Optimized clade 2.3.2.1c H5N1 recombinant-vaccine strains against highly pathogenic avian influenza

Jang, Jin-Wook; Lee, Chung-Young; Kim, Il-Hwan; Choi, Jun‐Gu; Lee, Youn‐Jeong; Yuk, Seong‐Su; Lee, Ji-Ho; Song, Chang‐Seon; Kim, Jae Hong; Kwon, Hyuk‐Joon

doi:10.4142/jvs.2017.18.s1.299

Cited by 9 publications

(14 citation statements)

References 40 publications

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“…The attenuated HA (mutation from multi-basic RERRRKR to mono-basic ASGR) and NA genome segments of a clade 2.3.2.1c HP A(H5N1) virus, A/mandarin duck/Korea/K10-483/2010 (K10-483), were previously cloned into a bidirectional reverse genetics vector, pHW2000, and six other internal genomes of A/Puerto Rico/8/34 (H1N1) (PR8) cloned into pHW2000 were used [29,31,32]. The amino acid sequences of HA and NA of K10-483 did not have known mutations affecting the biological traits tested in this study.…”

Section: Methodsmentioning

confidence: 99%

“…Most clade 2.3.2.1a and c viruses acquired both mutations. Previously, the PR8-based recombinant virus with HA and Neuraminidase (NA) of a clade 2.3.2.1c HP A(H5N1) virus isolated in Korea, A/mandarin duck/Korea/K10-483/2010 (K10-483), did not replicate well in embryonated chicken eggs (ECEs) and had low pathogenicity in mice [29,30]. To understand the effects of the mutations on replication efficiency in ECEs and mammalian cells and on the pathogenicity in mice, we generated PR8-derived mutant viruses and compared their biological characteristics.…”

Section: Introductionmentioning

confidence: 99%

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Novel Mutations Evading Avian Immunity around the Receptor Binding Site of the Clade 2.3.2.1c Hemagglutinin Gene Reduce Viral Thermostability and Mammalian Pathogenicity

An¹,

Lee

Hong

et al. 2019

Viruses

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Since 2007, highly pathogenic clade 2.3.2 H5N1 avian influenza A (A(H5N1)) viruses have evolved to clade 2.3.2.1a, b, and c; currently only 2.3.2.1c A(H5N1) viruses circulate in wild birds and poultry. During antigenic evolution, clade 2.3.2.1a and c A(H5N1) viruses acquired both S144N and V223I mutations around the receptor binding site of hemagglutinin (HA), with S144N generating an N-glycosylation sequon. We introduced single or combined reverse mutations, N144S and/or I223V, into the HA gene of the clade 2.3.2.1c A(H5N1) virus and generated PR8-derived, 2 + 6 recombinant A(H5N1) viruses. When we compared replication efficiency in embryonated chicken eggs, mammalian cells, and mice, the recombinant virus containing both N144S and I223V mutations showed increased replication efficiency in avian and mammalian hosts and pathogenicity in mice. The N144S mutation significantly decreased avian receptor affinity and egg white inhibition, but not all mutations increased mammalian receptor affinity. Interestingly, the combined reverse mutations dramatically increased the thermostability of HA. Therefore, the adaptive mutations possibly acquired to evade avian immunity may decrease viral thermostability as well as mammalian pathogenicity.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Novel Mutations Evading Avian Immunity around the Receptor Binding Site of the Clade 2.3.2.1c Hemagglutinin Gene Reduce Viral Thermostability and Mammalian Pathogenicity

An¹,

Lee

Hong

et al. 2019

Viruses

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“…The mammalian pathogenicity of HP A(H5N1) viruses is a multigenic trait, and the human pathogenicity of clade 2.3.2.1 viruses has been regarded as lower than that of other clades [53]. In our previous studies, a PR8-derived clade 2.3.2.1c recombinant vaccine strain showed less pathogenicity in mice than another PR8-derived recombinant virus containing HA and NA genes from low pathogenic (LP) A(H5N1) virus [29,54]. Although the amino acid sequences of the two HA proteins are only 89%…”

Section: Preprintsmentioning

confidence: 99%

“…The attenuated HA (mutation from multi-basic RERRRKR to mono-basic ASGR) and NA genome segments of a clade 2.3.2.1c HP A(H5N1) virus, A/mandarin duck/Korea/K10-483/2010 (K10-483), were previously cloned into a bidirectional reverse genetics vector, pHW2000, and 6 other internal genomes of A/Puerto Rico/8/34 (H1N1) (PR8) cloned into pHW2000 were used [29][30][31]. 293T, MDCK and A549 of 16 cells were purchased from Korean Collection for Type Cultures (KCTC, Daejeon, Korea).…”

Section: Viruses Plasmids Cells and Eggsmentioning

confidence: 99%

“…Previously, the PR8-based recombinant virus with HA and NA of a clade 2.3.2.1c HP A(H5N1) virus isolated in Korea, A/mandarin duck/Korea/K10-483/2010 (K10-483), did not replicate well in embryonated chicken eggs (ECEs) and had low pathogenicity in mice [29]. Therefore, in this study, we compared the HA amino acid sequences of clade 2.3.2 and clade 2.3.2.1a, b and c viruses and found two cumulative mutations (S144N and V223I) around the RBS.…”

Section: Introductionmentioning

confidence: 99%

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Novel Mutations Evading Avian Immunity around the Receptor Binding Site of the Clade 2.3.2.1c Hemagglutinin Gene Reduce Viral Thermostability and Mammalian Pathogenicity

An¹,

Lee²,

Hong³

et al. 2019

Preprint

Self Cite

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Since 2007, highly pathogenic clade 2.3.2 H5N1 avian influenza A [A(H5N1)] viruses have evolved to clade 2.3.2.1a, b and c, and currently only 2.3.2.1c A(H5N1) viruses circulate in wild birds and poultry. During antigenic evolution, clade 2.3.2.1a and c A(H5N1) viruses acquired both S144N and V223I mutations around the receptor binding site of hemagglutinin (HA), with S144N generating an N-glycosylation sequon. We introduced single or combined reverse mutations, N144S and/or I223V, into the HA gene of clade 2.3.2.1c A(H5N1) virus and generated PR8-derived, 2 + 6 recombinant A(H5N1) viruses. When we compared replication efficiency in embryonated chicken eggs, mammalian cells and mice, the recombinant virus containing both N144S and I223V mutations showed increased replication efficiency in avian and mammalian hosts and pathogenicity in mice. The N144S mutation significantly decreased avian receptor affinity and egg white inhibition, but not all mutations increased mammalian receptor affinity. Interestingly, the combined reverse mutations dramatically increased the thermostability of HA. Therefore, the adaptive mutations possibly acquired to evade avian immunity may decrease viral thermostability as well as mammalian pathogenicity.

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Gingiva-derived Stromal Cells Isolated from Cats Affected with Tooth Resorption Exhibit Increased Apoptosis, Inflammation, and Oxidative Stress while Experiencing Deteriorated Expansion and Anti-Oxidative Defense

Soltero-Rivera

Groborz²,

Janeczek

et al. 2023

Stem Cell Rev and Rep

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show abstract

Optimized clade 2.3.2.1c H5N1 recombinant-vaccine strains against highly pathogenic avian influenza

Cited by 9 publications

References 40 publications

Novel Mutations Evading Avian Immunity around the Receptor Binding Site of the Clade 2.3.2.1c Hemagglutinin Gene Reduce Viral Thermostability and Mammalian Pathogenicity

Novel Mutations Evading Avian Immunity around the Receptor Binding Site of the Clade 2.3.2.1c Hemagglutinin Gene Reduce Viral Thermostability and Mammalian Pathogenicity

Novel Mutations Evading Avian Immunity around the Receptor Binding Site of the Clade 2.3.2.1c Hemagglutinin Gene Reduce Viral Thermostability and Mammalian Pathogenicity

Gingiva-derived Stromal Cells Isolated from Cats Affected with Tooth Resorption Exhibit Increased Apoptosis, Inflammation, and Oxidative Stress while Experiencing Deteriorated Expansion and Anti-Oxidative Defense

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