Literature detail

Host-specific functional evolution of seal influenza A virus NS1 protein following avian-to-seal transmission.

Maryna Kuryshko1 Christine Luttermann2 Mahmoud Bayoumi3,4 Ahmed Mostafa3,5 Jula Weißmann2 Alexander Schäfer6 Lisa Wendt1 Thomas Hoenen1 Jendrik Müller1 Luis Martinez-Sobrido3 Thomas C Mettenleiter7 Elsayed M Abdelwhab1
Affiliations 7 institutions
  1. Institute of Molecular Virology and Cell Biology, Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Greifswald-Insel Riems, Germany.
  2. Institute of Immunology, Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Greifswald-Insel Riems, Germany.
  3. Disease Intervention and Prevention, Texas Biomedical Research Institute, San Antonio, Texas, USA.
  4. Virology Department, Faculty of Veterinary Medicine, Cairo University, Giza, Egypt.
  5. Center of Scientific Excellence for Influenza Viruses, National Research Centre, Giza, Egypt.
  6. Institute of Diagnostic Virology, Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Greifswald-Insel Riems, Germany.
  7. Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health, Greifswald-Insel Riems, Germany.
PMID 41874045 2026 J Virol eng ppublish
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Article

Publication summary

Marine mammals, particularly seals, are susceptible to both avian and human influenza A viruses (IAVs), making them potential intermediates for zoonotic virus emergence. In recent decades, repeated transmissions of avian influenza viruses (AIVs) from wild aquatic birds, their natural reservoir, have caused significant mortality in seals. Defining the molecular determinants of viral adaptation in marine mammals, and their implications for replication in human cells, is therefore essential. The non-structural protein 1 (NS1) of AIV, a key antagonist of the interferon (IFN) response, plays a central role in host adaptation. Here, we analyzed NS1 proteins from seal influenza viruses (H3, H4, H5, H7, and H10 subtypes) and their closest avian relatives isolated between 1980 and 2023, and evaluated their function in seal, avian, and human cells. Phylogenetic analysis confirmed multiple bird-to-seal transmission events. Seal-derived NS1 proteins generally contained few strain-specific amino acid substitutions and showed comparable expression and IFN antagonism to their avian precursors. A notable exception was the seal H10N7 virus isolated in 2014 in Northeastern Europe, which harbored three previously uncharacterized substitutions at NS1 amino acid residues 94, 104, and 171. These amino acid substitutions markedly altered NS1 properties to enhance protein stability, suppress IFN induction, mediate host transcription shut-off, and increase polymerase activity in human cells, without affecting NS1 expression or reducing virus replication in avian cells. Overall, these results reveal how NS1 undergoes host-specific functional evolution following avian-to-seal transmission and provide mechanistic insight into the adaptation of influenza A viruses to mammalian hosts.IMPORTANCEAvian influenza viruses (AIVs) circulate naturally in wild aquatic birds but occasionally infect mammals, including seals, where they can cause severe outbreaks. Seals are of particular concern because they can harbor both avian and human influenza viruses, creating opportunities for reassortment and the emergence of novel zoonotic strains. Understanding how AIVs adapt to mammalian hosts is therefore critical for anticipating and mitigating future influenza threats. Here, we investigated the role of the NS1 protein, a key viral factor that suppresses host immune responses, in seal-derived AIVs. Overall, NS1 expression and function were conserved across different subtypes and host cells. However, we identified unique amino acid substitutions in the NS1 of a seal H10N7 virus that enhanced protein stability, interferon antagonism, and viral adaptation in human cells. These findings illustrate how minor changes in NS1 protein can drive host adaptation and underscore the need for continued surveillance of AIVs in seals.

avian influenza virus (AIV) cross-species transmission interferon antagonism NS1 protein seals viral adaptation zoonotic potential Influenza A virus Influenza in Birds Orthomyxoviridae Infections Viral Nonstructural Proteins Amino Acid Substitution Animals Birds Evolution, Molecular Host Specificity Humans Influenza, Human

Structured evidence records

Evidence records

4 total
1 records
Extraction confidence 0.95
Key finding

Influenza A viruses were transmitted from wild aquatic birds to seals multiple times as confirmed by phylogenetic analysis.

Virus
Host
Location
Supporting text

Phylogenetic analysis confirmed multiple bird-to-seal transmission events.

Method
phylogenetic analysis
Study design
phylogenetic analysis
Transmission direction
animal-to-animal
Geographic raw
Northeastern Europe
1 records
Extraction confidence 0.90
Key finding

Phylogenetic and sequence analyses revealed host-specific evolution of the NS1 gene in seal influenza A viruses, with unique amino acid substitutions in the seal H10N7 virus following avian-to-seal transmission.

Virus
Host
Location
Not specified
Supporting text

Phylogenetic analysis confirmed multiple bird-to-seal transmission events. Seal-derived NS1 proteins generally contained few strain-specific amino acid substitutions... A notable exception was the seal H10N7 virus isolated in 2014 in Northeastern Europe, which harbored three previously uncharacterized substitutions at NS1 amino acid residues 94, 104, and 171.

Genes or proteins
NS1
Analysis methods
phylogenetic analysis; sequence analysis
1 records
Extraction confidence 0.98
Key finding

The seal H10N7 influenza A virus acquired three NS1 amino acid substitutions (94, 104, 171) that increased protein stability, interferon antagonism, and polymerase activity in human cells, reflecting host-specific molecular adaptation following avian-to-seal transmission.

Virus
Host
Not specified
Location
Not specified
Supporting text

A notable exception was the seal H10N7 virus isolated in 2014 in Northeastern Europe, which harbored three previously uncharacterized substitutions at NS1 amino acid residues 94, 104, and 171. These amino acid substitutions markedly altered NS1 properties to enhance protein stability, suppress IFN induction, mediate host transcription shut-off, and increase polymerase activity in human cells.

Genes or proteins
NS1
Host factors
interferon response
Mutations
NS1 residue 94 substitution; NS1 residue 104 substitution; NS1 residue 171 substitution
Mechanism types
immune_escape; polymerase_activity; host_factor_interaction
1 records
Extraction confidence 0.90
Key finding

Multiple avian influenza A viruses spilled over from wild birds to seals, including an H10N7 virus detected in 2014 in Northeastern Europe.

Virus
Host
Location
Supporting text

Phylogenetic analysis confirmed multiple bird-to-seal transmission events. A notable exception was the seal H10N7 virus isolated in 2014 in Northeastern Europe.

Method
phylogenetic analysis
Study design
phylogenetic analysis
Transmission direction
animal-to-human
Geographic raw
Northeastern Europe