Vioserpin, a serine protease inhibitor from Gloeobacter violaceus possibly regulated by heparin

Oliveira, Jocélia P.C.; Salazar, Natalia; Zani, Marcelo B.; Souza, Lucas R. de; Passos, Silvia G.; Sant'Ana, Aquiles M.; Andrade, Regiane A. de; Marcili, Arlei; Sperança, Márcia Aparecida; Puzer, Luciano

doi:10.1016/j.biochi.2016.05.006

Cited by 5 publications

(1 citation statement)

References 28 publications

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“…The expressed serpin, called vioserpin, shares heparin-binding sites with eukaryotic serpins such as kallistatin and thrombin. Vioserpin efficiently inhibits trypsin-like activity and forms a covalent complex [ 129 ]. Recently, a new serpin (PI-QT) was identified from the metagenome of a sponge-associated microorganism.…”

Section: Serpins Natural Inhibitors To Control the Activity Of Serine Proteasesmentioning

confidence: 99%

Gut Serpinome: Emerging Evidence in IBD

Mkaouar

Mariaule

Rhimi

et al. 2021

IJMS

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Inflammatory bowel diseases (IBD) are incurable disorders whose prevalence and global socioeconomic impact are increasing. While the role of host genetics and immunity is well documented, that of gut microbiota dysbiosis is increasingly being studied. However, the molecular basis of the dialogue between the gut microbiota and the host remains poorly understood. Increased activity of serine proteases is demonstrated in IBD patients and may contribute to the onset and the maintenance of the disease. The intestinal proteolytic balance is the result of an equilibrium between the proteases and their corresponding inhibitors. Interestingly, the serine protease inhibitors (serpins) encoded by the host are well reported; in contrast, those from the gut microbiota remain poorly studied. In this review, we provide a concise analysis of the roles of serine protease in IBD physiopathology and we focus on the serpins from the gut microbiota (gut serpinome) and their relevance as a promising therapeutic approach.

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Section: Serpins Natural Inhibitors To Control the Activity Of Serine Proteasesmentioning

confidence: 99%

Gut Serpinome: Emerging Evidence in IBD

Mkaouar

Mariaule

Rhimi

et al. 2021

IJMS

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Serpin Phage Display: The Use of a T7 System to Probe Reactive Center Loop Libraries with Different Serine Proteinases

Souza

Scott

Bhakta

et al. 2018

Methods in Molecular Biology

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Phage display is a protein engineering approach that involves construction of libraries of variant proteins displayed on the surface of bacteriophage as capsid fusion proteins and their screening for binding and inhibitory function through the use of bait proteins. Recently, we adapted a commercially available T7 phage display system to create phage-displayed serpin libraries hypervariable in up to five positions in their reactive center loop (RCL). The RCL is a key determinant in serpin specificity, the relationship between the structure of a given serpin and which target proteinase(s) it inhibits. In this chapter, we describe protocols to assess the feasibility of this method for different serpin/proteinase combinations and share experience with this technology gathered in the course of studying two serpins and multiple proteinases with this powerful iterative screening approach.

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