Proteolipid protein 2, also known as Differentiation-dependent protein A4 or Intestinal membrane A4 protein, is a membrance protein which is encoded by the PLP2 gene in humans. Differential screening of a subtractive cDNA library of a particular ht29-18-c1 sequence is a highly differentiated daughter clone of ht29-18, resulting in a differentially-dependent cDNA clone, PLP2. The complete clone encoding PLP2 was obtained and sorted. It is 945 bp in length and contains an open reading frame (ORF) of 456 bp. The amino acid sequence deduced from the ORF revealed a 152 amino acid polypeptide with a predicted molecular mass of 17,000 Da, which is confirmed by in vitro transcription and translation by a full-length PLP2 cDNA. This polypeptide contains four potential membrane-producing domains, as well as consensus sequences for n-chain glycosylation, as well as phosphorylation sites for protein kinase C and casein kinase II.
|Basic Information of PLP2|
|Protein Name||Proteolipid protein 2|
|Aliases||Differentiation-dependent protein A4, Intestinal membrane A4 protein|
|Organism||Homo sapiens (Human)|
Proteolipid protein 2 is a colonic epithelial fortification protein that is restricted to the endoplasmic reticulum, similar to other proteins. The protein doubled and exhibited ion channel characteristics. PLP2 may play a role in intestinal epithelial cell differentiation. PLP2 mRNAs were detected in various cells such as U-937, HL-60, HEK293, and Stanley cells. Overexpression of PLP2 stimulated twice the migration of ho/CCR1 cells by agonists, suggesting a role for PLP2 in chemotaxis through CCR1.
Fig.1 The structure of Proteolipid protein 2.
This study links a key function to the PLP2 gene to obtain the ligation enzyme activity of the virus and highlights the power of non-fatal haploid gene screens in human cells to identify pathogen-operated genes in the host immune system.
This article proposed a computational derivation model of MHV PLP2 combined with ubiquitin. The on-site directed mutagenesis revealed the potential interaction of ubiquitin and PLP2.
These results indicate that PLP2 inhibits IRF3 nuclear translocation, thus inhibiting transcriptional activation of IFN.
This result demonstrates the important role of PLP2 in the escape of arterial virus and provides new possibilities for the development of improved attenuated virus vaccines against economically important arterial viruses and other codes encoding similar bispecific proteases.
These results indicate that coronavirus PLP2, by interacting with Behrin-1, results in incomplete autophagy, which in turn regulates coronavirus replication and antiviral innate immunity.
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