» Articles » PMID: 36159797

Grass Carp SERPINA1 Inhibits GCRV Infection Through Degrading CF2

Overview
Journal Front Immunol
Date 2022 Sep 26
PMID 36159797
Authors
Affiliations
Soon will be listed here.
Abstract

SERPINA1, a member of the serine protease inhibitor family, plays a role in viral infection and inflammation by regulating the activities of serine and cysteine proteases. To date, there have been no reports on the immune function of SERPINA1 in fishes. In this study, we first cloned the gene of grass carp () and found that it could respond rapidly to the infection of Grass carp reovirus (GCRV), and overexpression of could enhance the antiviral response of CIK cells. A polyclonal antibody of SERPINA1 was prepared, and the protein interacting with SERPINA1 was screened by CoIP/MS in grass carp hepatopancreas tissue. It was found that SERPINA1 interacted with coagulation factor 2 (CF2) and could degrade it in a dose-dependent manner. In addition, overexpression of contributed to the infection of GCRV in CIK cells, whereas co-expression of and in grass carp reduced the copy number of GCRV in cells. The results showed that grass carp SERPINA1 could inhibit GCRV infection by degrading CF2. This study proposes that SERPINA1 can inhibit viral infection through interaction with the coagulation factor, providing new insights into the molecular mechanism of SERPINA1's antiviral function.

Citing Articles

Comparative Transcriptomics Analysis Reveals Unique Immune Response to Grass Carp Reovirus Infection in Barbel Chub ().

Huang Y, Wang X, Lv Z, Hu X, Xu B, Yang H Biology (Basel). 2024; 13(4).

PMID: 38666826 PMC: 11047996. DOI: 10.3390/biology13040214.

References
1.
Heit C, Jackson B, McAndrews M, Wright M, Thompson D, Silverman G . Update of the human and mouse SERPIN gene superfamily. Hum Genomics. 2013; 7:22. PMC: 3880077. DOI: 10.1186/1479-7364-7-22. View

2.
Andrews G, Simons B, Young J, Hawkridge A, Muddiman D . Performance characteristics of a new hybrid quadrupole time-of-flight tandem mass spectrometer (TripleTOF 5600). Anal Chem. 2011; 83(13):5442-6. PMC: 3138073. DOI: 10.1021/ac200812d. View

3.
Gabay C, Kushner I . Acute-phase proteins and other systemic responses to inflammation. N Engl J Med. 1999; 340(6):448-54. DOI: 10.1056/NEJM199902113400607. View

4.
Jonigk D, Al-Omari M, Maegel L, Muller M, Izykowski N, Hong J . Anti-inflammatory and immunomodulatory properties of α1-antitrypsin without inhibition of elastase. Proc Natl Acad Sci U S A. 2013; 110(37):15007-12. PMC: 3773761. DOI: 10.1073/pnas.1309648110. View

5.
Song S . Alpha-1 Antitrypsin Therapy for Autoimmune Disorders. Chronic Obstr Pulm Dis. 2019; 5(4):289-301. PMC: 6361478. DOI: 10.15326/jcopdf.5.4.2018.0131. View