR8 also protects against disease caused by a heterologous influenza B virus (B/Lee/40). Protection from B/Lee/40 challenge was partially eliminated in mice that did not express a functional type I IFN receptor, suggesting that innate immunity, and type I IFN in particular, are important in mediating protection against this virus. It was concluded that 244/PR8 has the ability to protect in vivo against heterologous IFN-sensitive respiratory viruses, in addition to homologous influenza A viruses, and that it acts by fundamentally different mechanisms.

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Daley, Aj, R. Nallusamy, and D. Isaacs. "Comparison of influenza A and influenza B virus infection in hospitalized children." Journal of Paediatrics and Child Health 36, no. 4 (August 2000): 332–35. http://dx.doi.org/10.1046/j.1440-1754.2000.00533.x.

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Shcherbinin, D. N., S. V. Alekseeva, M. M. Shmarov, Yu A. Smirnov, B. S. Naroditskiy, and A. L. Gintsburg. "The Analysis of B-Cell Epitopes of Influenza Virus Hemagglutinin." Acta Naturae 8, no. 1 (March 15, 2016): 13–20. http://dx.doi.org/10.32607/20758251-2016-8-1-13-20.

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Vaccination has been successfully used to prevent influenza for a long time. Influenza virus hemagglutinin (HA), which induces a humoral immune response in humans and protection against the flu, is the main antigenic component of modern influenza vaccines. However, new seasonal and pandemic influenza virus variants with altered structures of HA occasionally occur. This allows the pathogen to avoid neutralization with antibodies produced in response to previous vaccination. Development of a vaccine with the new variants of HA acting as antigens takes a long time. Therefore, during an epidemic, it is important to have passive immunization agents to prevent and treat influenza, which can be monoclonal or single-domain antibodies with universal specificity (broad-spectrum agents). We considered antibodies to conserved epitopes of influenza virus antigens as universal ones. In this paper, we tried to characterize the main B-cell epitopes of hemagglutinin and analyze our own and literature data on broadly neutralizing antibodies. We conducted a computer analysis of the best known conformational epitopes of influenza virus HAs using materials of different databases. The analysis showed that the core of the HA molecule, whose antibodies demonstrate pronounced heterosubtypic activity, can be used as a target for the search for and development of broad-spectrum antibodies to the influenza virus.

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Jiang, Jingwen, Jing Li, Wenhui Fan, Weinan Zheng, Meng Yu, Can Chen, Lei Sun, et al. "Robust Lys63-Linked Ubiquitination of RIG-I Promotes Cytokine Eruption in Early Influenza B Virus Infection." Journal of Virology 90, no. 14 (April 27, 2016): 6263–75. http://dx.doi.org/10.1128/jvi.00549-16.

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ABSTRACTInfluenza A and B virus infections both cause a host innate immunity response. Here, we report that the robust production of type I and III interferons (IFNs), IFN-stimulated genes, and proinflammatory factors can be induced by influenza B virus rather than influenza A virus infection in alveolar epithelial (A549) cells during early infection. This response is mainly dependent on the retinoic acid-inducible gene I (RIG-I)-mediated signaling pathway. Infection by influenza B virus promotes intense Lys63-linked ubiquitination of RIG-I, resulting in cytokine eruption. It is known that the influenza A virus NS1 protein (NS1-A) interacts with RIG-I and TRIM25 to suppress the activation of RIG-I-mediated signaling. However, the present results indicate that the influenza B virus NS1 protein (NS1-B) is unable to interact with RIG-I but engages in the formation of a RIG-I/TRIM25/NS1-B ternary complex. Furthermore, we demonstrate that the N-terminal RNA-binding domain (RBD) of NS1-B is responsible for interaction with TRIM25 and that this interaction blocks the inhibitory effect of the NS1-B C-terminal effector domain (TED) on RIG-I ubiquitination. Our findings reveal a novel mechanism for the host cytokine response to influenza B virus infection through regulatory interplay between host and viral proteins.IMPORTANCEInfluenza B virus generally causes local mild epidemics but is occasionally lethal to individuals. Existing studies describe the broad characteristics of influenza B virus epidemiology and pathology. However, to develop better prevention and treatments for the disease, determining the concrete molecular mechanisms of pathogenesis becomes pivotal to understand how the host reacts to the challenge of influenza B virus. Thus, we aimed to characterize the host innate immune response to influenza B virus infection. Here, we show that vigorous Lys63-linked ubiquitination of RIG-I and cytokine eruption dependent on RIG-I-mediated signal transduction are induced by virus infection. Additionally, TRIM25 positively regulates RIG-I-mediated signaling by ablating the inhibitory function of NS1-B on RIG-I ubiquitination.

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Peretz, A., M. Azrad, and A. Blum. "Influenza virus and atherosclerosis." QJM: An International Journal of Medicine 112, no. 10 (January 3, 2019): 749–55. http://dx.doi.org/10.1093/qjmed/hcy305.

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AbstractInfluenza viruses infect the upper respiratory system, causing usually a self-limited disease with mild respiratory symptoms. Acute lung injury, pulmonary microvascular leakage and cardiovascular collapse may occur in severe cases, usually in the elderly or in immunocompromised patients. Acute lung injury is a syndrome associated with pulmonary oedema, hypoxaemia and respiratory failure. Influenza virus primarily binds to the epithelium, interfering with the epithelial sodium channel function. However, the main clinical devastating effects are caused by endothelial dysfunction, thought to be the main mechanism leading to pulmonary oedema, respiratory failure and cardiovascular collapse. A significant association was found between influenza infection and acute myocardial infarction (AMI). The incidence of admission due to AMI during an acute viral infection was six times as high during the 7 days after laboratory confirmation of influenza infection as during the control interval (10-fold in influenza B, 5-fold in influenza A, 3.5-fold in respiratory syncytial virus and 2.7-fold for all other viruses). Our review will focus on the mechanisms responsible for endothelial dysfunction during influenza infection leading to cardiovascular collapse and death.

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