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Special Issue "Molecular Biology of Disease Vectors"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Microbiology".

Deadline for manuscript submissions: 31 December 2021.

Special Issue Editor

Dr. Michail Kotsyfakis
E-Mail Website1 Website2
Guest Editor
Institute of Parasitology, Biology Center of the Czech Academy of Sciences, 37005, Budweis (Ceske Budejovice), Czech Republic
Interests: biology of disease vectors; ectoparasite/host interaction; protease inhibitors; cystatin; arthropod; transcriptomics; proteomics; arthropod saliva; immunomodulation; hemostasis

Special Issue Information

Dear Colleagues,

Arthropod disease vectors transmit not only serious diseases like malaria, but many other diseases as well, many of which are neglected to various extents. In most cases, a tripartite interaction is involved between the arthropod disease vector, the vertebrate host, and the vector-borne pathogens. The aim of this Special issue is to collect the latest data (and up to date information in the case of reviews) about the molecular and biochemical events that mediate this tripartite interaction. The contribution of data (coming for example from systems biology and molecular biology/biochemical approaches or reviews) is anticipated to improve our knowledge of the biology of any of the three key partners involved in vector-borne disease transmission, and/or of their intimate interactions. Specific subtopics to be included in this Special issue, but our interest is not limited to these subtopics, are the following: disease vector–vertebrate host interactions, vector-borne pathogen interactions with the disease vector and the vertebrate host, molecular biology/microbiology of arthropod-borne pathogens, vertebrate host response to arthropod-borne pathogens, and molecular biology of disease vectors (e.g. arthropod immunity, blood meal digestion, oogenesis/reproduction, olfaction and other sensory cues, and insecticide resistance).

Dr. Michail Kotsyfakis
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • disease vector biology
  • arthropod
  • vector-borne disease
  • hematophagy
  • immune response to vector-borne pathogens
  • arthropod immunity
  • disease vector–pathogen interaction
  • disease vector–vertebrate host interactions
  • disease transmission
  • disease vector development
  • insecticide resistance 

Published Papers (5 papers)

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Research

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Article
Aedes aegypti Piwi4 Structural Features Are Necessary for RNA Binding and Nuclear Localization
Int. J. Mol. Sci. 2021, 22(23), 12733; https://doi.org/10.3390/ijms222312733 - 25 Nov 2021
Viewed by 342
Abstract
The PIWI-interacting RNA (piRNA) pathway provides an RNA interference (RNAi) mechanism known from Drosophila studies to maintain the integrity of the germline genome by silencing transposable elements (TE). Aedes aegypti mosquitoes, which are the key vectors of several arthropod-borne viruses, exhibit an expanded [...] Read more.
The PIWI-interacting RNA (piRNA) pathway provides an RNA interference (RNAi) mechanism known from Drosophila studies to maintain the integrity of the germline genome by silencing transposable elements (TE). Aedes aegypti mosquitoes, which are the key vectors of several arthropod-borne viruses, exhibit an expanded repertoire of Piwi proteins involved in the piRNA pathway, suggesting functional divergence. Here, we investigate RNA-binding dynamics and subcellular localization of A. aegypti Piwi4 (AePiwi4), a Piwi protein involved in antiviral immunity and embryonic development, to better understand its function. We found that AePiwi4 PAZ (Piwi/Argonaute/Zwille), the domain that binds the 3′ ends of piRNAs, bound to mature (3′ 2′ O-methylated) and unmethylated RNAs with similar micromolar affinities (KD = 1.7 ± 0.8 μM and KD of 5.0 ± 2.2 μM, respectively; p = 0.05) in a sequence independent manner. Through site-directed mutagenesis studies, we identified highly conserved residues involved in RNA binding and found that subtle changes in the amino acids flanking the binding pocket across PAZ proteins have significant impacts on binding behaviors, likely by impacting the protein secondary structure. We also analyzed AePiwi4 subcellular localization in mosquito tissues. We found that the protein is both cytoplasmic and nuclear, and we identified an AePiwi4 nuclear localization signal (NLS) in the N-terminal region of the protein. Taken together, these studies provide insights on the dynamic role of AePiwi4 in RNAi and pave the way for future studies aimed at understanding Piwi interactions with diverse RNA populations. Full article
(This article belongs to the Special Issue Molecular Biology of Disease Vectors)
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Article
Ixodes ricinus Salivary Serpin Iripin-8 Inhibits the Intrinsic Pathway of Coagulation and Complement
Int. J. Mol. Sci. 2021, 22(17), 9480; https://doi.org/10.3390/ijms22179480 - 31 Aug 2021
Cited by 2 | Viewed by 543
Abstract
Tick saliva is a rich source of antihemostatic, anti-inflammatory, and immunomodulatory molecules that actively help the tick to finish its blood meal. Moreover, these molecules facilitate the transmission of tick-borne pathogens. Here we present the functional and structural characterization of Iripin-8, a salivary [...] Read more.
Tick saliva is a rich source of antihemostatic, anti-inflammatory, and immunomodulatory molecules that actively help the tick to finish its blood meal. Moreover, these molecules facilitate the transmission of tick-borne pathogens. Here we present the functional and structural characterization of Iripin-8, a salivary serpin from the tick Ixodes ricinus, a European vector of tick-borne encephalitis and Lyme disease. Iripin-8 displayed blood-meal-induced mRNA expression that peaked in nymphs and the salivary glands of adult females. Iripin-8 inhibited multiple proteases involved in blood coagulation and blocked the intrinsic and common pathways of the coagulation cascade in vitro. Moreover, Iripin-8 inhibited erythrocyte lysis by complement, and Iripin-8 knockdown by RNA interference in tick nymphs delayed the feeding time. Finally, we resolved the crystal structure of Iripin-8 at 1.89 Å resolution to reveal an unusually long and rigid reactive center loop that is conserved in several tick species. The P1 Arg residue is held in place distant from the serpin body by a conserved poly-Pro element on the P′ side. Several PEG molecules bind to Iripin-8, including one in a deep cavity, perhaps indicating the presence of a small-molecule binding site. This is the first crystal structure of a tick serpin in the native state, and Iripin-8 is a tick serpin with a conserved reactive center loop that possesses antihemostatic activity that may mediate interference with host innate immunity. Full article
(This article belongs to the Special Issue Molecular Biology of Disease Vectors)
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Article
Mialostatin, a Novel Midgut Cystatin from Ixodes ricinus Ticks: Crystal Structure and Regulation of Host Blood Digestion
Int. J. Mol. Sci. 2021, 22(10), 5371; https://doi.org/10.3390/ijms22105371 - 20 May 2021
Viewed by 736
Abstract
The hard tick Ixodes ricinus is a vector of Lyme disease and tick-borne encephalitis. Host blood protein digestion, essential for tick development and reproduction, occurs in tick midgut digestive cells driven by cathepsin proteases. Little is known about the regulation of the digestive [...] Read more.
The hard tick Ixodes ricinus is a vector of Lyme disease and tick-borne encephalitis. Host blood protein digestion, essential for tick development and reproduction, occurs in tick midgut digestive cells driven by cathepsin proteases. Little is known about the regulation of the digestive proteolytic machinery of I. ricinus. Here we characterize a novel cystatin-type protease inhibitor, mialostatin, from the I. ricinus midgut. Blood feeding rapidly induced mialostatin expression in the gut, which continued after tick detachment. Recombinant mialostatin inhibited a number of I. ricinus digestive cysteine cathepsins, with the greatest potency observed against cathepsin L isoforms, with which it co-localized in midgut digestive cells. The crystal structure of mialostatin was determined at 1.55 Å to explain its unique inhibitory specificity. Finally, mialostatin effectively blocked in vitro proteolysis of blood proteins by midgut cysteine cathepsins. Mialostatin is likely to be involved in the regulation of gut-associated proteolytic pathways, making midgut cystatins promising targets for tick control strategies. Full article
(This article belongs to the Special Issue Molecular Biology of Disease Vectors)
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Review

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Review
Arboviruses: How Saliva Impacts the Journey from Vector to Host
Int. J. Mol. Sci. 2021, 22(17), 9173; https://doi.org/10.3390/ijms22179173 - 25 Aug 2021
Viewed by 540
Abstract
Arthropod-borne viruses, referred to collectively as arboviruses, infect millions of people worldwide each year and have the potential to cause severe disease. They are predominately transmitted to humans through blood-feeding behavior of three main groups of biting arthropods: ticks, mosquitoes, and sandflies. The [...] Read more.
Arthropod-borne viruses, referred to collectively as arboviruses, infect millions of people worldwide each year and have the potential to cause severe disease. They are predominately transmitted to humans through blood-feeding behavior of three main groups of biting arthropods: ticks, mosquitoes, and sandflies. The pathogens harbored by these blood-feeding arthropods (BFA) are transferred to animal hosts through deposition of virus-rich saliva into the skin. Sometimes these infections become systemic and can lead to neuro-invasion and life-threatening viral encephalitis. Factors intrinsic to the arboviral vectors can greatly influence the pathogenicity and virulence of infections, with mounting evidence that BFA saliva and salivary proteins can shift the trajectory of viral infection in the host. This review provides an overview of arbovirus infection and ways in which vectors influence viral pathogenesis. In particular, we focus on how saliva and salivary gland extracts from the three dominant arbovirus vectors impact the trajectory of the cellular immune response to arbovirus infection in the skin. Full article
(This article belongs to the Special Issue Molecular Biology of Disease Vectors)
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Other

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Addendum
Addendum: Kotál et al. Ixodes ricinus Salivary Serpin Iripin-8 Inhibits the Intrinsic Pathway of Coagulation and Complement. Int. J. Mol. Sci. 2021, 22, 9480
Int. J. Mol. Sci. 2021, 22(20), 11271; https://doi.org/10.3390/ijms222011271 - 19 Oct 2021
Viewed by 203
Abstract
The accession code will be added in Section 2 [...] Full article
(This article belongs to the Special Issue Molecular Biology of Disease Vectors)
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