Pub Date : 2026-01-27DOI: 10.1016/j.molbiopara.2026.111735
Wallyson André dos Santos Bezerra , Claudia Quintino da Rocha , Itabajara da Silva Vaz Junior , Shafi Ullah , Walter Filgueira de Azevedo Junior , Alexandra Martins dos Santos Soares
Ticks are widely distributed ectoparasites that transmit several pathogens and cause significant losses in livestock production. Resistance to commercial acaricides has become increasingly common, stimulating the search for new molecules with potential for tick control. Among possible targets, glutathione S-transferases (GSTs) play a central role in detoxification processes and are therefore attractive candidates for overcoming acaricide resistance. In this work, the inhibitory activity of plant compounds on recombinant GSTs from Rhipicephalus microplus (rGST-Rm) and R. decoloratus (rGST-Rd) was examined using in vitro and in silico approaches. Compounds tested included 3β-stearioxy-olean-12-ene, diosgenin, quercitrin, naringenin, ellagic acid, rutin, and quercetin, which belong to different chemical classes, including triterpenes, steroids, polyphenols, and flavonoids. In vitro assays showed that 3β-stearioxy-olean-12-ene and naringenin inhibited rGST-Rm with IC₅₀ values of 148.2 μM and 160.7 μM, respectively. For rGST-Rd, inhibition by quercitrin (IC₅₀ = 37.7 μM), naringenin (IC₅₀ = 177.7 μM), and rutin (IC₅₀ = 115.0 μM) was observed. Docking analyses predicted interactions between these molecules and tick GSTs. Overall, the results support the potential of GST inhibition as a strategy for acaricide development and indicate that some plant compounds may serve as starting points for future tick control methods.
{"title":"In vitro and in silico evaluation of plant compounds as inhibitors of glutathione S-transferase from Rhipicephalus microplus and R. decoloratus","authors":"Wallyson André dos Santos Bezerra , Claudia Quintino da Rocha , Itabajara da Silva Vaz Junior , Shafi Ullah , Walter Filgueira de Azevedo Junior , Alexandra Martins dos Santos Soares","doi":"10.1016/j.molbiopara.2026.111735","DOIUrl":"10.1016/j.molbiopara.2026.111735","url":null,"abstract":"<div><div>Ticks are widely distributed ectoparasites that transmit several pathogens and cause significant losses in livestock production. Resistance to commercial acaricides has become increasingly common, stimulating the search for new molecules with potential for tick control. Among possible targets, glutathione S-transferases (GSTs) play a central role in detoxification processes and are therefore attractive candidates for overcoming acaricide resistance. In this work, the inhibitory activity of plant compounds on recombinant GSTs from <em>Rhipicephalus microplus</em> (rGST-Rm) and <em>R. decoloratus</em> (rGST-Rd) was examined using <em>in vitro</em> and <em>in silico</em> approaches. Compounds tested included 3β-stearioxy-olean-12-ene, diosgenin, quercitrin, naringenin, ellagic acid, rutin, and quercetin, which belong to different chemical classes, including triterpenes, steroids, polyphenols, and flavonoids. <em>In vitro</em> assays showed that 3β-stearioxy-olean-12-ene and naringenin inhibited rGST-Rm with IC₅₀ values of 148.2 μM and 160.7 μM, respectively. For rGST-Rd, inhibition by quercitrin (IC₅₀ = 37.7 μM), naringenin (IC₅₀ = 177.7 μM), and rutin (IC₅₀ = 115.0 μM) was observed. Docking analyses predicted interactions between these molecules and tick GSTs. Overall, the results support the potential of GST inhibition as a strategy for acaricide development and indicate that some plant compounds may serve as starting points for future tick control methods.</div></div>","PeriodicalId":18721,"journal":{"name":"Molecular and biochemical parasitology","volume":"266 ","pages":"Article 111735"},"PeriodicalIF":1.5,"publicationDate":"2026-01-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146081180","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-24DOI: 10.1016/j.molbiopara.2026.111733
Sidhant Jain
The relationship between the liver fluke, Opisthorchis felineus (Of) and cholangiocarcinoma (CCA) has been assessed by a limited number of studies. In the case of animal models, such studies have pointed towards a causal association between Of infection and CCA. As per these studies, Of has the ability to interfere with DNA excision repair systems through the generation of reactive oxygen and nitrogen species. It can also cause accumulation of by-products generated via lipid peroxidation and is also involved in the production of oxysterol like compounds, hence possess the ability to mutate different genes. Although chalangiocarcinogenis through Of infection in humans is not established, but hospital based studies, case studies and case-controlled studies as well as the analysis of medical statistics, especially from Russian Federation, point towards a strong correlation between them. The aim of this work is to present the current understanding of the association between Of and CCA. On the basis of available studies, this work identifies an array of factors linked with Of infection, which have been independently identified as cancer inducers in various other studies. These factors point towards a possible causative link between Of infection and CCA induction in humans but this observation warrants for more epidemiological, clinical and pathological studies to conclusively state Of to be a CCA inducer in humans. However, Of infection, which is currently placed in group 3 of IARC classification for CCA should be re-classified to a higher group of cancer inducers.
{"title":"Exploring the potential role of Opisthorchis felineus infection in cholangiocarcinogenesis","authors":"Sidhant Jain","doi":"10.1016/j.molbiopara.2026.111733","DOIUrl":"10.1016/j.molbiopara.2026.111733","url":null,"abstract":"<div><div>The relationship between the liver fluke, <em>Opisthorchis felineus</em> (Of) and cholangiocarcinoma (CCA) has been assessed by a limited number of studies. In the case of animal models, such studies have pointed towards a causal association between Of infection and CCA. As per these studies, Of has the ability to interfere with DNA excision repair systems through the generation of reactive oxygen and nitrogen species. It can also cause accumulation of by-products generated via lipid peroxidation and is also involved in the production of oxysterol like compounds, hence possess the ability to mutate different genes. Although chalangiocarcinogenis through Of infection in humans is not established, but hospital based studies, case studies and case-controlled studies as well as the analysis of medical statistics, especially from Russian Federation, point towards a strong correlation between them. The aim of this work is to present the current understanding of the association between Of and CCA. On the basis of available studies, this work identifies an array of factors linked with Of infection, which have been independently identified as cancer inducers in various other studies. These factors point towards a possible causative link between Of infection and CCA induction in humans but this observation warrants for more epidemiological, clinical and pathological studies to conclusively state Of to be a CCA inducer in humans. However, Of infection, which is currently placed in group 3 of IARC classification for CCA should be re-classified to a higher group of cancer inducers.</div></div>","PeriodicalId":18721,"journal":{"name":"Molecular and biochemical parasitology","volume":"266 ","pages":"Article 111733"},"PeriodicalIF":1.5,"publicationDate":"2026-01-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146053155","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-23DOI: 10.1016/j.molbiopara.2026.111732
PKK Mishra , P. Joshi
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an enzyme involved in glycolysis. However, non-glycolytic activities of this enzyme were subsequently discovered including DNA repair, cell death, membrane fusion and transport. Recent studies have identified additional functions of this enzyme in parasites such as modulating host immune responses. For example, Haemonchus contortus GAPDH binds to complement C3 and also interacts with peripheral blood mononuclear cells. The enzyme from Leishmania major inhibits TNF-α production in host macrophages. Further, GAPDH of Schistosoma bovis, Dirofilaria immitis and Babesia microti binds to plasminogen that may facilitate parasite migration by preventing clot formation in its vicinity. Trichomonas vaginalis GAPDH interacts with many extracellular matrix proteins that may support initial adhesion of the organism to the host tissues. Surface associated GAPDH of Plasmodium berghei interacts with CD68 of Kupffer cells; a prerequisite for hepatocyte infection. This review discusses the general features of the enzyme and its significance in host-parasite relationships.
{"title":"Multifunctional glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of parasites","authors":"PKK Mishra , P. Joshi","doi":"10.1016/j.molbiopara.2026.111732","DOIUrl":"10.1016/j.molbiopara.2026.111732","url":null,"abstract":"<div><div>Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an enzyme involved in glycolysis. However, non-glycolytic activities of this enzyme were subsequently discovered including DNA repair, cell death, membrane fusion and transport. Recent studies have identified additional functions of this enzyme in parasites such as modulating host immune responses. For example, <em>Haemonchus contortus</em> GAPDH binds to complement C3 and also interacts with peripheral blood mononuclear cells. The enzyme from <em>Leishmania major</em> inhibits TNF-α production in host macrophages. Further, GAPDH of <em>Schistosoma bovis</em>, <em>Dirofilaria immitis</em> and <em>Babesia microti</em> binds to plasminogen that may facilitate parasite migration by preventing clot formation in its vicinity. <em>Trichomonas vaginalis</em> GAPDH interacts with many extracellular matrix proteins that may support initial adhesion of the organism to the host tissues. Surface associated GAPDH of <em>Plasmodium berghei</em> interacts with CD68 of Kupffer cells; a prerequisite for hepatocyte infection. This review discusses the general features of the enzyme and its significance in host-parasite relationships.</div></div>","PeriodicalId":18721,"journal":{"name":"Molecular and biochemical parasitology","volume":"266 ","pages":"Article 111732"},"PeriodicalIF":1.5,"publicationDate":"2026-01-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146037123","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
The digenean Clinostomum piscidium collected from the banded gourami (Trichogaster fasciata Bloch and Schneider, 1801) in India was morphologically identified, and the mitogenome was sequenced. Our results demonstrate that the parasite mitogenome is 14,318 bp long and consists of 12 protein-coding genes, 22 tRNA genes, two rRNA genes, and two non-coding control regions. Nucleotide skewness of the mt genome did not differ so much from other congeners. To date, the complete mitochondrial (mt) genome is available for only two Clinostomum species, Clinostomum complanatum and Clinostomum sinensis. Clinostomum piscidium exhibits a similar reorganization of the genome in comparison to all other sequenced Clinostomum species mt genomes except for the NCRs. The non-coding regions, the short NCR (SNCR) and long NCR (LNCR) are present and located between trnE and trnG and nad5 and trnE, respectively, in the C. piscidium genome. This is the first report on the mitogenome of Clinostomum sp. from India. The results provide data for further studies of the taxonomy and systematics of Clinostomum spp. It also advances Clinostomum mitochondrial genome resources, and thus offers imperative insights into the taxonomy and species identification of this genus.
{"title":"The first mitochondrial genome sequence and phylogenetic analysis of Clinostomum piscidium (Platyhelminthes: Clinostomidae): A first representative from India","authors":"Anshu Chaudhary , Dipannita Ghosh , Agnik Haldar , Ganga Narasimhan , Rakhi Baliyan , Suhani Singh , Bindu Sharma , Hridaya Shanker Singh","doi":"10.1016/j.molbiopara.2026.111731","DOIUrl":"10.1016/j.molbiopara.2026.111731","url":null,"abstract":"<div><div>The digenean <em>Clinostomum piscidium</em> collected from the banded gourami (<em>Trichogaster fasciata</em> Bloch and Schneider, 1801) in India was morphologically identified, and the mitogenome was sequenced. Our results demonstrate that the parasite mitogenome is 14,318 bp long and consists of 12 protein-coding genes, 22 tRNA genes, two rRNA genes, and two non-coding control regions. Nucleotide skewness of the mt genome did not differ so much from other congeners. To date, the complete mitochondrial (mt) genome is available for only two <em>Clinostomum</em> species, <em>Clinostomum complanatum</em> and <em>Clinostomum sinensis</em>. <em>Clinostomum piscidium</em> exhibits a similar reorganization of the genome in comparison to all other sequenced <em>Clinostomum</em> species mt genomes except for the NCRs. The non-coding regions, the short NCR (SNCR) and long NCR (LNCR) are present and located between trnE and trnG and nad5 and trnE, respectively, in the <em>C. piscidium</em> genome. This is the first report on the mitogenome of <em>Clinostomum</em> sp. from India. The results provide data for further studies of the taxonomy and systematics of <em>Clinostomum</em> spp. It also advances <em>Clinostomum</em> mitochondrial genome resources, and thus offers imperative insights into the taxonomy and species identification of this genus.</div></div>","PeriodicalId":18721,"journal":{"name":"Molecular and biochemical parasitology","volume":"266 ","pages":"Article 111731"},"PeriodicalIF":1.5,"publicationDate":"2026-01-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146046880","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-23DOI: 10.1016/j.molbiopara.2026.111734
Jennifer Nichols, Sean G. Forrester
Dirofilaria immitis is a parasitic nematode responsible for canine heartworm disease. Current heartworm treatment options include melarsomine chloridrate (an arsenical) to treat adult parasites and the macrocyclic lactones. Unfortunately, resistance to macrocyclic lactones is emerging which is highlighting the need for the discovery of new anthelmintics. Cys-loop ligand-gated ion channels are an untapped source for novel drug targets essential for nematode neurotransmission. This work presents the isolation and preliminary pharmacological characterization of a glutamate-gated chloride channel, GLC-2, from D. immitis. Expression levels of GLC-2, identified in the adult female, adult male and microfilaria (Mf) life stages, were measured via qPCR, with highest expression found in the adult stages. Dim-GLC-2 forms homomeric channels with low sensitivity to monosodium L-glutamate (MSG) and L-glutamic acid. Homodimer models were created to visualize docking of glutamate to the binding site, and several potential interactions were identified and compared to the original crystal structure of the glutamate-gated chloride channel from Caenorhabditis elegans.
{"title":"Isolation and characterization of a novel glutamate-gated chloride channel subunit (GLC-2) from the canine heartworm Dirofilaria immitis","authors":"Jennifer Nichols, Sean G. Forrester","doi":"10.1016/j.molbiopara.2026.111734","DOIUrl":"10.1016/j.molbiopara.2026.111734","url":null,"abstract":"<div><div><em>Dirofilaria immitis</em> is a parasitic nematode responsible for canine heartworm disease. Current heartworm treatment options include melarsomine chloridrate (an arsenical) to treat adult parasites and the macrocyclic lactones. Unfortunately, resistance to macrocyclic lactones is emerging which is highlighting the need for the discovery of new anthelmintics. Cys-loop ligand-gated ion channels are an untapped source for novel drug targets essential for nematode neurotransmission. This work presents the isolation and preliminary pharmacological characterization of a glutamate-gated chloride channel, GLC-2, from <em>D. immitis.</em> Expression levels of GLC-2, identified in the adult female, adult male and microfilaria (Mf) life stages, were measured via qPCR, with highest expression found in the adult stages. Dim-GLC-2 forms homomeric channels with low sensitivity to monosodium <span>L</span>-glutamate (MSG) and <span>L</span>-glutamic acid. Homodimer models were created to visualize docking of glutamate to the binding site, and several potential interactions were identified and compared to the original crystal structure of the glutamate-gated chloride channel from <em>Caenorhabditis elegans</em>.</div></div>","PeriodicalId":18721,"journal":{"name":"Molecular and biochemical parasitology","volume":"266 ","pages":"Article 111734"},"PeriodicalIF":1.5,"publicationDate":"2026-01-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146046734","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Amphids are sensory neurons that nematodes use to sense their environment. The IVR-10 strain is an ivermectin (IVM) resistant strain of Caenorhabditis elegans generated in the laboratory by repeated exposure to IVM. We found that the IVR-10 strain is dye filling defective which may be due to shortened amphids. The amphidial pore of the N2 Bristol strain lit up with an IVM antibody, providing direct immunolocalization of IVM and confirming early hypothesis based on functional studies. This suggests that IVM may enter the worms via the amphidial pore. The findings reiterate the importance of amphidial pore as a structure that is exposed to the chemical environment and may be a portal for drug entry.
{"title":"Ivermectin localization at the amphidial pore and dye-filling defects in the IVR-10 strain of Caenorhabditis elegans","authors":"Umer Chaudhry , Mohid Ashraf , Sidra Ashraf , Moneeb Ashraf , Sohaib Ashraf , Ali Raza , Shoaib Ashraf","doi":"10.1016/j.molbiopara.2026.111723","DOIUrl":"10.1016/j.molbiopara.2026.111723","url":null,"abstract":"<div><div>Amphids are sensory neurons that nematodes use to sense their environment. The IVR-10 strain is an ivermectin (IVM) resistant strain of <em>Caenorhabditis elegans</em> generated in the laboratory by repeated exposure to IVM. We found that the IVR-10 strain is dye filling defective which may be due to shortened amphids. The amphidial pore of the N2 Bristol strain lit up with an IVM antibody, providing direct immunolocalization of IVM and confirming early hypothesis based on functional studies. This suggests that IVM may enter the worms via the amphidial pore. The findings reiterate the importance of amphidial pore as a structure that is exposed to the chemical environment and may be a portal for drug entry.</div></div>","PeriodicalId":18721,"journal":{"name":"Molecular and biochemical parasitology","volume":"265 ","pages":"Article 111723"},"PeriodicalIF":1.5,"publicationDate":"2026-01-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145977529","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2026-01-08DOI: 10.1016/j.molbiopara.2026.111722
Ankita S. Gamit , Tejal R. Humal , Piyush S. Desai , Navin B. Patel , Adriana Moreno-Rodriguez , Gildardo Rivera , Faiyazalam M. Shaikh , Vatsal M. Patel
A series of amide-linked bis-benzothiazoles was synthesized using an efficient microwave-assisted strategy that integrates the Petasis multicomponent reaction with HATU-mediated amide coupling. The methodology enabled rapid reactions (2 and 5 min) with high isolated yields of up to 94 %, highlighting the operational simplicity and energy efficiency of microwave-assisted organic synthesis. The structures of synthesized compounds were confirmed by FT-IR, 1H and 13C NMR, and ESI-MS spectroscopy. In vitro safety profiling against J774.2 macrophages demonstrated low cytotoxicity for most derivatives (CC50 > 200 µM). Antiprotozoal evaluation revealed notable activity against Leishmania mexicana, with compound 4a (IC50 = 12.40 µM) and compound 5a (IC50 = 27.05 µM) showing the highest potency, along with potent to good inhibition of Trypanosoma cruzi by compounds 5b and 5 g (IC50 = 58.95 and 51.89 µM, respectively). Structure-activity relationship analysis indicated that electron-donating substituents (-CH3, -OCH3) on the amide moiety reduced cytotoxicity while enhancing antiprotozoal activity. In particular, compounds 5a, 5b, and 5 g emerged as promising lead candidates with a favourable balance between potency and safety for further development as antiprotozoal agents.
{"title":"Petasis-amide coupling enabled microwave-assisted synthesis of bis-benzothiazoles with safety profiling and antiprotozoal evaluation","authors":"Ankita S. Gamit , Tejal R. Humal , Piyush S. Desai , Navin B. Patel , Adriana Moreno-Rodriguez , Gildardo Rivera , Faiyazalam M. Shaikh , Vatsal M. Patel","doi":"10.1016/j.molbiopara.2026.111722","DOIUrl":"10.1016/j.molbiopara.2026.111722","url":null,"abstract":"<div><div>A series of amide-linked bis-benzothiazoles was synthesized using an efficient microwave-assisted strategy that integrates the Petasis multicomponent reaction with HATU-mediated amide coupling. The methodology enabled rapid reactions (2 and 5 min) with high isolated yields of up to 94 %, highlighting the operational simplicity and energy efficiency of microwave-assisted organic synthesis. The structures of synthesized compounds were confirmed by FT-IR, <sup>1</sup>H and <sup>13</sup>C NMR, and ESI-MS spectroscopy. <em>In vitro</em> safety profiling against J774.2 macrophages demonstrated low cytotoxicity for most derivatives (CC<sub>50</sub> > 200 µM). Antiprotozoal evaluation revealed notable activity against <em>Leishmania mexicana</em>, with compound <strong>4a</strong> (IC<sub>50</sub> = 12.40 µM) and compound <strong>5a</strong> (IC<sub>50</sub> = 27.05 µM) showing the highest potency, along with potent to good inhibition of <em>Trypanosoma cruzi</em> by compounds <strong>5b</strong> and <strong>5 g</strong> (IC<sub>50</sub> = 58.95 and 51.89 µM, respectively). Structure-activity relationship analysis indicated that electron-donating substituents (-CH<sub>3</sub>, -OCH3) on the amide moiety reduced cytotoxicity while enhancing antiprotozoal activity. In particular, compounds <strong>5a</strong>, <strong>5b</strong>, and <strong>5 g</strong> emerged as promising lead candidates with a favourable balance between potency and safety for further development as antiprotozoal agents.</div></div>","PeriodicalId":18721,"journal":{"name":"Molecular and biochemical parasitology","volume":"265 ","pages":"Article 111722"},"PeriodicalIF":1.5,"publicationDate":"2026-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145948390","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-20DOI: 10.1016/j.molbiopara.2025.111721
Romana Teixeira , Ana Valério-Bolas , Isilda Flor , Carlos Pinto , Luís Madeira de Carvalho , Maria Constança Pomba
Domestic cats can be infected with various cardiopulmonary metastrongylids. Although A. abstrusus is widely distributed globally, data regarding the occurrence of T. brevior and A. chaubaudi in Portugal are currently nonexistent. This study aimed to evaluate the presence of cardiopulmonary parasite species in domestic cats from the Azores, Portugal, using copromicroscopy and molecular methods. A total of 57 domestic cats were included in this study, and fecal samples were previously analyzed using the Baermann technique. The detected larvae were collected, morphologically identified, and subsequently confirmed through molecular analysis using triplex semi-nested PCR. 57 domestic cats tested positive for cardiopulmonary parasites by copromicroscopy. Triplex semi-nested PCR analysis confirmed the presence of A. abstrusus (326 bp), T. brevior (520 bp) and A. chabaudi (200 bp) in the Azores archipelago. The present study is the first to molecularly confirm A. abstrusus, T. brevior, and A. chabaudi in domestic cats from Portugal and the first molecular report of domestic cats from the Azores Islands. Future studies are recommended to further investigate the distribution and epidemiology of these parasites in felines.
{"title":"Molecular identification of Aelurostrongylus abstrusus, Troglostrongylus brevior and Angiostrongylus chabaudi in domestic cats from the Azores Islands (Portugal)","authors":"Romana Teixeira , Ana Valério-Bolas , Isilda Flor , Carlos Pinto , Luís Madeira de Carvalho , Maria Constança Pomba","doi":"10.1016/j.molbiopara.2025.111721","DOIUrl":"10.1016/j.molbiopara.2025.111721","url":null,"abstract":"<div><div>Domestic cats can be infected with various cardiopulmonary metastrongylids. Although <em>A. abstrusus</em> is widely distributed globally, data regarding the occurrence of <em>T. brevior</em> and <em>A. chaubaudi</em> in Portugal are currently nonexistent. This study aimed to evaluate the presence of cardiopulmonary parasite species in domestic cats from the Azores, Portugal, using copromicroscopy and molecular methods. A total of 57 domestic cats were included in this study, and fecal samples were previously analyzed using the Baermann technique. The detected larvae were collected, morphologically identified, and subsequently confirmed through molecular analysis using triplex semi-nested PCR. 57 domestic cats tested positive for cardiopulmonary parasites by copromicroscopy. Triplex semi-nested PCR analysis confirmed the presence of <em>A. abstrusus</em> (326 bp), <em>T. brevior</em> (520 bp) and <em>A. chabaudi</em> (200 bp) in the Azores archipelago. The present study is the first to molecularly confirm <em>A. abstrusus</em>, <em>T. brevior</em>, and <em>A. chabaudi</em> in domestic cats from Portugal and the first molecular report of domestic cats from the Azores Islands. Future studies are recommended to further investigate the distribution and epidemiology of these parasites in felines.</div></div>","PeriodicalId":18721,"journal":{"name":"Molecular and biochemical parasitology","volume":"265 ","pages":"Article 111721"},"PeriodicalIF":1.5,"publicationDate":"2025-12-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145810687","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-20DOI: 10.1016/j.molbiopara.2025.111720
Iman F. Abou-El-Naga
Toxocara canis is unable to synthesize sufficient lipids de novo to meet its biological requirements and therefore depends on host-derived lipids for survival. The parasite expresses a diverse set of lipid transport proteins spanning all major classes, such as pseudocoelomic fluid lipoproteins (vitellogenins), nematode polyprotein antigens/allergens, intracellular carriers (fatty-acid binding proteins, phosphatidylinositol-transfer proteins), secreted lipid-binding proteins (fatty acid-and retinol-binding proteins, venom allergen-like proteins), membrane-associated transporters (Niemann-Pick C, ABC transporters, microsomal triglyceride transfer protein, bridge-like lipid-transfer proteins) and lipid-anchored carriers (phosphatidylethanolamine-binding proteins). These proteins mediate uptake and distribution of dietary and host lipids to drive parasite growth and reproduction, while simultaneously modulating host immune responses. Many of these transporters are released in the parasite’s excretory/secretory products and are found in extracellular vesicles, where they mediate host-parasite interactions and immunomodulation. These specialized lipid-acquisition strategies support parasite survival, drive immune evasion and pathogenesis, and highlight these proteins as candidates for novel diagnostics or therapeutic targets.
{"title":"Lipid transport proteins in Toxocara canis: Host lipid acquisition and immune modulation","authors":"Iman F. Abou-El-Naga","doi":"10.1016/j.molbiopara.2025.111720","DOIUrl":"10.1016/j.molbiopara.2025.111720","url":null,"abstract":"<div><div><em>Toxocara canis</em> is unable to synthesize sufficient lipids de novo to meet its biological requirements and therefore depends on host-derived lipids for survival. The parasite expresses a diverse set of lipid transport proteins spanning all major classes, such as pseudocoelomic fluid lipoproteins (vitellogenins), nematode polyprotein antigens/allergens, intracellular carriers (fatty-acid binding proteins, phosphatidylinositol-transfer proteins), secreted lipid-binding proteins (fatty acid-and retinol-binding proteins, venom allergen-like proteins), membrane-associated transporters (Niemann-Pick C, ABC transporters, microsomal triglyceride transfer protein, bridge-like lipid-transfer proteins) and lipid-anchored carriers (phosphatidylethanolamine-binding proteins). These proteins mediate uptake and distribution of dietary and host lipids to drive parasite growth and reproduction, while simultaneously modulating host immune responses. Many of these transporters are released in the parasite’s excretory/secretory products and are found in extracellular vesicles, where they mediate host-parasite interactions and immunomodulation. These specialized lipid-acquisition strategies support parasite survival, drive immune evasion and pathogenesis, and highlight these proteins as candidates for novel diagnostics or therapeutic targets.</div></div>","PeriodicalId":18721,"journal":{"name":"Molecular and biochemical parasitology","volume":"265 ","pages":"Article 111720"},"PeriodicalIF":1.5,"publicationDate":"2025-12-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145810646","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-12-08DOI: 10.1016/j.molbiopara.2025.111712
Ellen Gomes , Camila Rolemberg Santana Travaglini Berti de Correia , Caroline Torres , Mariele Cristina de Carvalho , Taissa de Oliveira de Castro , Wesley Klaysson Pereira Regatieri , Nayore Tamie Takamiya , Luana Aparecida Rogerio , Adriano Cappellazzo Coelho , Juliana Ide Aoki , Sandra Regina Maruyama , Felipe Roberti Teixeira
LinfCul1 is a key component of the E3 ubiquitin ligase complex (LinfCRL1) in Leishmania infantum, which interacts with LinfSkp1 and LinfRbx1 at the N- and C-termini, respectively. To investigate the role of LinfCul1 in parasite proliferation, rosette formation, and macrophage infection, we generated a mutant LinfCul1 (mLinfCUL1) lacking the LinfSkp1 interaction region. Co-immunoprecipitation assays confirmed that mLinfCul1 exhibited reduced interaction with LinfSkp1, thereby disrupting LinfCRL1 function. Functional assays demonstrated that LinfCUL1 knockout (∆cul1) led to impaired proliferation and enhanced rosette formation, both of which were rescued by LinfCUL1 WT but not by mLinfCUL1 expression, confirming the requirement of the LinfCul1-LinfSkp1 interaction for these processes. Additionally, macrophage infection assays revealed that ∆cul1 parasites exhibited reduced infectivity and amastigote proliferation, which was restored upon LinfCUL1 WT expression in the parasites. Interestingly, mLinfCUL1 exhibited a lower infectivity index than ∆cul1, suggesting that LinfCul1 functions as a LinfCRL1 component that contributes to this process. These findings highlight the essential role of LinfCul1 in parasite proliferation and infectivity and reinforce its canonical function in ubiquitination-dependent parasite biology. Moreover, this study provides valuable insights into the molecular mechanisms governing parasite development and host interactions, thereby contributing to a better understanding of Leishmania infantum biology.
{"title":"LinfCul1 interaction with LinfSkp1 affects different cellular processes in Leishmania infantum","authors":"Ellen Gomes , Camila Rolemberg Santana Travaglini Berti de Correia , Caroline Torres , Mariele Cristina de Carvalho , Taissa de Oliveira de Castro , Wesley Klaysson Pereira Regatieri , Nayore Tamie Takamiya , Luana Aparecida Rogerio , Adriano Cappellazzo Coelho , Juliana Ide Aoki , Sandra Regina Maruyama , Felipe Roberti Teixeira","doi":"10.1016/j.molbiopara.2025.111712","DOIUrl":"10.1016/j.molbiopara.2025.111712","url":null,"abstract":"<div><div>LinfCul1 is a key component of the E3 ubiquitin ligase complex (LinfCRL1) in <em>Leishmania infantum</em>, which interacts with LinfSkp1 and LinfRbx1 at the N- and C-termini, respectively. To investigate the role of LinfCul1 in parasite proliferation, rosette formation, and macrophage infection, we generated a mutant LinfCul1 (<em>mLinfCUL1</em>) lacking the LinfSkp1 interaction region. Co-immunoprecipitation assays confirmed that mLinfCul1 exhibited reduced interaction with LinfSkp1, thereby disrupting LinfCRL1 function. Functional assays demonstrated that <em>LinfCUL1</em> knockout (∆<em>cul1</em>) led to impaired proliferation and enhanced rosette formation, both of which were rescued by <em>LinfCUL1</em> WT but not by <em>mLinfCUL1</em> expression, confirming the requirement of the LinfCul1-LinfSkp1 interaction for these processes. Additionally, macrophage infection assays revealed that ∆cul1 parasites exhibited reduced infectivity and amastigote proliferation, which was restored upon <em>LinfCUL1</em> WT expression in the parasites. Interestingly, <em>mLinfCUL1</em> exhibited a lower infectivity index than ∆<em>cul1</em>, suggesting that LinfCul1 functions as a LinfCRL1 component that contributes to this process. These findings highlight the essential role of LinfCul1 in parasite proliferation and infectivity and reinforce its canonical function in ubiquitination-dependent parasite biology. Moreover, this study provides valuable insights into the molecular mechanisms governing parasite development and host interactions, thereby contributing to a better understanding of <em>Leishmania infantum</em> biology.</div></div>","PeriodicalId":18721,"journal":{"name":"Molecular and biochemical parasitology","volume":"265 ","pages":"Article 111712"},"PeriodicalIF":1.5,"publicationDate":"2025-12-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145724213","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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