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Michel Drancourt - One of the best experts on this subject based on the ideXlab platform.
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RNA polymerase β-subunit-based phylogeny of Ehrlichia spp., Anaplasma spp., Neorickettsia spp. and Wolbachia Pipientis
International Journal of Systematic and Evolutionary Microbiology, 2003Co-Authors: Anne-véronique Taillardat-bisch, Michel DrancourtAbstract:Sequence analysis of rpoB, the gene encoding the β-subunit of RNA polymerase, was used in a phylogenetic investigation of nine species from the genera Ehrlichia, Neorickettsia, Wolbachia and Anaplasma. The complete nucleotide sequences obtained for Anaplasma phagocytophilum (HGE agent), Ehrlichia chaffeensis, Neorickettsia sennetsu, Neorickettsia risticii, Anaplasma marginale and Wolbachia Pipientis were amongst the longest rpoB sequences in GenBank and ranged from 4074 bp for N. sennetsu to 4311 bp for W. Pipientis. Additional partial rpoB sequences were obtained for Ehrlichia canis, Ehrlichia ruminantium and Ehrlichia muris. Identical phylogenetic trees were inferred from multiple sequence alignments of the nucleotide sequences and the derived amino acid sequences using either distance, maximum-likelihood or parsimony methods. This study confirms the phylogeny previously inferred from sequence analyses of the 16S rRNA gene, groESL and gltA and allows the confirmation of four monophyletic clades. The rpoB nucleotide sequences were more variable than the 16S rRNA gene and groESL sequences at the species level.
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RNA polymerase beta-subunit-based phylogeny of Ehrlichia spp., Anaplasma spp., Neorickettsia spp. and Wolbachia Pipientis.
International journal of systematic and evolutionary microbiology, 2003Co-Authors: Anne-véronique Taillardat-bisch, Michel DrancourtAbstract:Sequence analysis of rpoB, the gene encoding the beta-subunit of RNA polymerase, was used in a phylogenetic investigation of nine species from the genera Ehrlichia, Neorickettsia, Wolbachia and Anaplasma. The complete nucleotide sequences obtained for Anaplasma phagocytophilum (HGE agent), Ehrlichia chaffeensis, Neorickettsia sennetsu, Neorickettsia risticii, Anaplasma marginale and Wolbachia Pipientis were amongst the longest rpoB sequences in GenBank and ranged from 4074 bp for N. sennetsu to 4311 bp for W. Pipientis. Additional partial rpoB sequences were obtained for Ehrlichia canis, Ehrlichia ruminantium and Ehrlichia muris. Identical phylogenetic trees were inferred from multiple sequence alignments of the nucleotide sequences and the derived amino acid sequences using either distance, maximum-likelihood or parsimony methods. This study confirms the phylogeny previously inferred from sequence analyses of the 16S rRNA gene, groESL and gltA and allows the confirmation of four monophyletic clades. The rpoB nucleotide sequences were more variable than the 16S rRNA gene and groESL sequences at the species level.
Anne-véronique Taillardat-bisch - One of the best experts on this subject based on the ideXlab platform.
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RNA polymerase β-subunit-based phylogeny of Ehrlichia spp., Anaplasma spp., Neorickettsia spp. and Wolbachia Pipientis
International Journal of Systematic and Evolutionary Microbiology, 2003Co-Authors: Anne-véronique Taillardat-bisch, Michel DrancourtAbstract:Sequence analysis of rpoB, the gene encoding the β-subunit of RNA polymerase, was used in a phylogenetic investigation of nine species from the genera Ehrlichia, Neorickettsia, Wolbachia and Anaplasma. The complete nucleotide sequences obtained for Anaplasma phagocytophilum (HGE agent), Ehrlichia chaffeensis, Neorickettsia sennetsu, Neorickettsia risticii, Anaplasma marginale and Wolbachia Pipientis were amongst the longest rpoB sequences in GenBank and ranged from 4074 bp for N. sennetsu to 4311 bp for W. Pipientis. Additional partial rpoB sequences were obtained for Ehrlichia canis, Ehrlichia ruminantium and Ehrlichia muris. Identical phylogenetic trees were inferred from multiple sequence alignments of the nucleotide sequences and the derived amino acid sequences using either distance, maximum-likelihood or parsimony methods. This study confirms the phylogeny previously inferred from sequence analyses of the 16S rRNA gene, groESL and gltA and allows the confirmation of four monophyletic clades. The rpoB nucleotide sequences were more variable than the 16S rRNA gene and groESL sequences at the species level.
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RNA polymerase beta-subunit-based phylogeny of Ehrlichia spp., Anaplasma spp., Neorickettsia spp. and Wolbachia Pipientis.
International journal of systematic and evolutionary microbiology, 2003Co-Authors: Anne-véronique Taillardat-bisch, Michel DrancourtAbstract:Sequence analysis of rpoB, the gene encoding the beta-subunit of RNA polymerase, was used in a phylogenetic investigation of nine species from the genera Ehrlichia, Neorickettsia, Wolbachia and Anaplasma. The complete nucleotide sequences obtained for Anaplasma phagocytophilum (HGE agent), Ehrlichia chaffeensis, Neorickettsia sennetsu, Neorickettsia risticii, Anaplasma marginale and Wolbachia Pipientis were amongst the longest rpoB sequences in GenBank and ranged from 4074 bp for N. sennetsu to 4311 bp for W. Pipientis. Additional partial rpoB sequences were obtained for Ehrlichia canis, Ehrlichia ruminantium and Ehrlichia muris. Identical phylogenetic trees were inferred from multiple sequence alignments of the nucleotide sequences and the derived amino acid sequences using either distance, maximum-likelihood or parsimony methods. This study confirms the phylogeny previously inferred from sequence analyses of the 16S rRNA gene, groESL and gltA and allows the confirmation of four monophyletic clades. The rpoB nucleotide sequences were more variable than the 16S rRNA gene and groESL sequences at the species level.
Jennifer L. Martin - One of the best experts on this subject based on the ideXlab platform.
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The atypical thiol-disulfide exchange protein α-DsbA2 from Wolbachia Pipientis is a homotrimeric disulfide isomerase.
Acta crystallographica. Section D Structural biology, 2019Co-Authors: Patricia M. Walden, Begoña Heras, Gordon J. King, Andrew E. Whitten, Lakshmanane Premkumar, Maria A. Halili, Jennifer L. MartinAbstract:Disulfide-bond-forming (DSB) oxidative folding enzymes are master regulators of virulence that are localized to the periplasm of many Gram-negative bacteria. The archetypal DSB machinery from Escherichia coli K-12 consists of a dithiol-oxidizing redox-relay pair (DsbA/B), a disulfide-isomerizing redox-relay pair (DsbC/D) and the specialist reducing enzymes DsbE and DsbG that also interact with DsbD. By contrast, the Gram-negative bacterium Wolbachia Pipientis encodes just three DSB enzymes. Two of these, α-DsbA1 and α-DsbB, form a redox-relay pair analogous to DsbA/B from E. coli. The third enzyme, α-DsbA2, incorporates a DsbA-like sequence but does not interact with α-DsbB. In comparison to other DsbA enzymes, α-DsbA2 has ∼50 extra N-terminal residues (excluding the signal peptide). The crystal structure of α-DsbA2ΔN, an N-terminally truncated form in which these ∼50 residues are removed, confirms the DsbA-like nature of this domain. However, α-DsbA2 does not have DsbA-like activity: it is structurally and functionally different as a consequence of its N-terminal residues. Firstly, α-DsbA2 is a powerful disulfide isomerase and a poor dithiol oxidase: i.e. its role is to shuffle rather than to introduce disulfide bonds. Moreover, small-angle X-ray scattering (SAXS) of α-DsbA2 reveals a homotrimeric arrangement that differs from those of the other characterized bacterial disulfide isomerases DsbC from Escherichia coli (homodimeric) and ScsC from Proteus mirabilis (PmScsC; homotrimeric with a shape-shifter peptide). α-DsbA2 lacks the shape-shifter motif and SAXS data suggest that it is less flexible than PmScsC. These results allow conclusions to be drawn about the factors that are required for functionally equivalent disulfide isomerase enzymatic activity across structurally diverse protein architectures.
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The atypical thiol–disulfide exchange protein α-DsbA2 from Wolbachia Pipientis is a homotrimeric disulfide isomerase
Acta Crystallographica Section D Structural Biology, 2019Co-Authors: Patricia M. Walden, Begoña Heras, Gordon J. King, Andrew E. Whitten, Lakshmanane Premkumar, Maria A. Halili, Jennifer L. MartinAbstract:Disulfide-bond-forming (DSB) oxidative folding enzymes are master regulators of virulence that are localized to the periplasm of many Gram-negative bacteria. The archetypal DSB machinery from Escherichia coli K-12 consists of a dithiol-oxidizing redox-relay pair (DsbA/B), a disulfide-isomerizing redox-relay pair (DsbC/D) and the specialist reducing enzymes DsbE and DsbG that also interact with DsbD. By contrast, the Gram-negative bacterium Wolbachia Pipientis encodes just three DSB enzymes. Two of these, α-DsbA1 and α-DsbB, form a redox-relay pair analogous to DsbA/B from E. coli. The third enzyme, α-DsbA2, incorporates a DsbA-like sequence but does not interact with α-DsbB. In comparison to other DsbA enzymes, α-DsbA2 has ∼50 extra N-terminal residues (excluding the signal peptide). The crystal structure of α-DsbA2ΔN, an N-terminally truncated form in which these ∼50 residues are removed, confirms the DsbA-like nature of this domain. However, α-DsbA2 does not have DsbA-like activity: it is structurally and functionally different as a consequence of its N-terminal residues. Firstly, α-DsbA2 is a powerful disulfide isomerase and a poor dithiol oxidase: i.e. its role is to shuffle rather than to introduce disulfide bonds. Moreover, small-angle X-ray scattering (SAXS) of α-DsbA2 reveals a homotrimeric arrangement that differs from those of the other characterized bacterial disulfide isomerases DsbC from Escherichia coli (homodimeric) and ScsC from Proteus mirabilis (PmScsC; homotrimeric with a shape-shifter peptide). α-DsbA2 lacks the shape-shifter motif and SAXS data suggest that it is less flexible than PmScsC. These results allow conclusions to be drawn about the factors that are required for functionally equivalent disulfide isomerase enzymatic activity across structurally diverse protein architectures.
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The atypical thiol-disulfide exchange protein α-DsbA2 from Wolbachia Pipientis is a homotrimeric disulfide isomerase
2018Co-Authors: Patricia M. Walden, Begoña Heras, Gordon J. King, Andrew E. Whitten, Lakshmanane Premkumar, Maria A. Halili, Jennifer L. MartinAbstract:DiSulfide Bond (DSB) oxidative folding enzymes are master regulators of virulence localized to the periplasm of many Gram-negative bacteria. The archetypal DSB machinery from Escherichia coli K12 has a dithiol oxidizing redox relay pair (DsbA/B), a disulfide isomerizing redox relay pair (DsbC/D) and specialist reducing enzymes DsbE and DsbG that also interact with DsbD. By contrast the Gram-negative bacterium Wolbachia Pipientis encodes just three DSB enzymes. Two of these alpha-DsbA1 and alpha-DsbB form a redox relay pair analogous to E. coli DsbA/B. The third enzyme alpha-DsbA2 incorporates a DsbA-like sequence but does not interact with alpha-DsbB. In comparison with other DsbA enzymes, alpha-DsbA2 has ~50 extra N-terminal residues. The crystal structure of alpha-DsbA2DeltaN, the N-terminally truncated form in which these residues are removed confirms the DsbA-like nature of this domain. However, alpha-DsbA2 does not have DsbA-like activity: it is structurally and functionally different as a consequence of its N-terminal residues. First, alpha-DsbA2 is a powerful disulfide isomerase and a poor dithiol oxidase, ie its role is to shuffle rather than introduce disulfide bonds. Moreover, small-angle X-ray scattering of alpha-DsbA2 reveals a homotrimeric arrangement. Our results allow us to draw conclusions about the factors required for functionally equivalent enzymatic activity across structurally diverse protein architectures.
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The α-proteobacteria Wolbachia Pipientis protein disulfide machinery has a regulatory mechanism absent in γ-proteobacteria.
PloS one, 2013Co-Authors: Patricia M. Walden, Maria A. Halili, Julia K. Archbold, Fredrik Lindahl, David P. Fairlie, Kenji Inaba, Jennifer L. MartinAbstract:The α-proteobacterium Wolbachia Pipientis infects more than 65% of insect species worldwide and manipulates the host reproductive machinery to enable its own survival. It can live in mutualistic relationships with hosts that cause human disease, including mosquitoes that carry the Dengue virus. Like many other bacteria, Wolbachia contains disulfide bond forming (Dsb) proteins that introduce disulfide bonds into secreted effector proteins. The genome of the Wolbachia strain wMel encodes two DsbA-like proteins sharing just 21% sequence identity to each other, α-DsbA1 and α-DsbA2, and an integral membrane protein, α-DsbB. α-DsbA1 and α-DsbA2 both have a Cys-X-X-Cys active site that, by analogy with Escherichia coli DsbA, would need to be oxidized to the disulfide form to serve as a disulfide bond donor toward substrate proteins. Here we show that the integral membrane protein α-DsbB oxidizes α-DsbA1, but not α-DsbA2. The interaction between α-DsbA1 and α-DsbB is very specific, involving four essential cysteines located in the two periplasmic loops of α-DsbB. In the electron flow cascade, oxidation of α-DsbA1 by α-DsbB is initiated by an oxidizing quinone cofactor that interacts with the cysteine pair in the first periplasmic loop. Oxidizing power is transferred to the second cysteine pair, which directly interacts with α-DsbA1. This reaction is inhibited by a non-catalytic disulfide present in α-DsbA1, conserved in other α-proteobacterial DsbAs but not in γ-proteobacterial DsbAs. This is the first characterization of the integral membrane protein α-DsbB from Wolbachia and reveals that the non-catalytic cysteines of α-DsbA1 regulate the redox relay system in cooperation with α-DsbB.
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Structural and functional characterization of the oxidoreductase alpha-DsbA1 from Wolbachia Pipientis.
Antioxidants & redox signaling, 2009Co-Authors: Mareike Kurz, Scott Leslie O'neill, Inaki Iturbe-ormaetxe, Russell Jarrott, Begoña Heras, Stephen R. Shouldice, Merridee A. Wouters, Patrick Frei, Rudi Glockshuber, Jennifer L. MartinAbstract:The alpha-proteobacterium Wolbachia Pipientis is a highly successful intracellular endosymbiont of invertebrates that manipulates its host's reproductive biology to facilitate its own maternal transmission. The fastidious nature of Wolbachia and the lack of genetic transformation have hampered analysis of the molecular basis of these manipulations. Structure determination of key Wolbachia proteins will enable the development of inhibitors for chemical genetics studies. Wolbachia encodes a homologue (alpha-DsbA1) of the Escherichia coli dithiol oxidase enzyme EcDsbA, essential for the oxidative folding of many exported proteins. We found that the active-site cysteine pair of Wolbachia alpha-DsbA1 has the most reducing redox potential of any characterized DsbA. In addition, Wolbachia alpha-DsbA1 possesses a second disulfide that is highly conserved in alpha-proteobacterial DsbAs but not in other DsbAs. The alpha-DsbA1 structure lacks the characteristic hydrophobic features of EcDsbA, and the protein neither complements EcDsbA deletion mutants in E. coli nor interacts with EcDsbB, the redox partner of EcDsbA. The surface characteristics and redox profile of alpha-DsbA1 indicate that it probably plays a specialized oxidative folding role with a narrow substrate specificity. This first report of a Wolbachia protein structure provides the basis for future chemical genetics studies.
Scott Leslie O'neill - One of the best experts on this subject based on the ideXlab platform.
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Increased locomotor activity and metabolism of Aedes aegypti infected with a life-shortening strain of Wolbachia Pipientis.
Journal of Experimental Biology, 2009Co-Authors: Oliver Evans, Scott Leslie O'neill, Megan Woolfit, Eric P. Caragata, Conor J. Mcmeniman, David C. Green, Craig R. Williams, Craig E. Franklin, Elizabeth A. McgrawAbstract:A virulent strain of the obligate intracellular bacterium Wolbachia Pipientis that shortens insect lifespan has recently been transinfected into the primary mosquito vector of dengue virus, Aedes aegypti L. The microbe's ability to shorten lifespan and spread through host populations under the action of cytoplasmic incompatibility means it has the potential to be used as a biocontrol agent to reduce dengue virus transmission. Wolbachia is present in many host tissues and may have local effects on diverse biological processes. In other insects, Wolbachia infections have been shown to alter locomotor activity and response time to food cues. In mosquitoes, locomotor performance relates to the location of mates, human hosts, resting sites and oviposition sites. We have therefore examined the effect of the virulent, life-shortening Wolbachia strain wMelPop on the locomotion of Ae. aegypti as they age and as the pathogenicity of the infection increases. In parallel experiments we also examined CO(2) production as a proxy for metabolic rate, to investigate a potential mechanistic explanation for any changes in locomotion. Contrary to expectation, we found that the infection increased activity and metabolic rate and that these effects were relatively consistent over the insect's lifespan. The results do not fit a standard model of bacterial pathogenesis in insects, and instead may reveal additional physiological changes induced by infection, such as either increased hunger or defects in the nervous system.
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Structural and functional characterization of the oxidoreductase alpha-DsbA1 from Wolbachia Pipientis.
Antioxidants & redox signaling, 2009Co-Authors: Mareike Kurz, Scott Leslie O'neill, Inaki Iturbe-ormaetxe, Russell Jarrott, Begoña Heras, Stephen R. Shouldice, Merridee A. Wouters, Patrick Frei, Rudi Glockshuber, Jennifer L. MartinAbstract:The alpha-proteobacterium Wolbachia Pipientis is a highly successful intracellular endosymbiont of invertebrates that manipulates its host's reproductive biology to facilitate its own maternal transmission. The fastidious nature of Wolbachia and the lack of genetic transformation have hampered analysis of the molecular basis of these manipulations. Structure determination of key Wolbachia proteins will enable the development of inhibitors for chemical genetics studies. Wolbachia encodes a homologue (alpha-DsbA1) of the Escherichia coli dithiol oxidase enzyme EcDsbA, essential for the oxidative folding of many exported proteins. We found that the active-site cysteine pair of Wolbachia alpha-DsbA1 has the most reducing redox potential of any characterized DsbA. In addition, Wolbachia alpha-DsbA1 possesses a second disulfide that is highly conserved in alpha-proteobacterial DsbAs but not in other DsbAs. The alpha-DsbA1 structure lacks the characteristic hydrophobic features of EcDsbA, and the protein neither complements EcDsbA deletion mutants in E. coli nor interacts with EcDsbB, the redox partner of EcDsbA. The surface characteristics and redox profile of alpha-DsbA1 indicate that it probably plays a specialized oxidative folding role with a narrow substrate specificity. This first report of a Wolbachia protein structure provides the basis for future chemical genetics studies.
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An Ancient Horizontal Gene Transfer between Mosquito and the Endosymbiotic Bacterium Wolbachia Pipientis
Molecular biology and evolution, 2008Co-Authors: Megan Woolfit, Elizabeth A. Mcgraw, Inaki Iturbe-ormaetxe, Scott Leslie O'neillAbstract:The extent and biological relevance of horizontal gene transfer (HGT) in eukaryotic evolution remain highly controversial. Recent studies have demonstrated frequent and large-scale HGT from endosymbiotic bacteria to their hosts, but the great majority of these transferred genes rapidly become nonfunctional in the recipient genome. Here, we investigate an ancient HGT between a host metazoan and an endosymbiotic bacterium, Wolbachia Pipientis. The transferred gene has so far been found only in mosquitoes and Wolbachia. In mosquitoes, it is a member of a gene family encoding candidate receptors required for malaria sporozoite invasion of the mosquito salivary gland. The gene copy in Wolbachia has substantially diverged in sequence from the mosquito homolog, is evolving under purifying selection, and is expressed, suggesting that this gene is also functional in the bacterial genome. Several lines of evidence indicate that the gene may have been transferred from eukaryotic host to bacterial endosymbiont. Regardless of the direction of transfer, however, these results demonstrate that interdomain HGT may give rise to functional, persistent, and possibly evolutionarily significant new genes.
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Cloning, expression, purification and characterization of a DsbA-like protein from Wolbachia Pipientis.
Protein expression and purification, 2008Co-Authors: Mareike Kurz, Inaki Iturbe-ormaetxe, Russell Jarrott, Patrick Frei, Rudi Glockshuber, Nathan Cowieson, Gautier Robin, Alun Jones, Gordon J. King, Scott Leslie O'neillAbstract:Wolbachia Pipientis are obligate endosymbionts that infect a wide range of insect and other arthropod species. They act as reproductive parasites by manipulating the host reproduction machinery to enhance their own transmission. This unusual phenotype is thought to be a consequence of the actions of secreted Wolbachia proteins that are likely to contain disulfide bonds to stabilize the protein structure. In bacteria, the introduction or isomerization of disulfide bonds in proteins is catalyzed by Dsb proteins. The Wolbachia genome encodes two proteins, a-DsbA1 and a-DsbA2, that might catalyze these steps. In this work we focussed on the 234 residue protein a-DsbA1; the gene was cloned and expressed in Escherichia coli, the protein was purified and its identity confirmed by mass spectrometry. The sequence identity of a-DsbA1 for both dithiol oxidants(E. coli DsbA, 12%) and disulfide isomerases(E. coli DsbC, 14%) is similar. We therefore sought to establish whether a-DsbA1 is an oxidant or an isomerase based on functional activity. The purified a-DsbA1 was active in an oxidoreductase assay but had little isomerase activity, indicating that a-DsbA1 is DsbA-like rather than DsbC-like. This work represents the first successful example of the characterization of a recombinant Wolbachia protein. Purified a-DsbA1 will now be used in further functional studies to identify protein substrates that could help explain the molecular basis for the unusual Wolbachia phenotypes, and in structural studies to explore its relationship to other disulfide oxidoreductase proteins. Copyright © 2008 Elsevier Inc
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Crystallization and preliminary diffraction analysis of a DsbA homologue from Wolbachia Pipientis.
Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2008Co-Authors: Mareike Kurz, Scott Leslie O'neill, Inaki Iturbe-ormaetxe, Russell Jarrott, Karl A. Byriel, Jennifer L. Martin, Begoña HerasAbstract:α-DsbA1 is one of two DsbA homologues encoded by the Gram-negative α-proteobacterium Wolbachia Pipientis, an endosymbiont that can behave as a reproductive parasite in insects and as a mutualist in medically important filarial nematodes. The α-DsbA1 protein is thought to be important for the folding and secretion of Wolbachia proteins involved in the induction of reproductive distortions. Crystals of native and SeMet α-DsbA1 were grown by vapour diffusion and belong to the monoclinic space group C2, with unit-cell parameters a = 71.4, b = 49.5, c = 69.3 A, β = 107.0° and one molecule in the asymmetric unit (44% solvent content). X-ray data were recorded from native crystals to a resolution of 2.01 A using a copper anode and data from SeMet α-DsbA1 crystals were recorded to 2.45 A resolution using a chromium anode.
Kasem Kulkeaw - One of the best experts on this subject based on the ideXlab platform.
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Molecular identification of native Wolbachia Pipientis in Anopheles minimus in a low-malaria transmission area of Umphang Valley along the Thailand-Myanmar border.
Parasites & vectors, 2020Co-Authors: Nongnat Tongkrajang, Pichet Ruenchit, Chatchai Tananchai, Theeraphap Chareonviriyaphap, Kasem KulkeawAbstract:Wolbachia, obligate intracellular bacteria, infect the majority of arthropods, including many mosquito species of medical importance. Some Wolbachia strains interfere with the development of Plasmodium parasites in female Anopheles, a major vector of malaria. The use of Wolbachia as a means to block malaria transmission is an emerging vector control strategy in highly endemic areas. Hence, identification of native Wolbachia strains in areas where malaria transmission is low may uncover a particular Wolbachia strain capable of Plasmodium interference. This study aims to identify native Wolbachia strains in female Anopheles spp. that are predominant in a low-malaria transmission area in mainland Southeast Asia. Following a 2-year survey of malaria vectors in Umphang Valley of Tak Province, Thailand, DNA extracts of female An. minimus, An. peditaeniatus, and An. maculatus were subjected to amplification of the conserved region of the 16S rRNA-encoding gene. The DNA sequences of the amplicons were phylogenetically compared with those of known Wolbachia strains. Among three Anopheles spp., amplification was detected in only the DNA samples from An. minimus. The DNA sequencing of amplicons revealed 100% similarity to Wolbachia Pipientis, confirming the specificity of amplification. The Wolbachia-positive An. minimus samples were devoid of Plasmodium 18S rRNA amplification. The phylogenetic trees indicate a close relationship with Wolbachia strains in subgroup B. To the best of our knowledge, the data presented herein provide the first molecular evidence of a Wolbachia strain in An. minimus, hereinafter named wAnmi, in a low-malaria transmission area in the Umphang Valley of western Thailand. Further biological characterization is required to examine its potential for malaria transmission control in the field.
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Molecular Identification of Native Wolbachia Pipientis in Anopheles Minimus in a Low-Malaria Transmission Area of Umphang Valley Along the Thailand-Myanmar Border
2020Co-Authors: Nongnat Tongkrajang, Pichet Ruenchit, Chatchai Tananchai, Theeraphap Chareonviriyaphap, Kasem KulkeawAbstract:Abstract BackgroundWolbachia, obligate intracellular bacteria, infect the majority of arthropods, including many mosquito species of medical importance. Some Wolbachia strains interfere with the development of Plasmodium parasites in female Anopheles, a major vector of malaria. The use of Wolbachia as a means to block malaria transmission is an emerging vector control strategy in highly endemic areas. Hence, identification of native Wolbachia strains in areas where malaria transmission is low may uncover a particular Wolbachia strain capable of Plasmodium interference. This study aims to identify native Wolbachia strains in female Anopheles spp. that are predominant in a low-malaria transmission area in mainland Southeast Asia.MethodsFollowing a two-year survey of malaria vectors in Umphang Valley of Tak Province, Thailand, DNA extracts of female An. minimus, An. peditaeniatus, An. maculatus, and An. dirus were subjected to amplification of the conserved region of the 16S rRNA-encoding gene. The DNA sequences of the amplicons were phylogenetically compared with those of known Wolbachia strains.ResultsAmong four Anopheles spp., amplification was detected in only the DNA samples from An. minimus. The DNA sequencing of amplicons revealed 100% similarity to Wolbachia Pipientis, confirming the specificity of amplification. The phylogenetic trees indicate a close relationship with Wolbachia strains in subgroup B.ConclusionTo the best of our knowledge, the data presented herein provide the first molecular evidence of a Wolbachia strain in An. minimus, hereinafter named wAnmi, in a low-malaria transmission area in the Umphang Valley of western Thailand. Further biological characterization is required to examine its potential for malaria transmission control in the field.
