The Val430Ile neuraminidase (NA) substitution, identified in influenza B virus isolates, impacts the catalytic 116Arg residue causing reduced susceptibility to NA inhibitors

2019 ◽  
Vol 170 ◽  
pp. 104561 ◽  
Author(s):  
Yacine Abed ◽  
Clément Fage ◽  
Liva Checkmahomed ◽  
Gabriel Begin ◽  
Julie Carbonneau ◽  
...  
Keyword(s):  
Influenza B Virus ◽  
Influenza B ◽  
B Virus ◽  
Na Substitution ◽  
Virus Isolates

Effect of a single mutation in neuraminidase on the properties of Influenza B virus isolates

2003 ◽  
Vol 149 (1) ◽  
pp. 173-181 ◽  
Author(s):  
D. Katinger ◽  
J. Romanova ◽  
B. Ferko ◽  
H. Fekete ◽  
A. Egorov
Keyword(s):  
Influenza B Virus ◽  
Influenza B ◽  
Single Mutation ◽  
B Virus ◽  
Virus Isolates

scholarly journals Sequential mutations in hemagglutinins of influenza B virus isolates: definition of antigenic domains.

1983 ◽  
Vol 80 (14) ◽  
pp. 4527-4531 ◽  
Author(s):  
M. Krystal ◽  
J. F. Young ◽  
P. Palese ◽  
I. A. Wilson ◽  
J. J. Skehel ◽  
...  
Keyword(s):  
Influenza B Virus ◽  
Influenza B ◽  
B Virus ◽  
Antigenic Domains ◽  
Definition Of ◽  
Virus Isolates

scholarly journals Characterization of Influenza B Virus Variants with Reduced Neuraminidase Inhibitor Susceptibility

2018 ◽  
Vol 62 (11) ◽  
Author(s):  
R. Farrukee ◽  
A. E. Zarebski ◽  
J. M. McCaw ◽  
J. D. Bloom ◽  
P. C. Reading ◽  
...  
Keyword(s):  
Treatment Options ◽  
Transmission Efficiency ◽  
Enzyme Function ◽  
Influenza B Virus ◽  
Influenza B ◽  
Virus Infections ◽  
Wild Type ◽  
B Virus ◽  
Na Substitution

ABSTRACT Treatment options for influenza B virus infections are limited to neuraminidase inhibitors (NAIs), which block the neuraminidase (NA) glycoprotein on the virion surface. The development of NAI resistance would therefore result in a loss of antiviral treatment options for influenza B virus infections. This study characterized two contemporary influenza B viruses with known resistance-conferring NA amino acid substitutions, D197N and H273Y, detected during routine surveillance. The D197N and H273Y variants were characterized in vitro by assessing NA enzyme activity and affinity, as well as replication in cell culture compared to those of NAI-sensitive wild-type viruses. In vivo studies were also performed in ferrets to assess the replication and transmissibility of each variant. Mathematical models were used to analyze within-host and between-host fitness of variants relative to wild-type viruses. The data revealed that the H273Y variant had NA enzyme function similar to that of its wild type but had slightly reduced replication and transmission efficiency in vivo. The D197N variant had impaired NA enzyme function, but there was no evidence of reduction in replication or transmission efficiency in ferrets. Our data suggest that the influenza B virus variant with the H273Y NA substitution had a more notable reduction in fitness compared to wild-type viruses than the influenza B variant with the D197N NA substitution. Although a D197N variant is yet to become widespread, it is the most commonly detected NAI-resistant influenza B virus in surveillance studies. Our results highlight the need to carefully monitor circulating viruses for the spread of influenza B viruses with the D197N NA substitution.

scholarly journals Characterization of influenza B virus variants with reduced neuraminidase inhibitor susceptibility

2018 ◽  
Author(s):  
R Farrukee ◽  
AE Zarebski ◽  
JM McCaw ◽  
JD Bloom ◽  
PC Reading ◽  
...  
Keyword(s):  
Antiviral Treatment ◽  
Treatment Options ◽  
Transmission Efficiency ◽  
Enzyme Function ◽  
Influenza B Virus ◽  
Influenza B ◽  
Wild Type ◽  
B Virus ◽  
Na Substitution

AbstractTreatment options for influenza B virus infections are limited to neuraminidase inhibitors (NAIs) which block the neuraminidase (NA) glycoprotein on the virion surface. The development of NAI resistance would therefore result in a loss of antiviral treatment options for influenza B infections. This study characterized two contemporary influenza B viruses with known resistance-conferring NA amino acid substitutions, D197N and H273Y, detected during routine surveillance. The D197N and H273Y variants were characterized in vitro by assessing NA enzyme activity and affinity, as well as replication in cell culture compared to NAI-sensitive wild-type viruses. In vivo studies were also performed in ferrets to assess the replication and transmissibility of each variant. Mathematical models were used to analyse within-host and between-host fitness of variants relative to wild-type viruses. The data revealed that the H273Y variant had similar NA enzyme function relative to its wild-type but had slightly reduced replication and transmission efficiency in vivo. The D197N variant had impaired NA enzyme function but there was no evidence of reduction in replication or transmission efficiency in ferrets. Our data suggest that the influenza B variant with H273Y NA substitution had a more notable reduction in fitness compared to wild-type viruses than the influenza B variant with the D197N NA substitution. Although a D197N variant is yet to become widespread, it is the most commonly detected NAI-resistant influenza B virus in surveillance studies. Our results highlight the need to carefully monitor circulating viruses for the spread of influenza B viruses with the D197N NA substitution.

scholarly journals Identification of New Influenza B Virus Variants by Multiplex Reverse Transcription-PCR and the Heteroduplex Mobility Assay

1998 ◽  
Vol 36 (6) ◽  
pp. 1544-1548 ◽  
Author(s):  
Shimian Zou ◽  
Carol Stansfield ◽  
Jodi Bridge
Keyword(s):  
Influenza Virus ◽  
Reverse Transcription ◽  
Amino Acid Level ◽  
Critical Evaluation ◽  
Influenza Viruses ◽  
Influenza B Virus ◽  
Influenza B ◽  
Close Monitoring ◽  
B Virus ◽  
Virus Isolates

A quick genetic approach for the screening of influenza virus variants was developed in this laboratory (S. Zou, J. Clin. Microbiol. 35:2623–2627, 1997). It uses multiplex reverse transcription and multiplex PCR to amplify and differentiate the variable region of the hemagglutinin genes of different types and subtypes of influenza viruses. Variants within the same type or subtype are then identified by the heteroduplex mobility shift assay of the amplicons. The method was used to screen influenza virus isolates received from provincial laboratories during the 1996–1997 season and was able to identify new influenza B virus variants. Sequencing of the amplicons derived from the hemagglutinin gene of the identified variants and comparison with the vaccine strain B/Harbin/7/94 showed substitution rates of 2.26 to 2.55% at the nucleotide level and 4.26 to 4.68% at the amino acid level. The result further demonstrated that the approach provides a quick, sensitive, and reliable screening for influenza virus variants. It also suggested the necessity of close monitoring of influenza B virus isolates in the 1997–1998 season and critical evaluation of the reference strain for the type B influenza virus.

scholarly journals Recurring Influenza B Virus Infections in Seals

2013 ◽  
Vol 19 (3) ◽  
pp. 511-512 ◽  
Author(s):  
Rogier Bodewes ◽  
Danny Morick ◽  
Gerrie de Mutsert ◽  
Nynke Osinga ◽  
Theo Bestebroer ◽  
...  
Keyword(s):  
Influenza B Virus ◽  
Influenza B ◽  
Virus Infections ◽  
B Virus

scholarly journals Molecular Epidemiology and Phylogenetic Analyses of Influenza B Virus in Thailand during 2010 to 2014

PLoS ONE ◽  
2015 ◽  
Vol 10 (1) ◽  
pp. e0116302 ◽  
Author(s):  
Nipaporn Tewawong ◽  
Kamol Suwannakarn ◽  
Slinporn Prachayangprecha ◽  
Sumeth Korkong ◽  
Preeyaporn Vichiwattana ◽  
...  
Keyword(s):  
Molecular Epidemiology ◽  
Phylogenetic Analyses ◽  
Influenza B Virus ◽  
Influenza B ◽  
B Virus

scholarly journals Mutation E48K in PB1 Polymerase Subunit Improves Stability of a Candidate Live Attenuated Influenza B Virus Vaccine

Vaccines ◽  
2021 ◽  
Vol 9 (7) ◽  
pp. 800
Author(s):  
Jongsuk Mo ◽  
Stivalis Cardenas-Garcia ◽  
Jefferson J. S. Santos ◽  
Lucas M. Ferreri ◽  
C. Joaquín Cáceres ◽  
...  
Keyword(s):  
Vaccine Candidate ◽  
The Elderly ◽  
Potential Interaction ◽  
Respiratory Pathogen ◽  
Influenza B Virus ◽  
Influenza B ◽  
Epitope Tag ◽  
Live Attenuated Vaccine ◽  
B Virus ◽  
Homologous Challenge

Influenza B virus (IBV) is a major respiratory pathogen of humans, particularly in the elderly and children, and vaccines are the most effective way to control it. In previous work, incorporation of two mutations (E580G, S660A) along with the addition of an HA epitope tag in the PB1 segment of B/Brisbane/60/2008 (B/Bris) resulted in an attenuated strain that was safe and effective as a live attenuated vaccine. A third attempted mutation (K391E) in PB1 was not always stable. Interestingly, viruses that maintained the K391E mutation were associated with the mutation E48K. To explore the contribution of the E48K mutation to stability of the K391E mutation, a vaccine candidate was generated by inserting both mutations, along with attenuating mutations E580G and S660A, in PB1 of B/Bris (B/Bris PB1att 4M). Serial passages of the B/Bris PB1att 4M vaccine candidate in eggs and MDCK indicated high stability. In silico structural analysis revealed a potential interaction between amino acids at positions 48 and 391. In mice, B/Bris PB1att 4M was safe and provided complete protection against homologous challenge. These results confirm the compensatory effect of mutation E48K to stabilize the K391E mutation, resulting in a safer, yet still protective, IBV LAIV vaccine.

Sign in / Sign up

Export Citation Format

Share Document