ArticlePloS one2012
Antimicrobial activity and molecular mechanism of the CRES protein.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Mendelian Randomization to Examine the Causal Effects of Cystatin on Ovarian Lesions.International journal of women's health · 2026Article
- Evaluation of an experimental therapy based on bovine mesenchymal stem cell (MSC) secretome for the treatment of endometritis in dairy cows.Scientific reports · 2025Article
- Single-cell RNA sequencing comparison of CD4+, CD8+ and T-cell receptor γδ+ cutaneous T-cell lymphomas reveals subset-specific molecular phenotypes.The British journal of dermatology · 2025Article
- Molecular characterization, expression and immune functional analysis of cystatin 10 in turbot.Molecular biology reports · 2024Article
- Host defense functions of the epididymal amyloid matrix.Molecular human reproduction · 2022Article
- The epididymal amyloid matrix: structure and putative functions.Andrology · 2019Review
- The Functional Mammalian CRES (Cystatin-Related Epididymal Spermatogenic) Amyloid is Antiparallel β-Sheet Rich and Forms a Metastable Oligomer During Assembly.Scientific reports · 2019Article
- Why are Functional Amyloids Non-Toxic in Humans?Biomolecules · 2017Review
- Functional Amyloids in Reproduction.Biomolecules · 2017Review
- Male infertility-related molecules involved in sperm-oocyte fusion.The Journal of reproduction and development · 2017Review
- Cystatin-related epididymal spermatogenic subgroup members are part of an amyloid matrix and associated with extracellular vesicles in the mouse epididymal lumen.Molecular human reproduction · 2016Article
- Suppression of antimicrobial peptide expression by ureaplasma species.Infection and immunity · 2014Article
- Immunomodulatory and antibacterial effects of cystatin 9 against Francisella tularensis.Molecular medicine (Cambridge, Mass.) · 2013Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cystatin-related epididymal spermatogenic (CRES) protein, a member of the cystatin superfamily of cysteine protease inhibitors (also known as CST8), exhibits highly specific, age-dependent expression in mouse testis and epididymis. The CRES protein possesses four highly conserved cysteine residues which govern the overall conformation of the cystatins through the formation of two disulfide bonds. Previous studies have revealed that other cystatin family members, such as cystatin 3 and cystatin 11, show antibacterial activity in vitro. This prompted us to investigate the potential antimicrobial activity of the CRES protein. Colony forming assays and spectrophotometry were used to investigate the effects of recombinant CRES protein on Escherichia coli (E. coli) and Ureaplasma urealyticum (Uu), respectively, in vitro. After incubation of E. coli with CRES recombinant protein fused with glutathione-S-transferase (GST), a substantial decrease in colony forming units was observed, and the effect was dose and time dependent. Furthermore, it took longer for Uu to grow to plateau stage when incubated with GST-CRES recombinant protein compared with the control GST. The antibacterial and Anti-Uu activities were not impaired when the cysteine residues of CRES protein were mutated, indicating that the antimicrobial effect was not dependent on its disulfide bonds. Functional analysis of three CRES polypeptides showed that the N-terminal 30 residues (N30) had no antimicrobial activity while N60 showed similar activity as full-length CRES protein. These results suggest that the active center of CRES protein resides between amino acid residues 31 and 60 of its N-terminus. Mechanistically, E. coli membrane permeabilization was increased in a dose-dependent manner, and macromolecular synthesis was inhibited on treatment with GST-CRES. Together, our data on the antimicrobial activities of CRES protein suggest that it is a novel and innate antimicrobial protein which protecting the male reproductive tract against invading pathogens.
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