tetano
Editor, Senior Moderator
Bing Du Xue Bao. 2014 Sep;30(5):521-8.
[h=1][Preliminary study of a universal vaccine based on the HA2 protein of the H5N1 influenza virus].[/h] [Article in Chinese]
Xin L[SUP]1[/SUP], Yang XY, Yu ZJ, Bo H, Zhou JF, Qin K, Shu YL.
[h=3]Author information[/h]
[h=3]Abstract[/h] Fragments encoding amino acids 76-130 in the linear conserved region (LCR) of A/Hubei/1/2010 (H5N1) HA2 was fused to hepatitis B core antigen (HBc) to generate a LCR-HBe virus-like particle (VLP). Results showed that the fusion protein of LCR-HBc was highly expressed in this prokaryotic expression system. The purified LCR-HBc particle stimulated high levels of IgG production in mice with a titer of > 1:12 800, and provided 50% cross-protection against lethal challenge by H1N1 viruses.
PMID: 25562961 [PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/25562961
[h=1][Preliminary study of a universal vaccine based on the HA2 protein of the H5N1 influenza virus].[/h] [Article in Chinese]
Xin L[SUP]1[/SUP], Yang XY, Yu ZJ, Bo H, Zhou JF, Qin K, Shu YL.
[h=3]Author information[/h]
[h=3]Abstract[/h] Fragments encoding amino acids 76-130 in the linear conserved region (LCR) of A/Hubei/1/2010 (H5N1) HA2 was fused to hepatitis B core antigen (HBc) to generate a LCR-HBe virus-like particle (VLP). Results showed that the fusion protein of LCR-HBc was highly expressed in this prokaryotic expression system. The purified LCR-HBc particle stimulated high levels of IgG production in mice with a titer of > 1:12 800, and provided 50% cross-protection against lethal challenge by H1N1 viruses.
PMID: 25562961 [PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/25562961