4.6 Article

Emerging of H5N6 Subtype Influenza Virus with 129-Glycosylation Site on Hemagglutinin in Poultry in China Acquires Immune Pressure Adaption

Journal

MICROBIOLOGY SPECTRUM
Volume 10, Issue 3, Pages -

Publisher

AMER SOC MICROBIOLOGY
DOI: 10.1128/spectrum.02537-21

Keywords

antigenic drift; avian influenza virus; glycosylation; vaccination

Categories

Funding

  1. National Key Research and Development Program of China [2021YFD1800202]
  2. National Natural Science Foundation of China [31872473, 31872477, 32172942]
  3. Jiangsu Provincial Natural Science Fund for Excellent Young Scholars [BK20200105]
  4. High-Level Talent Support Plan of Yangzhou University [10, 28]
  5. Postgraduate Scientific Research and Innovation Projects of Yangzhou University [XKYCX19-143]
  6. Jiangsu Province University Outstanding Science and Technology Innovation Team Project
  7. Priority Academic Program Development of Jiangsu Higher Education (PAPD)

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The effects of glycosylation site modification on hemagglutinin (HA) on the biological characteristics of the H5N6 subtype avian influenza virus (AIV) were investigated. H5N6 AIVs containing a 129-glycosylation site on HA were found to be prevalent strains in China, showing increased thermostability, decreased pH stability, and attenuated pathogenicity and contact transmission in chickens. Furthermore, these H5N6 AIVs escaped the neutralization activity of serum antibodies.
For an investigation into the effects of glycosylation site modification on hemagglutinin (HA) on the biological characteristics of the H5N6 subtype avian influenza virus (AIV), the HA sequences of H5N6 AIVs from Global Initiative on Sharing All Influenza Data (GISAID) and the isolates in China were analyzed for genetic evolution and glycosylation site patterns. Eight recombinant H5N6 AIVs with different glycosylation site patterns were constructed, and their biological characteristics were determined. The results showed that H5N6 AIVs containing a 129-glycosylation site on HA are becoming prevalent strains in China. Acquisition of the 129-glycosylation site on the HA of H5N6 AIVs increased thermostability, decreased pH stability, and attenuated pathogenicity and contact transmission in chickens. Most importantly, H5N6 AIVs escaped the neutralization activity of the Re-8-like serum antibody. Our findings reveal that H5N6 AIVs containing the 129-glycosylation site affect antigenicity and have become prevalent strains in China. IMPORTANCE H5N6 avian influenza viruses (AIVs) were first reported in 2013 and have spread throughout many countries. In China, compulsory vaccine inoculation has been adopted to control H5 subtype avian influenza. However, the effect of vaccination on the antigenic drift of H5N6 AIVs remains unknown. Here, we found that H5N6 AIVs with the 129-glycosylation site on hemagglutinin were the dominant strains in poultry in China. The neutralization assay of the serum antibody against the H5 subtype vaccine Re-8 showed a significantly lower neutralization activity against H5N6 AIVs with the 129-glycosylation site compared to that against H5N6 AIVs without the 129-glycosylation site, indicating that the 129-glycosylation site may be a crucial molecular marker for immune evasion. H5N6 avian influenza viruses (AIVs) were first reported in 2013 and have spread throughout many countries. In China, compulsory vaccine inoculation has been adopted to control H5 subtype avian influenza.

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