2. Academic Validation
  3. SERINC5 restricts influenza virus infectivity

SERINC5 restricts influenza virus infectivity

  • PLoS Pathog. 2022 Oct 12;18(10):e1010907. doi: 10.1371/journal.ppat.1010907.
Fei Zhao 1,  Fengwen Xu 1,  Xiaoman Liu 1,  Yamei Hu 1,  Liang Wei 1,  Zhangling Fan 1,  Liming Wang 1,  Yu Huang 1,  Shan Mei 1,  Li Guo 2,  Long Yang 3,  Shan Cen 4,  Jianwei Wang 2,  Chen Liang 5,  Fei Guo 1
Affiliations

Affiliations

  • 1 NHC Key Laboratory of Systems Biology of Pathogens, Institute of Pathogen Biology, and Center for AIDS Research, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, P. R. China.
  • 2 NHC Key Laboratory of Systems Biology of Pathogens and Christophe Mérieux Laboratory, Institute of Pathogen Biology, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, P. R. China.
  • 3 School of Integrative Medicine, Tianjin University of Traditional Chinese Medicine, Tianjin, China.
  • 4 Institute of Medicinal Biotechnology, Chinese Academy of Medical Sciences & Peking Union Medical College, Beijing, P. R. China.
  • 5 McGill University AIDS Centre, Lady Davis Institute, Jewish General Hospital, Montreal, Quebec, Canada.
PMID: 36223419 DOI: 10.1371/journal.ppat.1010907
Abstract

SERINC5 is a multi-span transmembrane protein that is incorporated into HIV-1 particles in producing cells and inhibits HIV-1 entry. Multiple retroviruses like HIV-1, equine infectious anemia virus and murine leukemia virus are subject to SERINC5 inhibition, while HIV-1 pseudotyped with envelope glycoproteins of vesicular stomatitis virus and Ebola virus are resistant to SERINC5. The Antiviral spectrum and the underlying mechanisms of SERINC5 restriction are not completely understood. Here we show that SERINC5 inhibits influenza A virus Infection by targeting virus-cell membrane fusion at an early step of Infection. Further results show that different Influenza Hemagglutinin (HA) subtypes exhibit diverse sensitivities to SERINC5 restriction. Analysis of the amino acid sequences of influenza HA1 strains indicates that HA glycosylation sites correlate with the sensitivity of influenza HA to SERINC5, and the inhibitory effect of SERINC5 was lost when certain HA glycosylation sites were mutated. Our study not only expands the Antiviral spectrum of SERINC5, but also reveals the role of viral envelope glycosylation in resisting SERINC5 restriction.

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