h5n1 avian influenza virus
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2021 ◽  
Vol 26 (3) ◽  
pp. 115
Author(s):  
Dyah Ayu Hewajuli ◽  
NLP Indi Dharmayanti ◽  
I Wayan Teguh Wibawan

The objective of this research was to know the sensitivity of H5N1 clade 2.3.2 AIV from Indonesia to antiviral drug (amantadine) through molecular and in vitro tests. The study was conducted by virus isolation and identification, nucleotide analysis, and susceptibility to the amantadine hydrocloride in MDCK cells. The study result represented that the mean EID<sub>50 </sub>isolates of H5N1 clade 2.3.2 AIV was determined of &gt;10<sup>8 </sup>EID<sub>50</sub>/ml. The analysis of phylogenetic tree of M2 gene from six viruses of H5N1 clade 2.3.2 AIV from Indonesia were closed with H5N1 clade 2.3.2 AIV avian influenza viruses from Vietnam, China, Hongkong. The substitution of M2 protein (V27I) was identified in six isolates H5N1 clade 2.3.2 AIV isolated from Indonesia. Avian influenza of clade 2.3.2 H5N1 subtype from Indonesia produced the formation of CPE and the positive HA reaction with non-toxic concentration of amantadine hydrochloride in MDCK cells. The result of genetic analysis of M2 gene for amantadine resistance was related with the results of HA test and the formation of CPE in MDCK cells. These results established that amantadine resistance have been identified in H5N1 clade 2.3.2 AIV viruses isolated from Indonesia


2021 ◽  
Vol 12 ◽  
Author(s):  
Qiao Wang ◽  
Qi Zhang ◽  
Maiqing Zheng ◽  
Jie Wen ◽  
Qinghe Li ◽  
...  

As a highly pathogenic influenza virus, H5N1 avian influenza virus (AIV) poses a great threat to poultry production and public health. H5N1 AIV has a small genome and, therefore, relies heavily on its host cellular machinery to replicate. To develop a comprehensive understanding of how H5N1 AIV rewires host cellular machinery during the course of infection, it is crucial to identify which host proteins and complexes come into physical contact with the viral proteins. Here, we utilized affinity purification mass spectrometry (AP-MS) to systematically determine the physical interactions of 11 H5N1 AIV proteins with host proteins in chicken DF1 cells. We identified with high confidence 1,043 H5N1 AIV–chicken interactions involving 621 individual chicken proteins and uncovered a number of host proteins and complexes that were targeted by the viral proteins. Specifically, we revealed that chicken Staufen double-stranded RNA-binding protein 2 interacts with AIV non-structural protein 1 (NS1) and promotes the replication of the virus by enhancing the nuclear export of NS1 mRNA. This dataset facilitates a more comprehensive and detailed understanding of how the host machinery is manipulated during the course of H5N1 AIV infection.


2020 ◽  
Vol 18 (3) ◽  
pp. 477-485
Author(s):  
Pham Thi Van ◽  
Ho Thi Huong ◽  
Nguyen Thu Giang ◽  
Pham Bich Ngoc ◽  
Vu Huyen Trang ◽  
...  

Vaccination is one of the most effective and cost-beneficial interventions for protection of animals against the highly pathogenic A/H5N1 avian influenza virus. Haemagglutinin (HA) is a transmembrane glycoprotein of A/H5N1 virus and is a critical antigen for development of the influenza vaccine. The haemagglutinin-based vaccine produced in plants was demonstrated as a candidate vaccine since it elicited neutralizing antibodies against A/H5N1 virus. In this study, immunogenicity and protective ability of a plant-based recombinant HA antigen which was fused to IgMFc to form oligomerized HA antigen (H5TG oligomer) had been evaluated by vaccination in chickens. Chicken sera after each vaccination were collected for Western blot, ELISA and HI assays. Ten days after the second vaccination, the chickens have been challenged with A/duck/TG/NAVET(3)/2013 virus, clade 1.1. The analysis results showed that the oligomeric recombinant H5TG antigen elicited stronger H5TG-specific IgY antibodies and A/H5N1 clade 1.1 virus-neutralizing antibodies than the H5TGpII trimeric recombinant antigen without fusing IgMFc in vaccinated chickens. Notably, the chicken protection rate against A/H5N1 clade 1.1 virus of the H5TG oligomer antigen was 80% that is not significantly lower than that of a commercial vaccine as a positive control from National Veterinary Joint Stock company NAVETCO, Vietnam with the chicken protective rate of 90%. Whereas the chicken protection rate against A/H5N1 clade 1.1 virus of the H5TG trimer antigen was 50%. These results suggest that the IgMFc motif plays an important role in the forming of oligomeric proteins which had been proved for enhancing immunogenicity and protection ability in this study. Therefore, the plant-based oligomerized recombinant H5TG antigen is a potential vaccine candidate against A/H5N1 influenza virus in the future.


2020 ◽  
Vol 117 (30) ◽  
pp. 17957-17964 ◽  
Author(s):  
Ali H. Ellebedy ◽  
Raffael Nachbagauer ◽  
Katherine J. L. Jackson ◽  
Ya-Nan Dai ◽  
Julianna Han ◽  
...  

There is a need for improved influenza vaccines. In this study we compared the antibody responses in humans after vaccination with an AS03-adjuvanted versus nonadjuvanted H5N1 avian influenza virus inactivated vaccine. Healthy young adults received two doses of either formulation 3 wk apart. We found that AS03 significantly enhanced H5 hemagglutinin (HA)-specific plasmablast and antibody responses compared to the nonadjuvanted vaccine. Plasmablast response after the first immunization was exclusively directed to the conserved HA stem region and came from memory B cells. Monoclonal antibodies (mAbs) derived from these plasmablasts had high levels of somatic hypermutation (SHM) and recognized the HA stem region of multiple influenza virus subtypes. Second immunization induced a plasmablast response to the highly variable HA head region. mAbs derived from these plasmablasts exhibited minimal SHM (naive B cell origin) and largely recognized the HA head region of the immunizing H5N1 strain. Interestingly, the antibody response to H5 HA stem region was much lower after the second immunization, and this suppression was most likely due to blocking of these epitopes by stem-specific antibodies induced by the first immunization. Taken together, these findings show that an adjuvanted influenza vaccine can substantially increase antibody responses in humans by effectively recruiting preexisting memory B cells as well as naive B cells into the response. In addition, we show that high levels of preexisting antibody can have a negative effect on boosting. These findings have implications toward the development of a universal influenza vaccine.


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