Structural and functional properties of rBmTI-A: A Kunitz-BPTI serine protease inhibitor with therapeutical potential

Ferreira, Graziele Cristina; Camillo, Lívia de Moraes Bomediano; Sasaki, Sergio D.

doi:10.1016/j.biochi.2022.08.004

Cited by 3 publications

(1 citation statement)

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“…Elastase contributes to many activities reported for neutrophils [ 82 ], and neutrophil elastase inhibitors are under investigation to treat a number of inflammatory conditions [ 83 ]. As a proof of concept, a recombinant preparation of B. microplus Trypsin Inhibitor A (rBmTI-A)—originally extracted from tick larvae—is a strong neutrophil elastase inhibitor and presented anti-inflammatory properties in experimental models of elastase-induced emphysema and other pulmonary inflammatory disorders [ 84 ]. Interestingly, both Rhipilin-2 from R. hemaphysaloides [ 50 ] and IrSPI from I. ricinus [ 52 ] inhibit elastase but no other enzymes typically targeted by Kunitz-type inhibitors.…”

Section: Modulation Of Host Inflammation and Immunity By Tick Salivar...mentioning

confidence: 99%

Tick Salivary Kunitz-Type Inhibitors: Targeting Host Hemostasis and Immunity to Mediate Successful Blood Feeding

Jmel

Voet

Araújo

et al. 2023

IJMS

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Kunitz domain-containing proteins are ubiquitous serine protease inhibitors with promising therapeutic potential. They target key proteases involved in major cellular processes such as inflammation or hemostasis through competitive inhibition in a substrate-like manner. Protease inhibitors from the Kunitz superfamily have a low molecular weight (18–24 kDa) and are characterized by the presence of one or more Kunitz motifs consisting of α-helices and antiparallel β-sheets stabilized by three disulfide bonds. Kunitz-type inhibitors are an important fraction of the protease inhibitors found in tick saliva. Their roles in inhibiting and/or suppressing host homeostatic responses continue to be shown to be additive or synergistic with other protease inhibitors such as cystatins or serpins, ultimately mediating successful blood feeding for the tick. In this review, we discuss the biochemical features of tick salivary Kunitz-type protease inhibitors. We focus on their various effects on host hemostasis and immunity at the molecular and cellular level and their potential therapeutic applications. In doing so, we highlight that their pharmacological properties can be exploited for the development of novel therapies and vaccines.

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Section: Modulation Of Host Inflammation and Immunity By Tick Salivar...mentioning

confidence: 99%

Tick Salivary Kunitz-Type Inhibitors: Targeting Host Hemostasis and Immunity to Mediate Successful Blood Feeding

Jmel

Voet

Araújo

et al. 2023

IJMS

View full text Add to dashboard Cite

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Review of phage display: A jack-of-all-trades and master of most biomolecule display

Song,

Ch'ng,

Lim

2024

International Journal of Biological Macromolecules

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Identification and functional analysis of a serine protease inhibitor using machine learning strategy

Zhang,

Wu,

Zhu

et al. 2024

International Journal of Biological Macromolecules

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Structural and functional properties of rBmTI-A: A Kunitz-BPTI serine protease inhibitor with therapeutical potential

Cited by 3 publications

References 71 publications

Tick Salivary Kunitz-Type Inhibitors: Targeting Host Hemostasis and Immunity to Mediate Successful Blood Feeding

Tick Salivary Kunitz-Type Inhibitors: Targeting Host Hemostasis and Immunity to Mediate Successful Blood Feeding

Review of phage display: A jack-of-all-trades and master of most biomolecule display

Identification and functional analysis of a serine protease inhibitor using machine learning strategy

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