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Characterization of the testis-specific proteasome subunit ?4s in mammals.

ABSTRACT: The 26 S proteasome is responsible for regulated proteolysis in eukaryotic cells. It is composed of one 20 S core particle (CP) flanked by one or two 19 S regulatory particles. The CP is composed of seven different ?-type subunits (?1-?7) and seven different ?-type subunits, three of which are catalytic. Vertebrates encode four additional catalytic ? subunits that are expressed predominantly in immune tissues and produce distinct subtypes of CPs particularly well suited for the acquired immune system. In contrast, the diversity of ? subunits remains poorly understood. Recently, another ? subunit, referred to as ?4s, was reported. However, little is known about ?4s. Here we provide a detailed characterization of ?4s and the ?4s-containing CP. ?4s is exclusively expressed in germ cells that enter the meiotic prophase and is incorporated into the CP in place of ?4. A comparison of structural models revealed that the differences in the primary sequences between ?4 and ?4s are located on the outer surface of the CP, suggesting that ?4s interacts with specific molecules via these unique regions. ?4s-containing CPs account for the majority of the CPs in mouse sperm. The catalytic ? subunits in the ?4s-containing CP are ?1, ?2, and ?5, and immunosubunits are not included in the ?4s-containing CP. ?4s-containing CPs have a set of peptidase activities almost identical to those of ?4-containing CPs. Our results provide a basis for understanding the role of ?4s and male germ cell-specific proteasomes in mammals.

SUBMITTER: Uechi H

PROVIDER: S-EPMC4007433 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature

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Characterization of the testis-specific proteasome subunit α4s in mammals.

Uechi Hiroyuki H Hamazaki Jun J Murata Shigeo S

The Journal of biological chemistry 20140325 18

The 26 S proteasome is responsible for regulated proteolysis in eukaryotic cells. It is composed of one 20 S core particle (CP) flanked by one or two 19 S regulatory particles. The CP is composed of seven different α-type subunits (α1-α7) and seven different β-type subunits, three of which are catalytic. Vertebrates encode four additional catalytic β subunits that are expressed predominantly in immune tissues and produce distinct subtypes of CPs particularly well suited for the acquired immune s ...[more]

PMID: 24668818

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Project description:BackgroundPrevious study showed that Trichinella spiralis proteasome subunit beta type-7 (Tspst) gene is an up-regulated gene in intestinal infective larvae (IIL) compared to muscle larvae (ML), which was screened by using suppression subtractive hybridization (SSH) and confirmed by real-time PCR. Tspst may be related to the larval invasion of intestinal epithelial cells (IECs). The aim of this study was to identify Tspst and to investigate its immune protection against intestinal T. spiralis infection.MethodsThe Tspst gene encoding a 29 kDa protein from T. spiralis infective larvae was cloned, and recombinant Tspst protein (rTspst) was produced in an Escherichia coli expression system. The rTspst was used to immunize BALB/c mice. Anti-rTspst antibodies were used to determine the immunolocolization of Tspst in the parasite. Transcription and expression of Tspst at T. spiralis different developmental stages were observed by RT-PCR and immunofluorescence test (IFT). The in vitro or in vivo immune protection of anti-rTspst serum or rTspst against intestinal T. spiralis infection in BALB/c mice was evaluated.ResultsAnti-rTspst serum recognized the native Tspst protein with 29 kDa in ML crude antigens. Transcription and expression of gene was observed at all T. spiralis different developmental stages (IIL, adult worms, newborn larvae, and ML). An immunolocalization analysis identified Tspst in the cuticle and internal organs of the parasite. An in vitro invasion assay showed that, when anti-rTspst serum, serum of mice infected with T. spiralis or normal mouse serum were added to the medium, the invasion rate of the infective larvae in an IEC monolayer was 25.2%, 11.4%, and 79%, respectively (P < 0.05), indicating that anti-rTspst serum partially prevented the larval invasion of IECs. After a challenge infection with T. spiralis muscle larvae, mice immunized with rTspst conferred a 45.7% reduction in adult worm burden in intestines.ConclusionsIn the present study, Tspst was first identified and characterized. Tspst is an invasion-related protein of T. spiralis IIL and could be considered as a potential vaccine candidate antigen against intestinal T. spiralis infection that merits further study.

Dataset Information

Characterization of the testis-specific proteasome subunit ?4s in mammals.

Publications

Characterization of the testis-specific proteasome subunit α4s in mammals.

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