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A revision of the system of nomenclature for influenzaviruses: a W.H.O. memorandum.
TLDR
This revised system of nomenclature which has been in use since 1971 should be used universally from the date of publication of this Memorandum.Abstract:
In February 1980, the World Health Organization convened a meeting to consider information relevant to the nomenclature of influenza viruses and to make definitive proposals for the revision of the system which has been in use since 1971. The WHO recommendations are based on data derived from double immunodiffusion reactions involving haemagglutinin and neuraminidase antigens. The revised system of nomenclature is similar to the 1971 system in that it consists of two parts: (a) a type and strain designation, and (b) for influenza A viruses, a description of the antigenic specificity (subtype) of the surface antigens (H and N). The strain designation for influenza virus types A, B, and C contains information on the antigenic type of the virus (based on the antigenic specificity of the nucleoprotein), the host of origin (for strains isolated from non-human sources), geographical origin, strain number, and year of isolation. For influenza A viruses, the antigenic description, in parentheses, follows the strain designation and comprises two indices describing the antigenic subtype of the haemagglutinin and of the neuraminidase antigens. For the influenza A viruses from all species, the H antigens are grouped into 12 subtypes, H1-H12, while the N antigens are divided into 9 subtypes, N1-N9. Reference strains of influenza viruses are maintained by the WHO Collaborating Centres for Reference and Research on Influenza and the WHO Centres for the Study of Influenza Ecology in Animals, and are made available upon request.There is no provision for describing distinct subtypes of influenza B and C viruses. The existence of antigenic variation among influenza B strains is well established but the available information shows that a division into subtypes is not warranted.This revised system of nomenclature should be used universally from the date of publication of this Memorandum.read more
Citations
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Discovery of novel antiviral agents directed against the influenza A virus nucleoprotein using photo-cross-linked chemical arrays
Kyoji Hagiwara,Yasumitsu Kondoh,Atsushi Ueda,Kazunori D. Yamada,Hideo Goto,Toshiki Watanabe,Tadashi Nakata,Hiroyuki Osada,Yoko Aida +8 more
TL;DR: Artificial analogs of mycalamide A in a chemical array bound specifically with high affinity to NP and inhibited multiplication of the influenza virus, suggesting that chemical arrays are convenient tools for the screening of viral product inhibitors.
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Theoretical studies on the susceptibility of oseltamivir against variants of 2009 A/H1N1 influenza neuraminidase.
TL;DR: Molecular simulations show that N294S and H274Y, two popular drug-resistant mutations in different variants of NA, still cause significant resistance to oseltamivir, and the results will be useful for the rational design of NA inhibitors with high potency against drug- resistant A/H1N1 mutants.
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Failure to detect hemagglutination-inhibiting antibodies with intact avian influenza virions.
TL;DR: It is indicated that avian influenza viruses do induce high levels of antibodies in ferrets, ducks, and mice and produce long-lived memory for cytotoxic T-cells in mice and seroepidemiological studies with conventional hemagglutination inhibition tests could give misleading results.
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Recent Advances in Neuraminidase Inhibitor Development as Anti-influenza Drugs
Enguang Feng,Deju Ye,Jian Li,Dengyou Zhang,Jinfang Wang,Fei Zhao,Rolf Hilgenfeld,Rolf Hilgenfeld,Mingyue Zheng,Hualiang Jiang,Hong Liu +10 more
TL;DR: The structural characteristics of NA catalytic domains and the recent developments of new NA inhibitors using structure‐based drug design strategies are discussed and present promising options for therapeutics or leads for further development of NA inhibitors that may be useful in the event of a future influenza pandemic.
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Induced opening of influenza virus neuraminidase N2 150-loop suggests an important role in inhibitor binding
Yan Wu,Guangrong Qin,Feng Gao,Yue Liu,Christopher J. Vavricka,Jianxun Qi,Hualiang Jiang,Kunqian Yu,George F. Gao +8 more
TL;DR: It is demonstrated for the first time that oseltamivir carboxylate can induce opening of the rigid closed N2 150-loop and provide a novel mechanism for150-loop movement using molecular dynamics simulations, which provides the structural and biophysical basis of the open form of 150- loop.
References
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Journal ArticleDOI
Characterization of a Novel Influenza A Virus Hemagglutinin Subtype (H16) Obtained from Black-Headed Gulls
Ron A. M. Fouchier,Vincent J. Munster,Anders Wallensten,Theo M. Bestebroer,Sander Herfst,Derek J. Smith,Derek J. Smith,Gus F. Rimmelzwaan,Bjorn R. Olsen,Albert D. M. E. Osterhaus +9 more
TL;DR: A previously unidentified antigenic subtype of HA (H16), detected in viruses circulating in black-headed gulls in Sweden, is described and proposed that sequence analyses of HA and NA genes of influenza A viruses be used for the rapid identification of existing and novel HA andNA subtypes.
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A distinct lineage of influenza A virus from bats
Suxiang Tong,Yan Li,Pierre Rivailler,Christina Conrardy,Danilo A. Alvarez Castillo,Li-Mei Chen,Sergio Recuenco,James A. Ellison,Charles T. Davis,Ian A. York,Amy S. Turmelle,David Moran,Shannon Rogers,Mang Shi,Ying Tao,Michael R. Weil,Kevin Tang,Lori A. Rowe,Scott Sammons,Xiyan Xu,Michael Frace,Kim A. Lindblade,Nancy J. Cox,Larry J. Anderson,Charles E. Rupprecht,Ruben O. Donis +25 more
TL;DR: Despite its divergence from known influenza A virus, the bat virus is compatible for genetic exchange with human influenza viruses in human cells, suggesting the potential capability for reassortment and contributions to new pandemic or panzootic influenza A viruses.
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Structure of influenza hemagglutinin in complex with an inhibitor of membrane fusion
Rupert J. Russell,Philip S. Kerry,D.J. Stevens,David A. Steinhauer,Stephen R. Martin,Steven J. Gamblin,John J. Skehel +6 more
TL;DR: The structure of HA in complex with a known inhibitor of membrane fusion and virus infectivity, tert-butyl hydroquinone (TBHQ), shows that the inhibitor binds in a hydrophobic pocket formed at an interface between HA monomers that stabilizes the neutral pH structure.
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Bat-derived influenza-like viruses H17N10 and H18N11
TL;DR: Structural and functional studies of the two major surface envelope proteins demonstrate that neither has canonical HA or NA functions found in influenza viruses, but potential genomic reassortments of such influenza-like viruses with canonical influenza viruses cannot be excluded at this point and should be assessed.