Barik S. Immunophilins: for the love of proteins. Cell Mol Life Sci. 2006;63:2889–900.
Wang P, Heitman J. The cyclophilins. Genome Biol. 2005;6:226.
Galat A. Peptidylprolyl cis/trans isomerases (immunophilins): biological diversity-targets-functions. Curr Top Med Chem. 2003;3:1315–47.
Tuccinardi T, Rizzolio F. Peptidyl-prolyl isomerases in human pathologies. Front Pharmacol. 2019;10:794.
Favretto F, Jiménez-Faraco E, Conter C, Dominici P, Hermoso JA, Astegno A. Structural basis for cyclosporin isoform-specific inhibition of cyclophilins from Toxoplasma gondii. ACS Infect Dis. 2023;9:365–77.
Wu Y, Ma Z, Zhang Y, Zhang M, Shi X, Zhang M, et al. The role of cyclophilins in viral infection and the immune response. J Infect. 2022;85:365–73.
Kalinina A, Grigorieva E, Smirnova A, Kazansky D, Khromykh L. Pharmacokinetic parameters of recombinant human cyclophilin A in mice. Eur J Drug Metab Pharmacokinet. 2024;49:57–69.
Lin D-T, Lechleiter JD. Mitochondrial targeted cyclophilin D protects cells from cell death by peptidyl prolyl isomerization. J Biol Chem. 2002;277:31134–41.
Harding MW. Immunophilins, mTOR, and pharmacodynamic strategies for a targeted cancer therapy: commentary re: JM Peralba et al., pharmacodynamic evaluation of CCI-779, an inhibitor of mTOR, in cancer patients. Clin. Cancer Res., 9:2887–2892, 2003. Clin Cancer Res. 2003;9:2882–6.
Liang L, Lin R, Xie Y, Lin H, Shao F, Rui W, et al. The role of cyclophilins in inflammatory bowel disease and colorectal cancer. Int J Biol Sci. 2021;17:2548–60.
Tajti G, Gebetsberger L, Pamlitschka G, Aigner-Radakovics K, Leitner J, Steinberger P, et al. Cyclophilin–CD147 interaction enables SARS-CoV-2 infection of human monocytes and their activation via Toll-like receptors 7 and 8. Front Immunol. 2025;16:1460089.
Wang J-j, Chen C, Xie P-f, Pan Y, Tan Y-h, Tang L-j. Proteomic analysis and immune properties of exosomes released by macrophages infected with Mycobacterium avium. Microbes Infect. 2014;16:283–91.
Szempruch AJ, Dennison L, Kieft R, Harrington JM, Hajduk SL. Sending a message: extracellular vesicles of pathogenic protozoan parasites. Nat Rev Microbiol. 2016;14:669–75.
Sharma AK, Mal S, Sahu SK, Bagchi S, Majumder D, Chakravorty D, et al. Mycobacterial peptidyl prolyl isomerase A activates STING-TBK1-IRF3 signaling to promote IFNβ release in macrophages. FEBS J. 2025;292:94–114.
Zhao X, Zhao X, Di W, Wang C. Inhibitors of cyclophilin A: current and anticipated pharmaceutical agents for inflammatory diseases and cancers. Molecules. 2024;29:1235.
Wang T, Becker D, Twizerimana AP, Luedde T, Gohlke H, Münk C. Cyclophilin a regulates tripartite motif 5 alpha restriction of HIV-1. Int J Mol Sci. 2025;26:495.
Molle J, Duponchel S, Rieusset J, Ovize M, Ivanov AV, Zoulim F, et al. Exploration of the role of cyclophilins in established hepatitis B and C infections. Viruses. 2024;17:11.
Liao Y, Luo D, Peng K, Zeng Y. Cyclophilin A: a key player for etiological agent infection. Appl Microbiol Biotechnol. 2021;105:1365–77.
Xu M, Zhang X, Yu Q, Zhao Q, Li J, Gong P, et al. Characterization of cyclophilin 23 as a novel factor for development and pathogenicity of Cryptosporidium parvum. Vet Parasitol. 2025. https://doi.org/10.1016/j.vetpar.2025.110539.
Kameyama K, Nishimura M, Punsantsogvoo M, Ibrahim HM, Xuan X, Furuoka H, et al. Immunological characterization of Neospora caninum cyclophilin. Parasitology. 2012;139:294–301.
Tuo W, Fetterer R, Jenkins M, Dubey J. Identification and characterization of Neospora caninum cyclophilin that elicits gamma interferon production. Infect Immun. 2005;73:5093–100.
Acharya S, Da’dara AA, Skelly PJ. Schistosome immunomodulators. PLoS Pathog. 2021;17:e1010064.
Kulkarni MM, Karafova A, Kamysz W, Schenkman S, Pelle R, McGwire BS. Secreted trypanosome cyclophilin inactivates lytic insect defense peptides and induces parasite calcineurin activation and infectivity. J Biol Chem. 2013;288:8772–84.
Aranda-Chan V, Cárdenas-Guerra RE, Otero-Pedraza A, Pacindo-Cabrales EE, Flores-Pucheta CI, Montes-Flores O, et al. Insights into peptidyl-prolyl cis-trans isomerases from clinically important protozoans: from structure to potential biotechnological applications. Pathogens. 2024;13:644.
Bruchhaus I, Roeder T, Lotter H, Schwerdtfeger M, Tannich E. Differential gene expression in Entamoeba histolytica isolated from amoebic liver abscess. Mol Microbiol. 2002;44:1063–72.
Carrero JC, Petrossian P, Olivos A, Sánchez-Zerpa Ma, Ostoa-Soloma P, Laclette JP. Effect of cyclosporine A on Entamoeba histolytica. Arch Med Res. 2000;31:S8-9.
Naiyer S, Bhattacharya A, Bhattacharya S. Advances in Entamoeba histolytica biology through transcriptomic analysis. Front Microbiol. 2019;10:1921.
Yu H-S, Kong H-H, Chung D-I. Cloning and characterization of Giardia intestinalis cyclophilin. Korean J Parasitol. 2002;40:131–8.
Hosse RJ, Krücken J, Bierbaum S, Greif G, Wunderlich F. Eimeria tenella: genomic organization and expression of an 89 kDa cyclophilin. Exp Parasitol. 2008;118:275–9.
Perkins ME, Wu TW, Le Blancq SM. Cyclosporin analogs inhibit in vitro growth of Cryptosporidium parvum. Antimicrob Agents Chemother. 1998;42:843–8.
Martin T, Lou Y-C, Chou C-C, Wei S-Y, Sadotra S, Cho C-C, et al. Structural basis of interaction between dimeric cyclophilin 1 and Myb1 transcription factor in Trichomonas vaginalis. Sci Rep. 2018;8:5410.
Chu CH, Huang YH, Liu HW, Hsu HM, Tai JH. Membrane localization of a Myb3 transcription factor regulated by a TvCyP1 cyclophilin in the parasitic protozoan Trichomonas vaginalis. FEBS J. 2018;285:929–46.
Hsu H-M, Huang Y-H, Aryal S, Liu H-W, Chen C, Chen S-H, et al. Endomembrane protein trafficking regulated by a Tv CyP2 cyclophilin in the protozoan parasite, Trichomonas vaginalis. Sci Rep. 2020;10:1275.
Yau W-L, Blisnick T, Taly J-F, Helmer-Citterich M, Schiene-Fischer C, Leclercq O, et al. Cyclosporin A treatment of Leishmania donovani reveals stage-specific functions of cyclophilins in parasite proliferation and viability. PLoS Negl Trop Dis. 2010;4:e729.
Yau WL, Lambertz U, Colineau L, Pescher P, MacDonald A, Zander D, et al. Phenotypic characterization of a Leishmania donovani cyclophilin 40 null mutant. J Eukaryot Microbiol. 2016;63:823–33.
Perrone AE, Milduberger N, Fuchs AG, Bustos PL, Bua J. A functional analysis of the cyclophilin repertoire in the protozoan parasite Trypanosoma cruzi. Biomolecules. 2018;8:132.
Zheng Z-W, Li J, Chen H, He J-L, Chen Q-W, Zhang J-H, et al. Evaluation of in vitro antileishmanial efficacy of cyclosporin A and its non-immunosuppressive derivative, dihydrocyclosporin A. Parasit Vectors. 2020;13:132.
Rascher C, Pahl A, Pecht A, Brune K, Solbach W, Bang H. Leishmania major parasites express cyclophilin isoforms with an unusual interaction with calcineurin. Biochem J. 1998;334:659–67.
Jha B, Varikuti S, Bishop N, dos Santos G, McDonald J, Sur A, et al. An effective live vaccine strain of trypanosoma cruzi prevents chagas disease in the mouse model. https://www.researchgate.net/publication/346274839_An_Effective_Live_Vaccine_Strain_Of_Trypanosoma_Cruzi_Prevents_Chagas_Disease_In_The_Mouse_Model. 2020. Accessed Oct 2020.
Bua J, Fichera L, Fuchs A, Potenza M, Dubin M, Wenger R, et al. Anti-Trypanosoma cruzi effects of cyclosporin A derivatives: possible role of a P-glycoprotein and parasite cyclophilins. Parasitology. 2008;135:217–28.
Ibrahim HM, Nishimura M, Tanaka S, Awadin W, Furuoka H, Xuan X, et al. Overproduction of Toxoplasma gondii cyclophilin-18 regulates host cell migration and enhances parasite dissemination in a CCR5-independent manner. BMC Microbiol. 2014;14:76.
Favretto F, Jiménez-Faraco E, Catucci G, Di Matteo A, Travaglini-Allocatelli C, Sadeghi SJ, et al. Evaluating the potential of non-immunosuppressive cyclosporin analogs for targeting Toxoplasma gondii cyclophilin: insights from structural studies. Protein Sci. 2024;33:e5157.
Adams B, Musiyenko A, Kumar R, Barik S. A novel class of dual-family immunophilins. J Biol Chem. 2005;280:24308–14.
High K, Joiner K, Handschumacher R. Isolation, cDNA sequences, and biochemical characterization of the major cyclosporin-binding proteins of Toxoplasma gondii. J Biol Chem. 1994;269:9105–12.
Mineo TWP, Oliveira CJF, Silva DAO, Oliveira LL, Abatepaulo AR, Ribeiro DP, et al. Neospora caninum excreted/secreted antigens trigger CC-chemokine receptor 5-dependent cell migration. Int J Parasitol. 2010;40:797–805.
Berriman M, Fairlamb AH. Detailed characterization of a cyclophilin from the human malaria parasite Plasmodium falciparum. Biochem J. 1998;334:437–45.
Bianchin A, Chubb AJ, Bell A. Immunophilins as possible drug targets in apicomplexan parasites. Compr Anal Parasite Biol: Metab Drug Discov: Metab Drug Discov. 2016. https://doi.org/10.1002/9783527694082.ch8.
Leneghan D, Bell A. Immunophilin–protein interactions in Plasmodium falciparum. Parasitology. 2015;142:1404–14.
Zhao S, Liu J, Guan G, Liu A, Li Y, Yin H, et al. Theileria annulata Cyclophilin1 (TaCyp1) interacts with host cell MED21. Front Microbiol. 2018;9:2973.
Marín-Menéndez A, Bell A. Overexpression, purification and assessment of cyclosporin binding of a family of cyclophilins and cyclophilin-like proteins of the human malarial parasite Plasmodium falciparum. Protein Expr Purif. 2011;78:225–34.
Marín-Menéndez A, Monaghan P, Bell A. A family of cyclophilin-like molecular chaperones in Plasmodium falciparum. Mol Biochem Parasitol. 2012;184:44–7.
Bell A, Monaghan P, Page AP. Peptidyl-prolyl cis–trans isomerases (immunophilins) and their roles in parasite biochemistry, host–parasite interaction and antiparasitic drug action. Int J Parasitol. 2006;36:261–76.
Acharya P, Kumar R, Tatu U. Chaperoning a cellular upheaval in malaria: heat shock proteins in Plasmodium falciparum. Mol Biochem Parasitol. 2007;153:85–94.
Krücken J, Greif G, von Samson-Himmelstjerna G. In silico analysis of the cyclophilin repertoire of apicomplexan parasites. Parasit Vectors. 2009;2:27.
Mok S, Ashley EA, Ferreira PE, Zhu L, Lin Z, Yeo T, et al. Population transcriptomics of human malaria parasites reveals the mechanism of artemisinin resistance. Science. 2015;347:431–5.
Vance N. Quantification of Plasmodium falciparum Cyclophilin 19B transcripts via qPCR in normal and sickle-trait hemoglobin genotypes. Durham: Duke University; 2021.
Ibrahim HM, Bannai H, Xuan X, Nishikawa Y. Toxoplasma gondii cyclophilin 18-mediated production of nitric oxide induces bradyzoite conversion in a CCR5-dependent manner. Infect Immun. 2009;77:3686–95.
Ibrahim HM, Xuan X, Nishikawa Y. Toxoplasma gondii cyclophilin 18 regulates the proliferation and migration of murine macrophages and spleen cells. Clin Vaccine Immunol. 2010;17:1322–9.
Aliberti J, Valenzuela JG, Carruthers VB, Hieny S, Andersen J, Charest H, et al. Molecular mimicry of a CCR5 binding-domain in the microbial activation of dendritic cells. Nat Immunol. 2003;4:485–90.
Del Rio L, Butcher BA, Bennouna S, Hieny S, Sher A, Denkers EY. Toxoplasma gondii triggers myeloid differentiation factor 88-dependent IL-12 and chemokine ligand 2 (monocyte chemoattractant protein 1) responses using distinct parasite molecules and host receptors. J Immunol. 2004;172:6954–60.
Denkers EY. From cells to signaling cascades: manipulation of innate immunity by Toxoplasma gondii. FEMS Immunol Med Microbiol. 2003;39:193–203.
Golding H, Aliberti J, King LR, Manischewitz J, Andersen J, Valenzuela J, et al. Inhibition of HIV-1 infection by a CCR5-binding cyclophilin from Toxoplasma gondii. Blood. 2003;102:3280–6.
Sassi A, Brichacek B, Hieny S, Yarovinsky F, Golding H, Grivel J-C, et al. Toxoplasma gondii inhibits R5 HIV-1 replication in human lymphoid tissues ex vivo. Microbes Infect. 2009;11:1106–13.
Carey KL, Donahue CG, Ward GE. Identification and molecular characterization of GRA8, a novel, proline-rich, dense granule protein of Toxoplasma gondii. Mol Biochem Parasitol. 2000;105:25–37.
Ying Z, Wu Y, Sun Z, Liu J, Liu Q. The cyclophilin D (CypD) of Toxoplasma gondii is involved in the parasite’s response to oxidative stress damage. Parasitol Res. 2024;123:1–13.
Dos Santos GP, Abukawa FM, Souza-Melo N, Alcântara LM, Bittencourt-Cunha P, Moraes CB, et al. Cyclophilin 19 secreted in the host cell cytosol by Trypanosoma cruzi promotes ROS production required for parasite growth. Cell Microbiol. 2021;23:e13295.
Rêgo JV, Duarte AP, Liarte DB, de Carvalho SF, Barreto HM, Bua J, et al. Molecular characterization of cyclophilin (TcCyP19) in Trypanosoma cruzi populations susceptible and resistant to benznidazole. Exp Parasitol. 2015;148:73–80.
Perrone AE, Pinillo M, Rial MS, Fernández M, Milduberger N, González C, et al. Trypanosoma cruzi secreted cyclophilin Tc CyP19 as an early marker for trypanocidal treatment efficiency. Int J Mol Sci. 2023;24:11875.
Estrada D, Specker G, Martínez A, Dias PP, Hissa B, Andrade LO, et al. Cardiomyocyte diffusible redox mediators control Trypanosoma cruzi infection: role of parasite mitochondrial iron superoxide dismutase. Biochem J. 2018;475:1235–51.
Jha BK, Varikuti S, Verma C, Shivahare R, Bishop N, Dos Santos GP, et al. Immunization with a Trypanosoma cruzi cyclophilin-19 deletion mutant protects against acute Chagas disease in mice. NPJ Vaccines. 2023;8:63.
Rassi JA, Marin JA, Rassi A. Chronic Chagas cardiomyopathy: a review of the main pathogenic mechanisms and the efficacy of aetiological treatment following the BENznidazole Evaluation for Interrupting Trypanosomiasis (BENEFIT) trial. Mem Inst Oswaldo Cruz. 2017;112:224–35.
Bakhtiyari M, Haji Aghasi A, Banihashemi S, Abbassioun A, Tavakol C, Zalpoor H. CD147 and cyclophilin a: a promising potential targeted therapy for COVID-19 and associated cancer progression and chemo-resistance. Infect Agents Cancer. 2023;18:20.
Roy S, Basu S, Datta AK, Bhattacharyya D, Banerjee R, Dasgupta D. Equilibrium unfolding of cyclophilin from Leishmania donovani: characterization of intermediate states. Int J Biol Macromol. 2014;69:353–60.
Venugopal V, Datta AK, Bhattacharyya D, Dasgupta D, Banerjee R. Structure of cyclophilin from Leishmania donovani bound to cyclosporin at 2.6 Å resolution: correlation between structure and thermodynamic data. Acta Crystallogr D Biol Crystallogr. 2009;65:1187–95.
Agallou M, Athanasiou E, Samiotaki M, Panayotou G, Karagouni E. Identification of immunoreactive Leishmania infantum protein antigens to asymptomatic dog sera through combined immunoproteomics and bioinformatics analysis. PLoS ONE. 2016;11:e0149894.
Yurchenko V, Xue Z, Sherry B, Bukrinsky M. Functional analysis of Leishmania major cyclophilin. Int J Parasitol. 2008;38:633–9.
Venugopal V, Sen B, Datta AK, Banerjee R. Structure of cyclophilin from Leishmania donovani at 1.97 Å resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007;63:60–4.
Yurchenko V, Constant S, Eisenmesser E, Bukrinsky M. Cyclophilin–CD147 interactions: a new target for anti-inflammatory therapeutics. Clin Exp Immunol. 2010;160:305–17.
Afrin F, Khan I, Hemeg HA. Leishmania-host interactions—An epigenetic paradigm. Front Immunol. 2019;10:492.
Sen B, Venugopal V, Chakraborty A, Datta R, Dolai S, Banerjee R, et al. Amino acid residues of Leishmania donovani cyclophilin key to interaction with its adenosine kinase: biological implications. Biochemistry. 2007;46:7832–43.
Dhanda AS, Lulic KT, Vogl AW, Mc Gee MM, Chiu RH, Guttman JA. Listeria membrane protrusion collapse: requirement of cyclophilin A for Listeria cell-to-cell spreading. J Infect Dis. 2019;219:145–53.
Dhanda AS, Warren KE, Chiu RH, Guttman JA. Cyclophilin A controls Salmonella internalization levels and is present at E. coli actin-rich pedestals. Anat Rec. 2018;301:2086–94.
Dimou M, Venieraki A, Katinakis P. Microbial cyclophilins: specialized functions in virulence and beyond. World J Microbiol Biotechnol. 2017;33:164.
Floudas A, Cluxton CD, Fahel J, Khan AR, Saunders SP, Amu S, et al. Composition of the Schistosoma mansoni worm secretome: identification of immune modulatory cyclophilin A. PLoS Negl Trop Dis. 2017;11:e0006012.
Li J, Zhuang W, Cong L, Shi W, Cai X, Huang F, et al. Cyclophilin A from Schistosoma japonicum promotes a Th2 response in mice. Parasit Vectors. 2013;6:330.
Marin-Menendez A, Bell A. Identification and characterization of novel Plasmodium falciparum cyclophilins and their roles in the antimalarial actions of cyclosporin A and derivatives. Malar J. 2010;9:O3.
Allman WR, Dey R, Liu L, Siddiqui S, Coleman AS, Bhattacharya P, et al. TACI deficiency leads to alternatively activated macrophage phenotype and susceptibility to Leishmania infection. Proc Natl Acad Sci U S A. 2015;112:E4094–103.
Yun C, Lillehoj H, Lillehoj E. Intestinal immune responses to coccidiosis. Dev Comp Immunol. 2000;24:303–24.
Maeda H, Boldbaatar D, Kusakisako K, Galay RL, Aung KM, Umemiya-Shirafuji R, et al. Inhibitory effect of cyclophilin A from the hard tick Haemaphysalis longicornis on the growth of Babesia bovis and Babesia bigemina. Parasitol Res. 2013;112:2207–13.
Milduberger N, Bustos PL, González C, Perrone AE, Postan M, Bua J. Trypanosoma cruzi infection in cyclophilin D deficient mice. Exp Parasitol. 2021;220:108044.
Hoerauf A, Rascher C, Bang R, Pahl A, Solbach W, Brune K, et al. Host-cell cyclophilin is important for the intracellular replication of Leishmania major. Mol Microbiol. 1997;24:421–9.
Nigro P, Pompilio G, Capogrossi M. Cyclophilin A: a key player for human disease. Cell Death Dis. 2013;4:e888.
Luban J, Bossolt KL, Franke EK, Kalpana GV, Goff SP. Human immunodeficiency virus type 1 Gag protein binds to cyclophilins A and B. Cell. 1993;73:1067–78.
Bukrinsky MI. Cyclophilins: unexpected messengers in intercellular communications. Trends Immunol. 2002;23:323–5.
Thakur A, Mikkelsen H, Jungersen G. Intracellular pathogens: host immunity and microbial persistence strategies. J Immunol Res. 2019;2019:1356540.
Schor S, Einav S. Combating intracellular pathogens with repurposed host-targeted drugs. ACS Infect Dis. 2018;4:88–92.
Jin S, Zhang M, Qiao X. Cyclophilin A: promising target in cancer therapy. Cancer Biol Ther. 2024;25:2425127.
Williams PD, Owens CR, Dziegielewski J, Moskaluk CA, Read PW, Larner JM, et al. Cyclophilin B expression is associated with in vitro radioresistance and clinical outcome after radiotherapy. Neoplasia. 2011;13:1122–31.
Motawea KR, Elhalag RH, Rouzan SS, Talat NE, Reyad SM, Chébl P, et al. Cyclophilin c as a novel diagnostic and prognostic biomarker of coronary artery diseases. a systematic review and meta-analysis. Curr Probl Cardiol. 2023;48:101812.
Yao Q, Li M, Yang H, Chai H, Fisher W, Chen C. Roles of cyclophilins in cancers and other organ systems. World J Surg. 2005;29:276–80.
Zhang L, Liu Y, Zhou R, He B, Wang W, Zhang B. Cyclophilin d: guardian or executioner for tumor cells? Front Oncol. 2022;12:939588.
Piao M, Lee SH, Li Y, Choi J-K, Yeo C-Y, Lee KY. Cyclophilin E (CypE) functions as a positive regulator in osteoblast differentiation by regulating the transcriptional activity of Runx2. Cells. 2023;12:2549.
Ure DR, Trepanier DJ, Mayo PR, Foster RT. Cyclophilin inhibition as a potential treatment for nonalcoholic steatohepatitis (NASH). Expert Opin Investig Drugs. 2020;29:163–78.
Rajan S, Yoon HS. Structural insights into plasmodium PPIases. Front Cell Infect Microbiol. 2022;12:931635.
Clipstone NA, Crabtree GR. Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation. Nature. 1992;357:695–7.
Jin L, Harrison SC. Crystal structure of human calcineurin complexed with cyclosporin A and human cyclophilin. Proc Natl Acad Sci U S A. 2002;99:13522–6.
Stauffer WT, Goodman AZ, Gallay PA. Cyclophilin inhibition as a strategy for the treatment of human disease. Front Pharmacol. 2024;15:1417945.
Potenza M, Galat A, Minning T, Ruiz A, Duran R, Tarleton R, et al. Analysis of the Trypanosoma cruzi cyclophilin gene family and identification of Cyclosporin A binding proteins. Parasitology. 2006;132:867–82.
Liu C, von Brunn A, Zhu D. Cyclophilin A and CD147: novel therapeutic targets for the treatment of COVID-19. Med Drug Discov. 2020;7:100056.
Gavigan CS, Kiely SP, Hirtzlin J, Bell A. Cyclosporin-binding proteins of Plasmodium falciparum. Int J Parasitol. 2003;33:987–96.
Kucharski M, Wirjanata G, Nayak S, Boentoro J, Dziekan JM, Assisi C, et al. Short tandem repeat polymorphism in the promoter region of cyclophilin 19B drives its transcriptional upregulation and contributes to drug resistance in the malaria parasite Plasmodium falciparum. PLoS Pathog. 2023;19:e1011118.
Chaurasiya A, Kumari G, Garg S, Shoaib R, Anam Z, Joshi N, et al. Targeting artemisinin-resistant malaria by repurposing the anti-hepatitis C virus drug alisporivir. Antimicrob Agents Chemother. 2022;66:e00392–22.
Prakash P, Zeeshan M, Saini E, Muneer A, Khurana S, Kumar Chourasia B, et al. Human cyclophilin B forms part of a multi-protein complex during erythrocyte invasion by Plasmodium falciparum. Nat Commun. 2017;8:1548.
Satchwell TJ, Wright KE, Haydn-Smith KL, Sanchez-Roman Teran F, Moura PL, Hawksworth J, et al. Genetic manipulation of cell line derived reticulocytes enables dissection of host malaria invasion requirements. Nat Commun. 2019;10:3806.
Gavigan C, Shen M, Machado S, Bell A. Influence of the Plasmodium falciparum P-glycoprotein homologue 1 (pfmdr1 gene product) on the antimalarial action of cyclosporin. J Antimicrob Chemother. 2007;59:197–203.
Reed MB, Saliba KJ, Caruana SR, Kirk K, Cowman AF. Pgh1 modulates sensitivity and resistance to multiple antimalarials in Plasmodium falciparum. Nature. 2000;403:906–9.
Carraro R, Búa J, Ruiz A, Paulino M. Modelling and study of cyclosporin A and related compounds in complexes with a Trypanosoma cruzi cyclophilin. J Mol Graph Model. 2007;26:48–61.
Morales MA, Watanabe R, Dacher M, Chafey P, Osorio y Fortéa J, Scott DA, et al. Phosphoproteome dynamics reveal heat-shock protein complexes specific to the Leishmania donovani infectious stage. Proc Natl Acad Sci USA. 2010;107:8381–6.
Morales MA, Watanabe R, Laurent C, Lenormand P, Rousselle JC, Namane A, et al. Phosphoproteomic analysis of Leishmania donovani pro-and amastigote stages. Proteomics. 2008;8:350–63.
Yau WaiLok YW, Pescher P, MacDonald A, Hem S, Zander D, Retzlaff S, et al. The Leishmania donovani chaperone cyclophilin 40 is essential for intracellular infection independent of its stage-specific phosphorylation status. Mol Microbiol. 2014;93:80–97.
Santos-Gomes G, Rodrigues A, Teixeira F, Carreira J, Alexandre-Pires G, Carvalho S, et al. Immunization with the Leishmania infantum recombinant cyclophilin protein 1 confers partial protection to subsequent parasite infection and generates specific memory T cells. Vaccine. 2014;32:1247–53.
Yu Q, Huang X, Gong P, Zhang Q, Li J, Zhang G, et al. Protective immunity induced by a recombinant BCG vaccine encoding the cyclophilin gene of Toxoplasma gondii. Vaccine. 2013;31:6065–71.
Gong P, Huang X, Yu Q, Li Y, Huang J, Li J, et al. The protective effect of a DNA vaccine encoding the Toxoplasma gondii cyclophilin gene in BALB/c mice. Parasite Immunol. 2013;35:140–6.
Watanabe Costa R, da Silveira JF, Bahia D. Interactions between Trypanosoma cruzi secreted proteins and host cell signaling pathways. Front Microbiol. 2016;7:388.
Tuo W, Feng X, Cao L, Vinyard B, Dubey J, Fetterer R, et al. Vaccination with Neospora caninum-cyclophilin and-profilin confers partial protection against experimental neosporosis-induced abortion in sheep. Vaccine. 2021;39:4534–44.
Fereig RM, Abdelbaky HH, Kuroda Y, Nishikawa Y. Critical role of TLR2 in triggering protective immunity with cyclophilin entrapped in oligomannose-coated liposomes against Neospora caninum infection in mice. Vaccine. 2019;37:937–44.
Liu J, Farmer JD, Lane WS, Friedman J, Weissman I, Schreiber SL. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell. 1991;66:807–15.
Singh B, Varikuti S, Halsey G, Volpedo G, Hamza OM, Satoskar AR. Host-directed therapies for parasitic diseases. Future Med Chem. 2019;11:1999–2018.
Su L-H, Lee GA, Huang Y-C, Chen Y-H, Sun C-H. Neomycin and puromycin affect gene expression in Giardia lamblia stable transfection. Mol Biochem Parasitol. 2007;156:124–35.
Chatellard-Gruaz D, Saurat J-H, Siegenthaler G. Differential expression of cyclophilin isoforms during keratinocyte differentiation. Biochem J. 1994;303:863–7.
Matrangolo FS, Liarte DB, Andrade LC, de Melo MF, Andrade JM, Ferreira RF, et al. Comparative proteomic analysis of antimony-resistant and-susceptible Leishmania braziliensis and Leishmania infantum chagasi lines. Mol Biochem Parasitol. 2013;190:63–75.
Colebrook A, Jenkins D, Lightowlers M. Anti-parasitic effect of cyclosporin A on Echinococcus granulosus and characterization of the associated cyclophilin protein. Parasitology. 2002;125:485–93.
Ortona E, Vaccari S, Margutti P, Delunardo F, Rigano R, Profumo E, et al. Immunological characterization of Echinococcus granulosus cyclophilin, an allergen reactive with IgE and IgG4 from patients with cystic echinococcosis. Clin Exp Immunol. 2002;128:124–30.
Rakshit R, Bahl A, Arunima A, Pandey S, Tripathi D. Beyond protein folding: the pleiotropic functions of PPIases in cellular processes and microbial virulence. Biochem Biophys Acta. 2025;1869:130754.
Ma Z, Zhang W, Wu Y, Zhang M, Wang L, Wang Y, et al. Cyclophilin A inhibits A549 cell oxidative stress and apoptosis by modulating the PI3K/Akt/mTOR signaling pathway. 2021. Biosci Rep. https://doi.org/10.1042/BSR20203219.
Guo Y, Jiang M, Zhao X, Gu M, Wang Z, Xu S, et al. Cyclophilin A promotes non-small cell lung cancer metastasis via p38 MAPK. Thorac Cancer. 2018;9:120–8.
Prieto JH, Fischer E, Koncarevic S, Yates J, Becker K. Large-scale differential proteome analysis in Plasmodium falciparum under drug treatment. In: Parasite Genomics Protocols. New York: Springer; 2015.
Dousti M, Manzano-Román R, Rashidi S, Barzegar G, Ahmadpour NB, Mohammadi A, et al. A proteomic glimpse into the effect of antimalarial drugs on Plasmodium falciparum proteome towards highlighting possible therapeutic targets. Pathog Dis. 2021;79:ftaa071.
Lopes KF, Freire ML, Murta SMF, Oliveira E. Efficacy of vaccines based on chimeric or multiepitope antigens for protection against visceral leishmaniasis: a systematic review. PLoS Negl Trop Dis. 2024;18:e0012757.
Mortazavidehkordi N, Fallah A, Abdollahi A, Kia V, Khanahmad H, Najafabadi ZG, et al. A lentiviral vaccine expressing KMP11-HASPB fusion protein increases immune response to Leishmania major in BALB/C. Parasitol Res. 2018;117:2265–73.
Muruaga EJ, Briones G, Roset MS. Biochemical and functional characterization of Brucella abortus cyclophilins: so similar, yet so different. Front Microbiol. 2022;13:1046640.