Serine incorporator 5 is a membrane protein that is encoded by the SERINC5 gene in humans. Researchers have reported that this protein is an important factor in the process of host-virus interaction. SERINC5 is closely related to the serine biosynthesis process, which is a vital way for serine metabolization in vivo. It is always companied by another member of SERINC family, SERINC3. They both have a vital influence on human’s health together.
|Basic Information of SERINC5|
|Protein Name||Serine incorporator 5|
|Organism||Homo sapiens (Human)|
SERINC5 is a restriction factor of controlling infectivity of lentiviruses like HIV-1. It always functions by inhibiting an early step of viral infection. The protein can boost the penetration of the viral particle into the cytoplasm and promote the incorporation of serine into phosphatidylserine and sphingolipids. It can also provide serine molecules to help the formation of myelin glycosphingolipids in oligodendrocytes. SERINC5 takes part in various processes such as innate immune response, L-serine biosynthetic process, phosphatidylserine metabolic process, positive regulation of CDP-diacylglycerol-serine O-phosphatidyltransferase activity and sphingolipid metabolic process. It can also affect the lipid biosynthesis and lipid metabolism process.
Fig.1 SERINC5 is a restriction factor that impairs the infectivity of retroviral particles. (Heigele, 2016)
This report shows that the host cell proteins SERINC3 and SERINC5 are potent inhibitors of HIV-1 particle infectivity and Nef can regulate these effects. Both SERINC3 and SERINC5 are restrictions to HIV replication in human cells, which might be novel activities for the HIV pathogenesis factor.
In this article, authors find that S2 is compatible with a key role of the post-translational modification, and its N-terminal glycine is required for the anti-SERINC5 activity.
HIV is usually not found by host antiviral immunity by downregulating cell-surface immunoreceptors. In this paper, authors systematically examine how HIV-1 infection remodels the T cell surface and identifies serine carriers SERINC3/5 and alanine transporter SNAT1 as targets of HIV-1 Nef and Vpu, respectively.
This article shows that the cellular factor SERINC5 can impair HIV-1 infectivity but is antagonized by the viral Nef protein. They also find a significant correlation between anti-SERINC5 potency and the SIV prevalence in the respective ape and monkey species. Nef-mediates SERINC5 antagonism may determine the ability of primate lentiviruses to spread within natural hosts.
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