SERINC5 restricts influenza virus infectivity
Fei Zhao1, Fengwen Xu1, Xiaoman Liu1
1NHC 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.
Plos Pathogens
|October 12, 2022
Summary
The serine incorporator 5 (SERINC5) protein restricts influenza A virus by blocking early cell entry. Viral hemagglutinin (HA) glycosylation sites influence sensitivity to SERINC5 restriction.
Area of Science:
- Virology
- Cell Biology
- Protein Function
Background:
- Serine incorporator 5 (SERINC5) is a transmembrane protein known to inhibit human immunodeficiency virus type 1 (HIV-1) and other retroviruses.
- The precise antiviral spectrum and molecular mechanisms of SERINC5 restriction remain incompletely elucidated.
Purpose of the Study:
- To investigate the role of SERINC5 in the restriction of influenza A virus (IAV) infection.
- To determine the impact of viral envelope glycoproteins, specifically influenza hemagglutinin (HA), on SERINC5-mediated restriction.
Main Methods:
- Assessing SERINC5's effect on influenza A virus infection.
- Analyzing the sensitivity of different influenza HA subtypes to SERINC5.
- Mutational analysis of HA glycosylation sites to evaluate their role in SERINC5 resistance.
Main Results:
- SERINC5 inhibits influenza A virus infection by targeting an early step in virus-cell membrane fusion.
- Different influenza HA subtypes display varying degrees of sensitivity to SERINC5.
- Specific HA glycosylation sites were identified as crucial for conferring resistance to SERINC5 restriction, with mutations abolishing the inhibitory effect.
Conclusions:
- The antiviral activity of SERINC5 extends to influenza A virus, targeting the fusion process.
- Viral envelope glycosylation, particularly on HA, plays a significant role in mediating resistance to SERINC5.
- This study expands the known antiviral targets of SERINC5 and highlights the importance of viral glycoproteins in host restriction mechanisms.
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