Suomen asenne A H5N1-viruksen esiintymiseen epätavallisissa lajeissa kuten lämminveriset turkiseläimet.

 https://wahis.woah.org/#/in-review/5119

SOURCE OF EVENT OR ORIGIN OF INFECTION

• Unknown or inconclusive

EPIDEMIOLOGICAL COMMENTS

Note: previously published precise location data of the outbreaks was changed to approximate in follow-up report 3 to insure privacy of the farmers. Follow-up report on 24.8.2023: Several HPAI H5N1 outbreaks on fur farms raising arctic foxes, silver foxes, American minks and raccoon dogs have been detected. Wild birds are currently considered the most likely source of the infection, based on epidemiological investigations and sequencing of the viruses. The competent authority has imposed restrictive orders on infected fur animal farms. All minks from the infected farms are culled. Other fur animals from infected farms are culled based on the decisions that are made on a case-by-case basis and do not necessarily apply to all animals on the farm. In addition, samples are taken from infected farms to monitor the course of the epidemic. If the virus is detected, the culling will continue. Veterinary authorities are working in tight collaboration with the public health authority. Improved biosecurity measures and use of personal protection equipment on fur farms are encouraged. Follow-up report on 5.10.2023: Starting from 11 September 2023, a new culling policy has been adopted and all animals on HPAI virus-positive farms, including foxes and common raccoon dogs, are culled.

 Wahis raportoi 25.4.2024  Suomessa  kasseerattujen  turkisfarmieläinten määräksi 457 232.

A H5N1 viruses, clade 2.3.4.4b

 

Review

• 2025 Jun 17;99(6):e0042425.

doi: 10.1128/jvi.00424-25. Epub 2025 May 9.

Clade 2.3.4.4b highly pathogenic avian influenza H5N1 viruses: knowns, unknowns, and challenges

Zimin Xie ^{#  1   2} , Jiayun Yang ^{#  3} , Wanlin Jiao  ^{1   2} , Xueqing Li  ^{1   2} , Munir Iqbal  ³ , Ming Liao  ^{1   2} , Manman Dai  ^{1   2}

Affiliations

• PMID: 40340397
• PMCID: PMC12172449
• DOI: 10.1128/jvi.00424-25

Abstract

Since 2020, the clade 2.3.4.4b highly pathogenic avian influenza (HPAI) H5N1 viruses have caused unprecedented outbreaks in wild birds and domestic poultry globally, resulting in significant ecological damage and economic losses due to the disease and enforced stamp-out control. In addition to the avian hosts, the H5N1 viruses have expanded their host range to infect many mammalian species, potentially increasing the zoonotic risk. Here, we review the current knowns and unknowns of clade 2.3.4.4b HPAI H5N1 viruses, and we highlight common challenges in prevention. By integrating our knowledge of viral evolution and ecology, we aim to identify discrepancies and knowledge gaps for a more comprehensive understanding of the virus. Ultimately, this review will serve as a theoretical foundation for researchers involved in related avian influenza virus studies, aiding in improved control and prevention of H5N1 viruses.

Keywords: Clade 2.3.4.4b; H5N1; evolution; highly pathogenic avian influenza; pathogenicity.

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Conflict of interest statement

The authors declare no conflict of interest.

A H5N1 viruksen yksityiskohdista. vRNP-M1-NEP tumasta ulos kuljettava kompleksi

 

•  2014 Jul 18;289(29):20067-77.

doi: 10.1074/jbc.M114.569178. Epub 2014 Jun 2.The nuclear export protein of H5N1 influenza A viruses recruits Matrix 1 (M1) protein to the viral ribonucleoprotein to mediate nuclear export

Linda Brunotte  ¹ , Joe Flies  ¹ , Hardin Bolte  ¹ , Peter Reuther  ¹ , Frank Vreede  ² , Martin Schwemmle  ³

Affiliations

• PMID: 24891509
• PMCID: PMC4106323
• DOI: 10.1074/jbc.M114.569178

Abstract

In influenza A virus-infected cells, replication and transcription of the viral genome occurs in the nucleus. To be packaged into viral particles at the plasma membrane, encapsidated viral genomes must be exported from the nucleus. Intriguingly, the nuclear export protein (NEP) is involved in both processes. Although NEP stimulates viral RNA synthesis by binding to the viral polymerase, its function during nuclear export implicates interaction with viral ribonucleoprotein (vRNP)-associated M1. The observation that both interactions are mediated by the C-terminal moiety of NEP raised the question whether these two features of NEP are linked functionally. Here we provide evidence that the interaction between M1 and the vRNP depends on the NEP C terminus and its polymerase activity-enhancing property for the nuclear export of vRNPs. This suggests that these features of NEP are linked functionally. Furthermore, our data suggest that the N-terminal domain of NEP interferes with the stability of the vRNP-M1-NEP nuclear export complex, probably mediated by its highly flexible intramolecular interaction with the NEP C terminus. On the basis of our data, we propose a new model for the assembly of the nuclear export complex of Influenza A vRNPs.

Keywords: Influenza Virus; Protein Export; Ribonucleoprotein (RNP); Viral Polymerase; Viral Protein.

© 2014 by The American Society for Biochemistry and Molecular Biology, Inc. 

 

See this image and copyright information in PMC

FIGURE 1.

Schematic of the nuclear export complex. A, in the currently proposed daisy chain model of the nuclear export model, M1 interacts with the vRNP. NEP binds with its C-terminal (C) domain to vRNP-associated M1 and, with its NES-containing N terminus (N), establishes an interaction with the cellular export protein CRM1. B, refined model of the vRNP nuclear export complex. NEP interacts with the viral polymerase to provide additional binding site and support M1/vRNP association. The N-Terminus of NEP is flexible and interacts with CRM1.

Influenssatilanteesta 2025 PubMed uutinen

 Editorial: The 2025 World Health Assembly Pandemic Agreement and the 2024 Amendments to the International Health Regulations Combine for Pandemic Preparedness and Response.

Parums DV. Med Sci Monit. 2025 Jul 1;31:e950411. doi: 10.12659/MSM.950411. PMID: 40589223Abstract

The importance of pandemic preparedness is underscored by two recent and significant findings in the US, including outbreaks of measles in children and adults, as well as the demonstration of airborne transmission of the influenza A(H5N1) virus (bird flu). 

On June 1, 2024, the 77th World Health Assembly of the World Health Organization (WHO) reached a consensus on amendments to the 2005 International Health Regulations, representing a new universal legal framework for global health, pandemic preparedness, and response that will enter into force in September 2025. 

On May 20, 2025, the 78th World Health Assembly of the WHO adopted the Pandemic Agreement, following three years of negotiations that identified gaps and inequities in the global response to the COVID-19 pandemic.

 The WHO Pandemic Agreement document outlines the principles, approaches, and tools to enhance international coordination for pandemic prevention, preparedness, and response, including equitable access to vaccines, diagnostics, and therapeutics. This editorial aims to highlight the timeliness of the 2025 WHO Pandemic Agreement and the 2024 amendments to the International Health Regulations, as well as the need for improved pandemic preparedness and response at this time.

Influenssaviruksen RNP ja riippuvaisuus sinkistä hakusanana. 2 vastausta vuosilta 2004 ja 2002.

 

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Introduction of a temperature-sensitive phenotype into influenza A/WSN/33 virus by altering the basic amino acid domain of influenza virus matrix protein.

Liu T, Ye Z. J Virol. 2004 Sep;78(18):9585-91. doi: 10.1128/JVI.78.18.9585-9591.2004. PMID: 15331690 Free PMC article.

Abstract

Our previous studies with influenza A viruses indicated that the association of M1 with viral RNA and nucleoprotein (NP) is required for the efficient formation of helical ribonucleoprotein (RNP) and for the nuclear export of RNPs. RNA-binding domains of M1 map to the following two independent regions: a zinc finger motif at amino acid positions 148 to 162 and a series of basic amino acids (RKLKR) at amino acid positions 101 to 105. Altering the zinc finger motif of M1 reduces viral growth slightly. A substitution of Ser for Arg at either position 101 or position 105 of the RKLKR domain partially reduces the nuclear export of RNP and viral replication. To further understand the role of the zinc finger motif and the RKLKR domain in viral assembly and replication, we introduced multiple mutations by using reverse genetics to modify these regions of the M gene of influenza virus A/WSN/33. Of multiple mutants analyzed, a double mutant, R101S-R105S, of RKLKR resulted in a temperature-sensitive phenotype. The R101S-R105S double mutant had a greatly reduced ratio of M1 to NP in viral particles and a weaker binding of M1 to RNPs. These results suggest that mutations can be introduced into the RKLKR domain to control viral replication.

2

Restriction of viral replication by mutation of the influenza virus matrix protein.

Liu T, Ye Z. J Virol. 2002 Dec;76(24):13055-61. doi: 10.1128/jvi.76.24.13055-13061.2002. PMID: 12438632 Free PMC article.

Abstract The matrix protein (M1) of influenza virus plays an essential role in viral assembly and has a variety of functions, including association with influenza virus ribonucleoprotein (RNP). Our previous studies show that the association of M1 with viral RNA and nucleoprotein not only promotes formation of helical RNP but also is required for export of RNP from the nucleus during viral replication. The RNA-binding domains of M1 have been mapped to two independent regions: a zinc finger motif at amino acid positions 148 to 162 and a series of basic amino acids (RKLKR) at amino acid positions 101 to 105, which is also involved in RNP-binding activity. To further understand the role of the RNP-binding domain of M1 in viral assembly and replication, mutations in the coding sequences of RKLKR and the zinc finger motif of M1 were constructed using a PCR technique and introduced into wild-type influenza virus by reverse genetics. Altering the zinc finger motif of M1 only slightly affected viral growth. Substitution of Arg with Ser at position 101 or 105 of RKLKR did not have a major impact on nuclear export of RNP or viral replication. In contrast, deletion of RKLKR or substitution of Lys with Asn at position 102 or 104 of RKLKR resulted in a lethal mutation. These results indicate that the RKLKR domain of M1 protein plays an important role in viral replication.

WAHIS kertoo ilveksen kuolleen A H5N5 lintuinfluenssaan Norjassa. Mitä kuuluu HPAI H5N1 virukseen Suomessa?

 Löydän  suomalaisen tutkimuksen HPAI-lintuinfluenssaviruksesta ja sen  tarttuvuudesta myös ihmiskuntaan. Artikkeli on  tullut 2.1. 2025  esiin luewttavaksi. Sen voi kuunnella englanninkielellä.Kirjoittajat: Altan E, Avelin V, Aaltonen K, Korhonen E, Laine L, Lindh E.

https://www.tandfonline.com/doi/full/10.1080/22221751.2024.2447618#abstract

Research Article

Highly Pathogenic Avian Influenza (HPAI) H5N1 virus in Finland in 2021-2023 – Genetic diversity of the viruses and infection kinetics in human dendritic cells

 Accepted author version posted online: 02 Jan 2025

• Cite this article
• https://doi.org/10.1080/22221751.2024.2447618

 

WHO antaa lausuntonsa koronavirusrokotteiden antigeenikoostumuksesta 23.12.2024 , suosituksia

 https://www.who.int/news/item/23-12-2024-statement-on-the-antigen-composition-of-covid-19-vaccines

 

• Currently circulating SARS-CoV-2 variants are all derived from JN.1. The weekly proportion of XEC sequences among all SARS-CoV-2 sequences submitted to GISAID continues to increase, while the weekly proportions of all other Variants of Interest (JN.1) or Variants Under Monitoring (KP.2, KP.3, KP.3.1.1, JN.1.18 and LB.1) are now declining. There are other JN.1-derived variants that are currently in low proportions, but which have mutations that may give them an advantage over XEC: currently LP.8.1, NP.1, LF.7.2 are variants being monitored and/or characterized.
• In published and unpublished data using antisera from naïve animal models, circulating JN.1-derived variants (JN.1, JN.1.16.1, KP.2, KP.2.3, KP.3, KP.3.1.1, LB.1 and XEC) are antigenically closely related.

 ...

The timing, specific mutations and antigenic characteristics of emerging and future variants are difficult to predict, and the potential public health impact of these variants remain unknown. There are JN.1-derived variants such as LP.8.1, NP.1 and LF.7.2 that are currently in low proportions, but which have mutations that may give them more immune escape than XEC. These will continue to be monitored and/or characterized. The TAG-CO-VAC strongly supports the ongoing work of the TAG-VE. 

Estimates of VE against recently circulating SARS-CoV-2 variants, including XBB or JN.1 descendent lineages, are limited in terms of the number and geographic diversity of studies, vaccine platforms evaluated, populations assessed, and duration of follow-up. Furthermore, the referent population for VE estimates varies substantially with respect to prior history of vaccination. There are currently no direct comparative estimates for monovalent JN.1, KP.2 or XBB.1.5 vaccines versus other antigen composition(s) delivered during the same time period. Finally, VE estimates may be confounded by differences in undocumented infection-derived immunity between groups, leading to potential underestimation of VE (virus evolution)

...

Recommendations for COVID-19 vaccine antigen composition

Given the breadth in immune responses demonstrated by monovalent JN.1 lineage vaccines against circulating variants, the TAG-CO-VAC advises retaining the current COVID-19 vaccine antigen composition, i.e. a monovalent JN.1 lineage variant (NextStrain: 24A, GenBank: PP298019, GISAID: EPI_ISL_18872762) as one approach to induce enhanced neutralizing antibody responses to JN.1 and its descendent variants (e.g., KP.3.1.1 and XEC).

Other approaches that demonstrate broad and robust neutralizing antibody responses against currently circulating JN.1 descendent lineage variants, such as vaccine antigens derived from more recent variants or alternative formulations, could also be considered.

As per the WHO Director General’s  standing recommendations for COVID-19, Member States are recommended to continue to offer COVID-19 vaccination based on the recommendations of the WHO SAGE. Vaccination should not be delayed in anticipation of access to vaccines with an updated composition; vaccination programmes can continue to use any available WHO emergency-use listed or prequalified COVID-19 vaccines.

 

Further data requested

Given the limitations of the evidence upon which the recommendations above are derived and the anticipated continued evolution of the virus, the TAG-CO-VAC strongly encourages generation of the following data (in addition to the types of data outlined in October 2024): 

• Immune responses and clinical endpoints (i.e. VE and/or comparator rates of infection and severe disease) in varied human populations who receive COVID-19 vaccines with a monovalent JN.1 or KP.2 vaccine antigen composition, across different vaccine platforms, as well as further clinical and laboratory data on the performance of all currently approved COVID-19 vaccines against emerging SARS-CoV-2 variants.
• Strengthened epidemiological and virological surveillance, as per the Standing Recommendations for COVID-19 in accordance with the International Health Regulations (2005), to determine if emerging variants are antigenically distinct and able to displace circulating variants.
• Clinical evaluation of relevant new vaccine antigens derived from more recent variants.