{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T00:52:40Z","timestamp":1785372760834,"version":"3.55.0"},"reference-count":142,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2022,7,7]],"date-time":"2022-07-07T00:00:00Z","timestamp":1657152000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Microorganisms"],"abstract":"<jats:p>The Apicomplexa are obligate intracellular parasites responsible for several important human diseases. These protozoan organisms have evolved several strategies to modify the host cell environment to create a favorable niche for their survival. The host cytoskeleton is widely manipulated during all phases of apicomplexan intracellular infection. Moreover, the localization and organization of host organelles are altered in order to scavenge nutrients from the host. Small GTPases are a class of proteins widely involved in intracellular pathways governing different processes, from cytoskeletal and organelle organization to gene transcription and intracellular trafficking. These proteins are already known to be involved in infection by several intracellular pathogens, including viruses, bacteria and protozoan parasites. In this review, we recapitulate the mechanisms by which apicomplexan parasites manipulate the host cell during infection, focusing on the role of host small GTPases. We also discuss the possibility of considering small GTPases as potential targets for the development of novel host-targeted therapies against apicomplexan infections.<\/jats:p>","DOI":"10.3390\/microorganisms10071370","type":"journal-article","created":{"date-parts":[[2022,7,7]],"date-time":"2022-07-07T07:51:56Z","timestamp":1657180316000},"page":"1370","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":10,"title":["Role of Host Small GTPases in Apicomplexan Parasite Infection"],"prefix":"10.3390","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-5961-9746","authenticated-orcid":false,"given":"Silvio","family":"Paone","sequence":"first","affiliation":[{"name":"Department of Infectious Diseases, Istituto Superiore di Sanit\u00e0, 00161 Rome, Italy"},{"name":"Department of Public Health and Infectious Diseases, Sapienza Universit\u00e0 di Roma, 00161 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3882-8017","authenticated-orcid":false,"given":"Anna","family":"Olivieri","sequence":"additional","affiliation":[{"name":"Department of Infectious Diseases, Istituto Superiore di Sanit\u00e0, 00161 Rome, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,7,7]]},"reference":[{"key":"ref_1","unstructured":"WHO (2022). World Malaria Report 2021, World Health Organization."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"12102","DOI":"10.1038\/s41598-020-69078-9","article-title":"Global, regional, and country seroprevalence of Toxoplasma gondii in pregnant women: A systematic review, modelling and meta-analysis","volume":"10","author":"Bigna","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"129","DOI":"10.4103\/2229-5070.190817","article-title":"Toxoplasmosis in HIV infection: An overview","volume":"6","author":"Basavaraju","year":"2016","journal-title":"Trop. Parasitol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1556\/1886.2019.00019","article-title":"Infection: Epidemiology, Pathogenesis, and Differential Diagnosis","volume":"9","author":"Gerace","year":"2019","journal-title":"Eur. J. Microbiol. Immunol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1016\/j.ijpara.2012.09.009","article-title":"Evolution of apicomplexan secretory organelles","volume":"42","author":"Gubbels","year":"2012","journal-title":"Int. J. Parasitol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"684","DOI":"10.1080\/10635150701494127","article-title":"Diversity, nomenclature, and taxonomy of protists","volume":"56","author":"Adl","year":"2007","journal-title":"Syst. Biol."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Krishnan, A., and Soldati-Favre, D. (2021). Amino Acid Metabolism in Apicomplexan Parasites. Metabolites, 11.","DOI":"10.3390\/metabo11020061"},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Shunmugam, S., Arnold, C.S., Dass, S., Katris, N.J., and Bott\u00e9, C.Y. (2022). The flexibility of Apicomplexa parasites in lipid metabolism. PLoS Pathog., 18.","DOI":"10.1371\/journal.ppat.1010313"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"649184","DOI":"10.3389\/fcell.2021.649184","article-title":"How Malaria Parasites Acquire Nutrients From Their Host","volume":"9","author":"Counihan","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1436","DOI":"10.1017\/S0031182014000493","article-title":"Besnoitia besnoiti and Toxoplasma gondii: Two apicomplexan strategies to manipulate the host cell centrosome and Golgi apparatus","volume":"141","author":"Cardoso","year":"2014","journal-title":"Parasitology"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.exppara.2018.02.008","article-title":"Modulation of cis- and trans- Golgi and the Rab9A-GTPase during infection by Besnoitia besnoiti, Toxoplasma gondii and Neospora caninum","volume":"187","author":"Cardoso","year":"2018","journal-title":"Exp. Parasitol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"jcs252213","DOI":"10.1242\/jcs.252213","article-title":"Hijacking of the host cell Golgi by Plasmodium berghei liver stage parasites","volume":"134","author":"Caldelari","year":"2021","journal-title":"J. Cell Sci."},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Kellermann, M., Scharte, F., and Hensel, M. (2021). Manipulation of Host Cell Organelles by Intracellular Pathogens. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22126484"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1974","DOI":"10.1091\/mbc.e12-11-0827","article-title":"Toxoplasma gondii salvages sphingolipids from the host Golgi through the rerouting of selected Rab vesicles to the parasitophorous vacuole","volume":"24","author":"Romano","year":"2013","journal-title":"Mol. Biol. Cell"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"4235","DOI":"10.1083\/jcb.201701108","article-title":"The parasite Toxoplasma sequesters diverse Rab host vesicles within an intravacuolar network","volume":"216","author":"Romano","year":"2017","journal-title":"J. Cell Biol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"15611","DOI":"10.1074\/jbc.M109.095778","article-title":"Coordinate control of host centrosome position, organelle distribution, and migratory response by Toxoplasma gondii via host mTORC2","volume":"285","author":"Wang","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/j.cell.2006.01.056","article-title":"Toxoplasma gondii sequesters lysosomes from mammalian hosts in the vacuolar space","volume":"125","author":"Coppens","year":"2006","journal-title":"Cell"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"957","DOI":"10.1017\/S0031182016000524","article-title":"Apicomplexans pulling the strings: Manipulation of the host cell cytoskeleton dynamics","volume":"143","author":"Cardoso","year":"2016","journal-title":"Parasitology"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1146\/annurev.micro.62.081307.162802","article-title":"Hijacking of host cellular functions by the Apicomplexa","volume":"62","author":"Plattner","year":"2008","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"107","DOI":"10.3389\/fcimb.2016.00107","article-title":"Hijacking Host Cell Highways: Manipulation of the Host Actin Cytoskeleton by Obligate Intracellular Bacterial Pathogens","volume":"6","author":"Colonne","year":"2016","journal-title":"Front. Cell. Infect. Microbiol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1016\/j.chom.2009.05.013","article-title":"Role of the parasite and host cytoskeleton in apicomplexa parasitism","volume":"5","year":"2009","journal-title":"Cell Host. Microbe"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1680","DOI":"10.1128\/EC.00079-10","article-title":"Host cell invasion by Toxoplasma gondii is temporally regulated by the host microtubule cytoskeleton","volume":"9","author":"Sweeney","year":"2010","journal-title":"Eukaryot. Cell"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"3199","DOI":"10.1038\/srep03199","article-title":"Characterization of the interaction between Toxoplasma gondii rhoptry neck protein 4 and host cellular \u03b2-tubulin","volume":"3","author":"Takemae","year":"2013","journal-title":"Sci. Rep."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/j.chom.2009.01.011","article-title":"Host cell entry by apicomplexa parasites requires actin polymerization in the host cell","volume":"5","author":"Gonzalez","year":"2009","journal-title":"Cell Host Microbe"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1110","DOI":"10.1038\/ncb1007-1110","article-title":"The many faces of actin: Matching assembly factors with cellular structures","volume":"9","author":"Chhabra","year":"2007","journal-title":"Nat. Cell Biol."},{"key":"ref_26","first-page":"4333","article-title":"Toxofilin upregulates the host cortical actin cytoskeleton dynamics, facilitating Toxoplasma invasion","volume":"125","author":"Abrivard","year":"2012","journal-title":"J. Cell Sci."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.micinf.2010.10.007","article-title":"Involvement of host calpain in the invasion of Cryptosporidium parvum","volume":"13","author":"Nie","year":"2011","journal-title":"Microbes Infect."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"2117","DOI":"10.1242\/jcs.110.17.2117","article-title":"Association of host cell endoplasmic reticulum and mitochondria with the Toxoplasma gondii parasitophorous vacuole membrane: A high affinity interaction","volume":"110","author":"Sinai","year":"1997","journal-title":"J. Cell Sci."},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Pernas, L., Adomako-Ankomah, Y., Shastri, A.J., Ewald, S.E., Treeck, M., Boyle, J.P., and Boothroyd, J.C. (2014). Toxoplasma effector MAF1 mediates recruitment of host mitochondria and impacts the host response. PLoS Biol., 12.","DOI":"10.1371\/journal.pbio.1001845"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"e00183-17","DOI":"10.1128\/mSphere.00183-17","article-title":"MAF1b Binds the Host Cell MIB Complex To Mediate Mitochondrial Association","volume":"2","author":"Kelly","year":"2017","journal-title":"mSphere"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1111\/boc.201900107","article-title":"Sitting in the driver\u2019s seat: Manipulation of mammalian cell Rab GTPase functions by apicomplexan parasites","volume":"112","author":"Coppens","year":"2020","journal-title":"Biol. Cell"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"3459","DOI":"10.1182\/blood-2014-06-583054","article-title":"Export of virulence proteins by malaria-infected erythrocytes involves remodeling of host actin cytoskeleton","volume":"124","author":"Rug","year":"2014","journal-title":"Blood"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.chom.2012.12.001","article-title":"A host GPCR signaling network required for the cytolysis of infected cells facilitates release of apicomplexan parasites","volume":"13","author":"Millholland","year":"2013","journal-title":"Cell Host Microbe"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1299","DOI":"10.1126\/science.1062023","article-title":"The guanine nucleotide-binding switch in three dimensions","volume":"294","author":"Vetter","year":"2001","journal-title":"Science"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.1242\/jcs.03428","article-title":"Rho activation at a glance","volume":"120","author":"Buchsbaum","year":"2007","journal-title":"J. Cell Sci."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"3014","DOI":"10.1007\/s00018-005-5136-x","article-title":"GTPase activating proteins: Structural and functional insights 18 years after discovery","volume":"62","author":"Scheffzek","year":"2005","journal-title":"Cell. Mol. Life Sci. CMLS"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.ajps.2018.06.004","article-title":"Small GTPases: Structure, biological function and its interaction with nanoparticles","volume":"14","author":"Song","year":"2019","journal-title":"Asian J. Pharm. Sci."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1016\/S0092-8674(00)81442-7","article-title":"S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells","volume":"93","author":"Hardt","year":"1998","journal-title":"Cell"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1038\/45829","article-title":"A salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion","volume":"401","author":"Fu","year":"1999","journal-title":"Nature"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1449","DOI":"10.1016\/S1097-2765(00)00141-6","article-title":"Modulation of host signaling by a bacterial mimic: Structure of the Salmonella effector SptP bound to Rac1","volume":"6","author":"Stebbins","year":"2000","journal-title":"Mol. Cell"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"e983863","DOI":"10.4161\/sgtp.28209","article-title":"Bacterial factors exploit eukaryotic Rho GTPase signaling cascades to promote invasion and proliferation within their host","volume":"5","author":"Popoff","year":"2014","journal-title":"Small GTPases"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"27407","DOI":"10.1074\/jbc.274.39.27407","article-title":"Neosynthesis and activation of Rho by Escherichia coli cytotoxic necrotizing factor (CNF1) reverse cytopathic effects of ADP-ribosylated Rho","volume":"274","author":"Barth","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"3344","DOI":"10.1128\/IAI.01937-06","article-title":"The cytotoxic necrotizing factors from Yersinia pseudotuberculosis and from Escherichia coli bind to different cellular receptors but take the same route to the cytosol","volume":"75","author":"Blumenthal","year":"2007","journal-title":"Infect. Immun."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"32977","DOI":"10.1074\/jbc.M114.601310","article-title":"AMPylation of Rho GTPases subverts multiple host signaling processes","volume":"289","author":"Woolery","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1038\/nature17657","article-title":"Ubiquitination independent of E1 and E2 enzymes by bacterial effectors","volume":"533","author":"Qiu","year":"2016","journal-title":"Nature"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"2902","DOI":"10.1099\/vir.0.014159-0","article-title":"Cross-talk between Rac1 and Cdc42 GTPases regulates formation of filopodia required for dengue virus type-2 entry into HMEC-1 cells","volume":"90","author":"Meza","year":"2009","journal-title":"J. Gen. Virol."},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Wang, J.L., Zhang, J.L., Chen, W., Xu, X.F., Gao, N., Fan, D.Y., and An, J. (2010). Roles of small GTPase Rac1 in the regulation of actin cytoskeleton during dengue virus infection. PLoS Negl. Trop. Dis., 4.","DOI":"10.1371\/journal.pntd.0000809"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"7138","DOI":"10.1128\/JVI.78.13.7138-7147.2004","article-title":"Actin cytoskeletal reorganizations and coreceptor-mediated activation of rac during human immunodeficiency virus-induced cell fusion","volume":"78","author":"Pontow","year":"2004","journal-title":"J. Virol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"2024","DOI":"10.1182\/blood-2011-06-364828","article-title":"Regulation of CXCR4 conformation by the small GTPase Rac1: Implications for HIV infection","volume":"119","author":"Zoughlami","year":"2012","journal-title":"Blood"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"6526","DOI":"10.3390\/v7122955","article-title":"CDC42 Use in Viral Cell Entry Processes by RNA Viruses","volume":"7","author":"Swaine","year":"2015","journal-title":"Viruses"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1080\/21541248.2017.1346552","article-title":"Viral interactions with host cell Rab GTPases","volume":"9","author":"Spearman","year":"2018","journal-title":"Small GTPases"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"9259","DOI":"10.1128\/JVI.00840-07","article-title":"Activation of cellular Arf GTPases by poliovirus protein 3CD correlates with virus replication","volume":"81","author":"Belov","year":"2007","journal-title":"J. Virol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1544","DOI":"10.1128\/JVI.00688-11","article-title":"Activation of the Ras\/Raf\/MEK pathway facilitates hepatitis C virus replication via attenuation of the interferon-JAK-STAT pathway","volume":"86","author":"Zhang","year":"2012","journal-title":"J. Virol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"12417","DOI":"10.1073\/pnas.0605375103","article-title":"A picornavirus protein interacts with Ran-GTPase and disrupts nucleocytoplasmic transport","volume":"103","author":"Porter","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"360","DOI":"10.3389\/fmicb.2018.00360","article-title":"Rac1\/WAVE2 and Cdc42\/N-WASP Participation in Actin-Dependent Host Cell Invasion by Extracellular Amastigotes of","volume":"9","author":"Ferreira","year":"2018","journal-title":"Front. Microbiol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1186\/s13071-015-1097-6","article-title":"Revealing Annexin A2 and ARF-6 enrollment during Trypanosoma cruzi extracellular amastigote-host cell interaction","volume":"8","author":"Teixeira","year":"2015","journal-title":"Parasit. Vectors"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1007\/s00436-005-1333-7","article-title":"Role of small GTPases in Trypanosoma cruzi invasion in MDCK cell lines","volume":"96","author":"Dutra","year":"2005","journal-title":"Parasitol. Res."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"2735","DOI":"10.1002\/eji.200636089","article-title":"Phagocytosis of Leishmania donovani amastigotes is Rac1 dependent and occurs in the absence of NADPH oxidase activation","volume":"36","author":"Lodge","year":"2006","journal-title":"Eur. J. Immunol."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"2613","DOI":"10.1128\/IAI.74.5.2613-2618.2006","article-title":"Leishmania donovani requires functional Cdc42 and Rac1 to prevent phagosomal maturation","volume":"74","author":"Lerm","year":"2006","journal-title":"Infect. Immun."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1007\/978-1-61779-442-1_6","article-title":"Posttranslational lipid modification of Rho family small GTPases","volume":"827","author":"Mitin","year":"2012","journal-title":"Methods Mol. Biol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1301","DOI":"10.1242\/jcs.01118","article-title":"Rho-family GTPases: It\u2019s not only Rac and Rho (and I like it)","volume":"117","author":"Wennerberg","year":"2004","journal-title":"J. Cell Sci."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"560","DOI":"10.1093\/emboj\/21.4.560","article-title":"Distinct mechanisms of internalization of Neisseria gonorrhoeae by members of the CEACAM receptor family involving Rac1- and Cdc42-dependent and -independent pathways","volume":"21","author":"Billker","year":"2002","journal-title":"EMBO J."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"17","DOI":"10.3389\/fcimb.2011.00017","article-title":"Major host factors involved in epithelial cell invasion of Campylobacter jejuni: Role of fibronectin, integrin beta1, FAK, Tiam-1, and DOCK180 in activating Rho GTPase Rac1","volume":"1","author":"Boehm","year":"2011","journal-title":"Front. Cell Infect. Microbiol."},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Ford, C., Nans, A., Boucrot, E., and Hayward, R.D. (2018). Chlamydia exploits filopodial capture and a macropinocytosis-like pathway for host cell entry. PLoS Pathog., 14.","DOI":"10.1371\/journal.ppat.1007051"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"34035","DOI":"10.1074\/jbc.M100609200","article-title":"SopE and SopE2 from Salmonella typhimurium activate different sets of RhoGTPases of the host cell","volume":"276","author":"Friebel","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1042\/BJ20110419","article-title":"Salmonella enterica serotype Typhimurium usurps the scaffold protein IQGAP1 to manipulate Rac1 and MAPK signalling","volume":"440","author":"Kim","year":"2011","journal-title":"Biochem. J."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"2431","DOI":"10.1111\/j.1462-5822.2007.00971.x","article-title":"Role of the small Rho GTPases Rac1 and Cdc42 in host cell invasion of Campylobacter jejuni","volume":"9","author":"Rohde","year":"2007","journal-title":"Cell. Microbiol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1544","DOI":"10.1111\/j.1462-5822.2012.01819.x","article-title":"Cryptococcus neoformans phospholipase B1 activates host cell Rac1 for traversal across the blood-brain barrier","volume":"14","author":"Maruvada","year":"2012","journal-title":"Cell. Microbiol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1016\/j.cell.2006.06.056","article-title":"Yersinia virulence depends on mimicry of host Rho-family nucleotide dissociation inhibitors","volume":"126","author":"Prehna","year":"2006","journal-title":"Cell"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1111\/j.1574-6968.2007.00768.x","article-title":"Rac1, RhoA, and Cdc42 participate in HeLa cell invasion by group B streptococcus","volume":"272","author":"Burnham","year":"2007","journal-title":"FEMS Microbiol. Lett."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1016\/S0092-8674(02)01132-7","article-title":"CNF1 exploits the ubiquitin-proteasome machinery to restrict Rho GTPase activation for bacterial host cell invasion","volume":"111","author":"Doye","year":"2002","journal-title":"Cell"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"22054","DOI":"10.1038\/s41598-020-79052-0","article-title":"Characterization of the erythrocyte GTPase Rac1 in relation to Plasmodium falciparum invasion","volume":"10","author":"Paone","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"e01498-21","DOI":"10.1128\/AAC.01498-21","article-title":"In vitro antimalarial activity of inhibitors of the human GTPase Rac1","volume":"66","author":"Parapini","year":"2021","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"M111.010678","DOI":"10.1074\/mcp.M111.010678","article-title":"The malaria parasite progressively dismantles the host erythrocyte cytoskeleton for efficient egress","volume":"10","author":"Millholland","year":"2011","journal-title":"Mol. Cell. Proteom."},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Messina, V., Loizzo, S., Travaglione, S., Bertuccini, L., Condello, M., Superti, F., Guidotti, M., Alano, P., Silvestrini, F., and Fiorentini, C. (2019). The bacterial protein CNF1 as a new strategy against Plasmodium falciparum cytoadherence. PLoS ONE, 14.","DOI":"10.1371\/journal.pone.0213529"},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Na, R.-H., Zhu, G.-H., Luo, J.-X., Meng, X.-J., Cui, L., Peng, H.-J., Chen, X.-g., and Gomez-Cambronero, J. (2013). Enzymatically active Rho and Rac small-GTPases are involved in the establishment of the vacuolar membrane after Toxoplasma gondii invasion of host cells. BMC Microbiol., 13.","DOI":"10.1186\/1471-2180-13-125"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"610","DOI":"10.1007\/s11427-019-9564-0","article-title":"Host cell Rac1 GTPase facilitates Toxoplasma gondii invasion","volume":"63","author":"Wei","year":"2020","journal-title":"Sci. China Life Sci."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"3011","DOI":"10.1128\/IAI.72.5.3011-3021.2004","article-title":"Cdc42 and the actin-related protein\/neural Wiskott-Aldrich syndrome protein network mediate cellular invasion by Cryptosporidium parvum","volume":"72","author":"Chen","year":"2004","journal-title":"Infect. Immun."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"31671","DOI":"10.1074\/jbc.M401592200","article-title":"Phosphatidylinositol 3-kinase and frabin mediate Cryptosporidium parvum cellular invasion via activation of Cdc42","volume":"279","author":"Chen","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_80","doi-asserted-by":"crossref","unstructured":"Ma, M., and Baumgartner, M. (2013). Filopodia and membrane blebs drive efficient matrix invasion of macrophages transformed by the intracellular parasite Theileria annulata. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0075577"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1367","DOI":"10.1016\/j.bcp.2006.06.033","article-title":"Listeria monocytogenes induced Rac1-dependent signal transduction in endothelial cells","volume":"72","author":"Schmeck","year":"2006","journal-title":"Biochem. Pharmacol."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"19427","DOI":"10.1074\/jbc.M109.003442","article-title":"Cdc42 and the phosphatidylinositol 3-kinase-Akt pathway are essential for PspC-mediated internalization of pneumococci by respiratory epithelial cells","volume":"284","author":"Agarwal","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1263","DOI":"10.1248\/bpb.b21-00054","article-title":"NSC23766 and Ehop016 Suppress Herpes Simplex Virus-1 Replication by Inhibiting Rac1 Activity","volume":"44","author":"Zhang","year":"2021","journal-title":"Biol. Pharm. Bull."},{"key":"ref_84","doi-asserted-by":"crossref","unstructured":"Dierkes, R., Warnking, K., Liedmann, S., Seyer, R., Ludwig, S., and Ehrhardt, C. (2014). The Rac1 inhibitor NSC23766 exerts anti-influenza virus properties by affecting the viral polymerase complex activity. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0088520"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"1647","DOI":"10.1111\/j.1462-5822.2005.00582.x","article-title":"Leishmania donovani promastigotes induce periphagosomal F-actin accumulation through retention of the GTPase Cdc42","volume":"7","author":"Lodge","year":"2005","journal-title":"Cell Microbiol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"4571","DOI":"10.1128\/IAI.70.8.4571-4580.2002","article-title":"Opsonization modulates Rac-1 activation during cell entry by Leishmania amazonensis","volume":"70","author":"Morehead","year":"2002","journal-title":"Infect. Immun."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1086\/528988","article-title":"Rho kinase inhibition in severe malaria: Thwarting parasite-induced collateral damage to endothelia","volume":"197","author":"Taoufiq","year":"2008","journal-title":"J. Infect. Dis."},{"key":"ref_88","doi-asserted-by":"crossref","unstructured":"Seixas, E., Ramalho, J.S., Mota, L.J., Barral, D.C., and Seabra, M.C. (2012). Bacteria and protozoa differentially modulate the expression of Rab proteins. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0039858"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"12998","DOI":"10.1038\/s41598-018-31171-5","article-title":"Rab GTPase regulation of bacteria and protozoa phagocytosis occurs through the modulation of phagocytic receptor surface expression","volume":"8","author":"Seixas","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1111\/boc.202000005","article-title":"The unicellular eukaryotic parasite Toxoplasma gondii hijacks the migration machinery of mononuclear phagocytes to promote its dissemination","volume":"112","author":"Barragan","year":"2020","journal-title":"Biol. Cell"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"656","DOI":"10.1016\/j.bbrc.2008.11.108","article-title":"ARF6, PI3-kinase and host cell actin cytoskeleton in Toxoplasma gondii cell invasion","volume":"378","author":"Cruz","year":"2009","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"e00709-19","DOI":"10.1128\/mSphere.00709-19","article-title":"Recruitment of Host Nuclear Pore Components to the Vicinity of Theileria Schizonts","volume":"5","author":"Huber","year":"2020","journal-title":"Msphere"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"7618","DOI":"10.1073\/pnas.0307512101","article-title":"Rational design and characterization of a Rac GTPase-specific small molecule inhibitor","volume":"101","author":"Gao","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"2329","DOI":"10.1016\/j.yexcr.2013.04.021","article-title":"Hijacking of Rho GTPases during bacterial infection","volume":"319","author":"Lemichez","year":"2013","journal-title":"Exp. Cell Res."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"35666","DOI":"10.1074\/jbc.M703571200","article-title":"Specificity and mechanism of action of EHT 1864, a novel small molecule inhibitor of Rac family small GTPases","volume":"282","author":"Shutes","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"840","DOI":"10.2174\/18715206113136660334","article-title":"Preclinical development of novel Rac1-GEF signaling inhibitors using a rational design approach in highly aggressive breast cancer cell lines","volume":"14","author":"Cardama","year":"2014","journal-title":"Anticancer Agents Med. Chem."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"3637","DOI":"10.1182\/blood-2006-03-005942","article-title":"Rac GTPases regulate the morphology and deformability of the erythrocyte cytoskeleton","volume":"108","author":"Kalfa","year":"2006","journal-title":"Blood"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"2384","DOI":"10.1099\/mic.0.059972-0","article-title":"Host cell kinases, \u03b15 and \u03b21 integrins, and Rac1 signalling on the microtubule cytoskeleton are important for non-typable Haemophilus influenzae invasion of respiratory epithelial cells","volume":"158","author":"Cano","year":"2012","journal-title":"Microbiology"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"1723","DOI":"10.1056\/NEJMra013170","article-title":"Cryptosporidiosis","volume":"346","author":"Chen","year":"2002","journal-title":"N. Engl. J. Med."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"554","DOI":"10.1128\/CMR.12.4.554","article-title":"New insights into human cryptosporidiosis","volume":"12","author":"Clark","year":"1999","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1146\/annurev.micro.53.1.1","article-title":"Transformation of leukocytes by Theileria parva and T. annulata","volume":"53","author":"Dobbelaere","year":"1999","journal-title":"Annu. Rev. Microbiol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/j.vetimm.2004.01.003","article-title":"Quantitative analysis of pro-inflammatory cytokine mRNA expression in Theileria annulata-infected cell lines derived from resistant and susceptible cattle","volume":"99","author":"McGuire","year":"2004","journal-title":"Vet. Immunol. Immunopathol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"3308","DOI":"10.1038\/sj.emboj.7601778","article-title":"PtdIns(4,5)P-restricted plasma membrane localization of FAN is involved in TNF-induced actin reorganization","volume":"26","author":"Haubert","year":"2007","journal-title":"EMBO J."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1061","DOI":"10.1046\/j.1365-2958.1997.4151781.x","article-title":"Molecular localization of the Escherichia coli cytotoxic necrotizing factor CNF1 cell-binding and catalytic domains","volume":"24","author":"Lemichez","year":"1997","journal-title":"Mol. Microbiol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1038\/nrm2728","article-title":"Rab GTPases as coordinators of vesicle traffic","volume":"10","author":"Stenmark","year":"2009","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"e1140615","DOI":"10.1080\/21592799.2016.1140615","article-title":"Sequential recruitment of Rab GTPases during early stages of phagocytosis","volume":"6","author":"Yeo","year":"2016","journal-title":"Cell. Logist."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1038\/nrm2438","article-title":"Ras oncogenes: Split personalities","volume":"9","author":"Karnoub","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1038\/nrm3117","article-title":"ARF family G proteins and their regulators: Roles in membrane transport, development and disease","volume":"12","author":"Donaldson","year":"2011","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"1249","DOI":"10.1091\/mbc.E18-12-0820","article-title":"ARF GTPases and their GEFs and GAPs: Concepts and challenges","volume":"30","author":"Sztul","year":"2019","journal-title":"Mol. Biol. Cell"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"41573","DOI":"10.1074\/jbc.R300026200","article-title":"Multiple roles for Arf6: Sorting, structuring, and signaling at the plasma membrane","volume":"278","author":"Donaldson","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"345","DOI":"10.3389\/fcell.2020.00345","article-title":"Ran GTPase: A Key Player in Tumor Progression and Metastasis","volume":"8","author":"Boudhraa","year":"2020","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/S0074-7696(08)61858-6","article-title":"Annulate lamellae: A last frontier in cellular organelles","volume":"133","author":"Kessel","year":"1992","journal-title":"Int. Rev. Cytol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"e12838","DOI":"10.1111\/cmi.12838","article-title":"Identification and characterisation of a Theileria annulata proline-rich microtubule and SH3 domain-interacting protein (TaMISHIP) that forms a complex with CLASP1, EB1, and CD2AP at the schizont surface","volume":"20","author":"Huber","year":"2018","journal-title":"Cell. Microbiol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"30","DOI":"10.4103\/2229-5070.175081","article-title":"Antimalarial drug resistance: An overview","volume":"6","author":"Antony","year":"2016","journal-title":"Trop. Parasitol."},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Fairhurst, R.M., and Dondorp, A.M. (2016). Artemisinin-Resistant Plasmodium falciparum Malaria. Microbiol. Spectr., 4.","DOI":"10.1128\/microbiolspec.EI10-0013-2016"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"2587","DOI":"10.3389\/fmicb.2018.02587","article-title":"Drug Resistance in","volume":"9","author":"Montazeri","year":"2018","journal-title":"Front. Microbiol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/s44149-021-00002-y","article-title":"Current status and challenges in drug discovery against the globally important zoonotic cryptosporidiosis","volume":"1","author":"Zhu","year":"2021","journal-title":"Anim. Dis."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"290","DOI":"10.2174\/138161213804070276","article-title":"Targeting host factors to circumvent anti-malarial drug resistance","volume":"19","author":"Mota","year":"2013","journal-title":"Curr. Pharm. Des."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"e01932-17","DOI":"10.1128\/mBio.01932-17","article-title":"Mitigating the Impact of Antibacterial Drug Resistance through Host-Directed Therapies: Current Progress, Outlook, and Challenges","volume":"9","author":"Chiang","year":"2018","journal-title":"MBio"},{"key":"ref_120","doi-asserted-by":"crossref","unstructured":"Stanley, S.A., Barczak, A.K., Silvis, M.R., Luo, S.S., Sogi, K., Vokes, M., Bray, M.A., Carpenter, A.E., Moore, C.B., and Siddiqi, N. (2014). Identification of host-targeted small molecules that restrict intracellular Mycobacterium tuberculosis growth. PLoS Pathog., 10.","DOI":"10.1371\/journal.ppat.1003946"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1111\/hel.12102","article-title":"Helicobacter pylori induces increased expression of the vitamin d receptor in immune responses","volume":"19","author":"Guo","year":"2014","journal-title":"Helicobacter"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"599","DOI":"10.1128\/AAC.04220-14","article-title":"In vitro antiviral activity and preclinical and clinical resistance profile of miravirsen, a novel anti-hepatitis C virus therapeutic targeting the human factor miR-122","volume":"59","author":"Ottosen","year":"2015","journal-title":"Antimicrob Agents Chemother."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"7367","DOI":"10.1128\/JVI.00632-13","article-title":"The small molecules AZD0530 and dasatinib inhibit dengue virus RNA replication via Fyn kinase","volume":"87","author":"LaCroix","year":"2013","journal-title":"J. Virol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"1756284818759483","DOI":"10.1177\/1756284818759483","article-title":"Host-targeting therapies for hepatitis C virus infection: Current developments and future applications","volume":"11","author":"Crouchet","year":"2018","journal-title":"Ther. Adv. Gastroenterol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"4721","DOI":"10.1128\/AAC.49.11.4721-4732.2005","article-title":"Maraviroc (UK-427,857), a potent, orally bioavailable, and selective small-molecule inhibitor of chemokine receptor CCR5 with broad-spectrum anti-human immunodeficiency virus type 1 activity","volume":"49","author":"Dorr","year":"2005","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1016\/j.pt.2018.07.011","article-title":"Opportunities for Host-targeted Therapies for Malaria","volume":"34","author":"Glennon","year":"2018","journal-title":"Trends Parasitol."},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Szewczyk-Golec, K., Paw\u0142owska, M., Weso\u0142owski, R., Wr\u00f3blewski, M., and Mila-Kierzenkowska, C. (2021). Oxidative Stress as a Possible Target in the Treatment of Toxoplasmosis: Perspectives and Ambiguities. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22115705"},{"key":"ref_128","doi-asserted-by":"crossref","unstructured":"Brizuela, M., Huang, H.M., Smith, C., Burgio, G., Foote, S.J., and McMorran, B.J. (2014). Treatment of erythrocytes with the 2-cys peroxiredoxin inhibitor, Conoidin A, prevents the growth of Plasmodium falciparum and enhances parasite sensitivity to chloroquine. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0092411"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"534","DOI":"10.1182\/blood-2014-04-567149","article-title":"Red cells from ferrochelatase-deficient erythropoietic protoporphyria patients are resistant to growth of malarial parasites","volume":"125","author":"Smith","year":"2015","journal-title":"Blood"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"629917","DOI":"10.3389\/fimmu.2021.629917","article-title":"Imiquimod Targets Toxoplasmosis through Modulating Host Toll-Like Receptor-MyD88 Signaling","volume":"12","author":"Hamie","year":"2021","journal-title":"Front. Immunol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1016\/j.tranon.2014.07.004","article-title":"The Rac Inhibitor EHop-016 Inhibits Mammary Tumor Growth and Metastasis in a Nude Mouse Model","volume":"7","author":"Hernandez","year":"2014","journal-title":"Transl. Oncol."},{"key":"ref_132","first-page":"19","article-title":"Pharmacokinetics of Rac inhibitor EHop-016 in mice by ultra-performance liquid chromatography tandem mass spectrometry","volume":"981\u2013982","author":"Duconge","year":"2015","journal-title":"J. Chromatogr. B Analyt. Technol. Biomed. Life Sci."},{"key":"ref_133","doi-asserted-by":"crossref","unstructured":"Prieto-Dominguez, N., Parnell, C., and Teng, Y. (2019). Drugging the Small GTPase Pathways in Cancer Treatment: Promises and Challenges. Cells, 8.","DOI":"10.3390\/cells8030255"},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"1925","DOI":"10.1158\/1535-7163.MCT-13-0164","article-title":"RAC1: An emerging therapeutic option for targeting cancer angiogenesis and metastasis","volume":"12","author":"Bid","year":"2013","journal-title":"Mol. Cancer Ther."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1128\/CMR.00111-16","article-title":"Susceptibility Testing of Medically Important Parasites","volume":"30","author":"Debnath","year":"2017","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"1269","DOI":"10.1128\/AAC.01203-07","article-title":"In vitro susceptibility of various genotypic strains of Toxoplasma gondii to pyrimethamine, sulfadiazine, and atovaquone","volume":"52","author":"Meneceur","year":"2008","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"739","DOI":"10.4269\/ajtmh.1993.48.739","article-title":"Parasite lactate dehydrogenase as an assay for Plasmodium falciparum drug sensitivity","volume":"48","author":"Makler","year":"1993","journal-title":"Am. J. Trop. Med. Hyg."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"5363","DOI":"10.2174\/0929867325666180706101404","article-title":"Recent Drug-Repurposing-Driven Advances in the Discovery of Novel Antibiotics","volume":"26","author":"Konreddy","year":"2019","journal-title":"Curr. Med. Chem."},{"key":"ref_139","doi-asserted-by":"crossref","unstructured":"Trivedi, J., Mohan, M., and Byrareddy, S.N. (2020). Drug Repurposing Approaches to Combating Viral Infections. J. Clin. Med., 9.","DOI":"10.3390\/jcm9113777"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1172\/JCI16432","article-title":"CD28-dependent Rac1 activation is the molecular target of azathioprine in primary human CD4+ T lymphocytes","volume":"111","author":"Tiede","year":"2003","journal-title":"J. Clin. Invest."},{"key":"ref_141","doi-asserted-by":"crossref","unstructured":"Oprea, T.I., Sklar, L.A., Agola, J.O., Guo, Y., Silberberg, M., Roxby, J., Vestling, A., Romero, E., Surviladze, Z., and Murray-Krezan, C. (2015). Novel Activities of Select NSAID R-Enantiomers against Rac1 and Cdc42 GTPases. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0142182"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1186\/1475-2875-8-102","article-title":"Azathioprine favourably influences the course of malaria","volume":"8","author":"Bobbala","year":"2009","journal-title":"Malar. J."}],"container-title":["Microorganisms"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-2607\/10\/7\/1370\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T23:43:49Z","timestamp":1760139829000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-2607\/10\/7\/1370"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,7,7]]},"references-count":142,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2022,7]]}},"alternative-id":["microorganisms10071370"],"URL":"https:\/\/doi.org\/10.3390\/microorganisms10071370","relation":{},"ISSN":["2076-2607"],"issn-type":[{"value":"2076-2607","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,7,7]]}}}