H9N2 influenza viruses prevalent in poultry in China are phylogenetically distinct from A/quail/Hong Kongl/G1/97 presumed to be the donor of the internal protein genes of the H5N1 Hong Kong/97 virus

Liu, Jinhua; Okazaki, Katsunori; Ozaki, Hiroichi; Sakoda, Yoshihiro; Wu, Qingmin; Chen, Fuyong; Kida, Hiroshi

doi:10.1080/0307-9450310001596728

Cited by 45 publications

(36 citation statements)

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“…Attention has not only been on the epidemics in the major poultry species, the domestic fowl (Liu et al ., 2003;de Wit et al ., 2004;Ellis et al ., 2004a, b;Lee et al ., 2004a;Armin et al ., 2004), but also in minor species, including turkeys , commercial ducks (Kwon et al ., 2005), and waterfowl and other wild birds (Ellis et al ., 2004a).…”

Section: Viruses Of Wild Birds and Minor Domestic Speciesmentioning

confidence: 99%

Coronaviruses in poultry and other birds

2005

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Section: Viruses Of Wild Birds and Minor Domestic Speciesmentioning

confidence: 99%

Coronaviruses in poultry and other birds

2005

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“…To test whether PB1-F2 protein contributes to virulence of highly pathogenic influenza viral strains, we cloned the PB1 gene from the A/HK/156/97 virus, a pathogenic H5N1 virus which caused a lethal infection in a 3-year-old boy in Hong Kong in 1997 (5). Interestingly, the PB1 gene of this virus came from a distinct avian source (10,14). Using the strategy outlined above, we knocked out the PB1-F2 protein open reading frame and generated two viruses: WSN with HK PB1 (WH) and WSN with HK PB1 knocked out for PB1-F2 (WHdelF2).…”

Section: Pb1-f2 Protein Expression In the Context Of Viral Infectionmentioning

confidence: 99%

Influenza A Virus PB1-F2 Protein Contributes to Viral Pathogenesis in Mice

Zamarin

Ortigoza

Palese

2006

J Virol

275

307

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The influenza virus PB1-F2 protein is a novel protein previously shown to be involved in induction of cell death. Here we characterize the expression and the function of the protein within the context of influenza viral infection in tissue culture and a mouse model. We show that the C-terminal region of the protein can be expressed from a downstream initiation codon and is capable of interaction with the full-length protein. Using this knowledge, we generated influenza viruses knocked out for the expression of PB1-F2 protein and its downstream truncation products. Knocking out the PB1-F2 protein had no effect on viral replication in tissue culture but diminished virus pathogenicity and mortality in mice. The viruses replicated to similar levels in mouse lungs by day 3 postinfection, suggesting that the knockout did not impair viral replication. However, while the PB1-F2 knockout viruses were cleared after day 5, the wild-type viruses were detectable in mouse lungs until day 7, implying that expression of PB1-F2 resulted in delayed clearance of the viruses by the host immune system. Based on our findings and on the fact that the PB1 genomic segment was always newly introduced into some pandemic influenza viruses of the last century, we speculate that the PB1-F2 protein plays an important role in pathogenesis of influenza virus infection and may be an important contributor to pathogenicity of pandemic influenza viruses.In the course of a systematic search for influenza virus antigenic peptides presented by major histocompatibility complex class I on the surface of infected cells, a cytotoxic T lymphocyte (CTL) peptide that did not correspond to any of the known standard viral open reading frames was identified (4). Further screening of the influenza virus genome revealed that the peptide corresponded to residues 62 to 70 of an 87-amino-acidlong protein encoded by an alternate reading frame within the PB1 gene (4). The translation of the novel protein starts from nucleotide position 120 in the PB1 genomic segment and is believed to be initiated by ribosomal scanning (4, 13). In view of the fact that the protein is expressed from a second open reading frame (ϩ1) of the PB1 gene, it was named PB1-F2 (4).Further work showed that PB1-F2 is a relatively short-lived protein which is maximally expressed about 5 hours postinfection (4). The protein localizes to both inner and outer mitochondrial membranes, resulting in alteration of mitochondrial morphology, dissipation of mitochondrial membrane potential, and cell death. Knocking out the PB1-F2 open reading frame attenuated the ability of the A/Puerto Rico/8/34 virus to induce apoptosis in immune cells (4). Subsequently, the basic amphipathic helix in the C-terminal region of the PB1-F2 protein was shown to be responsible for its inner mitochondrial membrane targeting (9, 26) and peptides derived from the C-terminal domain were shown to have a cytotoxic effect and to induce formation of nonspecific pores in synthetic bilayer membranes (2).We further recently showed that P...

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“…Subsequently, specific antibodies to H9N2 AIV were detected in poultry workers and patients (1,5). These findings pointed to a possibility that AIVs such as H9N2 could infect humans directly, without acquiring human or mammalian influenza genes in an intermediate host, and emerge as or contribute to the reemergence of highly pathogenic viruses (3,4,(6)(7)(8).…”

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confidence: 99%