Structural dynamics of <i>Rhipicephalus microplus</i> serpin-3

Pongprayoon, Prapasiri; Kaewhom, Paitoon; Kaewmongkol, Sarawan; Suwan, Eukote; Stich, Roger W.; Wiriya, Benjamaporn; Jittapalapong, Sathaporn

doi:10.1080/08927022.2021.1962011

Cited by 4 publications

(5 citation statements)

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“…, 2020; Pongprayoon et al. , 2021). However, the majority of serpins have not yet been evaluated in vaccination trials, highlighting the need for further investigation to advance vaccine development.…”

Section: Discussionmentioning

confidence: 99%

“…Rabbits developed anti-tick immunity after recombinant Iris protein injection, as indicated by higher mortality and lower weight gain in tick nymphs, whereas adult females experienced longer feeding periods and higher mortality rates (Prevot et al, 2007). Several functionally characterized tick serpins, including RmS-3 and AAS41, have been suggested as potential vaccine candidates (Kim et al, 2020;Pongprayoon et al, 2021). However, the majority of serpins have not yet been evaluated in vaccination trials, highlighting the need for further investigation to advance vaccine development.…”

Section: Discussionmentioning

confidence: 99%

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Targeting Haemaphysalis longicornis serpin to prevent tick feeding and pathogen transmission

Feng,

Tong,

Zhang

et al. 2023

Insect Science

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Serine proteinase inhibitors (serpins), identified from the hard tick Haemaphysalis longicornis of China, play significant roles in various animal physiological processes. In this study, we showed that H. longicornis serpins (Hlserpin‐a and Hlserpin‐b) were induced during blood‐feeding in nymph ticks and exhibited anticoagulation activity in vitro. Silencing Hlserpins through RNA interference (RNAi) significantly impaired tick feeding. Immunization of mice with recombinant Hlserpins or passive transfer of Hlserpin antiserum significantly curtails the efficacy of tick feeding. Concurrently, the transmission of the Langat virus (LGTV) from ticks to mice witnessed a substantial decrease when Hlserpins were silenced. Our findings suggest that inhibiting Hlserpins can hamper tick engorgement and pathogen transmission, indicating the potential of Hlserpins as a vaccine to counter tick‐borne diseases.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Targeting Haemaphysalis longicornis serpin to prevent tick feeding and pathogen transmission

Feng,

Tong,

Zhang

et al. 2023

Insect Science

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“…Another elastase inhibitor from I. ricinus is Iripin-5, which affects neutrophil migration, decreases nitric oxide production by macrophages, and modifies complement function, thus exhibiting potent anti-inflammatory activity ( Kascakova et al., 2021 ). Anti-elastase activity was described for the other two tick serpins, namely AamS6 and RmS-3 ( Chalaire et al., 2011 ; Syrovets et al., 2012 ; Mulenga et al., 2013 ; Pongprayoon et al., 2021 ).…”

Section: The Importance Of Tick Salivary Serpins In Tick-host Interac...mentioning

confidence: 99%

“…administered recombinant Iris protein into mice and rabbits, but only rabbits developed anti-tick immunity as evidenced by higher mortality and lower weight gain in nymphs and by a prolonged feeding period and a higher mortality rate in adult females ( Prevot et al., 2007 ). Most of the functionally characterized tick serpins, such as RmS-3, AAS41, and others, have been suggested as prospective vaccine candidates ( Kim et al., 2020 ; Pongprayoon et al., 2021 ). However, the majority of these serpins have not been evaluated in vaccination experiments (see Table 1 ).…”

Section: Tick Serpins As Epitopes For Anti-tick Vaccine Developmentmentioning

confidence: 99%

Serpins in Tick Physiology and Tick-Host Interaction

Abbas

Chlastáková

Jmel

et al. 2022

Front. Cell. Infect. Microbiol.

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Tick saliva has been extensively studied in the context of tick-host interactions because it is involved in host homeostasis modulation and microbial pathogen transmission to the host. Accumulated knowledge about the tick saliva composition at the molecular level has revealed that serine protease inhibitors play a key role in the tick-host interaction. Serpins are one highly expressed group of protease inhibitors in tick salivary glands, their expression can be induced during tick blood-feeding, and they have many biological functions at the tick-host interface. Indeed, tick serpins have an important role in inhibiting host hemostatic processes and in the modulation of the innate and adaptive immune responses of their vertebrate hosts. Tick serpins have also been studied as potential candidates for therapeutic use and vaccine development. In this review, we critically summarize the current state of knowledge about the biological role of tick serpins in shaping tick-host interactions with emphasis on the mechanisms by which they modulate host immunity. Their potential use in drug and vaccine development is also discussed.

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“…To obtain molecular insights, molecular dynamics (MD) simulations were performed. MD simulations have been successfully used to reveal the behaviors of other tick proteins [ 33 , 34 , 35 ]. The key interactions for GSH and GTX binding are extracted here.…”

Section: Introductionmentioning

confidence: 99%

Observing How Glutathione and S-Hexyl Glutathione Bind to Glutathione S-Transferase from Rhipicephalus (Boophilus) microplus

Rangubpit

Suwan

Sangthong

et al. 2022

IJMS

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Rhipicephalus (Boophilus) microplus is one of the most widespread ticks causing a massive loss to livestock production. The long-term use of acaracides rapidly develops acaracide resistance. In R. microplus, enhancing the metabolic activity of glutathione S-transferase (RmGST) is one of the mechanisms underlying acaracide resistance. RmGST catalyzes the conjugation of glutathione (GSH) to insecticides causing an easy-to-excrete conjugate. The active RmGST dimer contains two active sites (hydrophobic co-substrate binding site (H-site) and GSH binding site (G-site)) in each monomer. To preserve the insecticide efficacy, s-hexyl glutathione (GTX), a GST inhibitor, has been used as a synergist. To date, no molecular information on the RmGST-GSH/GTX complex is available. The insight is important for developing a novel RmGST inhibitor. Therefore, in this work, molecular dynamics simulations (MD) were performed to explore the binding of GTX and GSH to RmGST. GSH binds tighter and sits rigidly inside the G-site, while flexible GTX occupies both active sites. In GSH, the backbone mainly interacts with W8, R43, W46, K50, N59, L60, Q72, and S73, while its thiol group directs to Y7. In contrast, the aliphatic hexyl of GTX protrudes into the H-site and allows a flexible peptide core to form various interactions. Such high GTX flexibility and the protrusion of its hexyl moiety to the H-site suggest the dual role of GTX in preventing the conjugation reaction and the binding of acaracide. This insight can provide a better understanding of an important insecticide-resistance mechanism, which may in turn facilitate the development of novel approaches to tick control.

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Structural dynamics of Rhipicephalus microplus serpin-3

Cited by 4 publications

References 47 publications

Targeting Haemaphysalis longicornis serpin to prevent tick feeding and pathogen transmission

Targeting Haemaphysalis longicornis serpin to prevent tick feeding and pathogen transmission

Serpins in Tick Physiology and Tick-Host Interaction

Observing How Glutathione and S-Hexyl Glutathione Bind to Glutathione S-Transferase from Rhipicephalus (Boophilus) microplus

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