|
|
|
| Recombinant Malaria Protein rVAR2 and Its Application in Tumor-targeted Therapy |
JIANG Jin-lu1,2,PAN Hai-feng2,3,YU Si-yuan2,3,LI Ting-dong2,3,GE Sheng-xiang2,3,**( ) |
1 School of Life Science, National Institute of Diagnostics and Vaccine Development in Infectious Disease, Xiamen University, Xiamen 361102, China
2 Department of Laboratory Medicine, School of Public Health, State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, Xiamen University, Xiamen 361102, China
3 Collaborative Innovation Center of Biological Products, Xiamen University, Xiamen 361102, China |
|
|
|
Abstract Malignant tumor is considered to be one of the main causes of human death, and its morbidity and mortality are increasing by years. Tumor-targeted drugs can act precisely on tumors and have gained a lot of attention in recent years. Specific identification and extensive binding to tumor cells are key to achieving tumor-targeted therapy, and the lack of effective and specific pan-tumor targeting tools has greatly limited the further development of tumor-targeted therapy. Compared with existing tumor targeting approaches, Plasmodium recombinant protein rVAR2 can specifically bind Oncofetal chondroitin sulfate (ofCS), which is widely expressed on the surface of tumor cells, and has the advantage of pan-tumor targeting, providing a new idea for tumor targeting therapy. In this paper, we analyze and summarize the characteristics of rVAR2 and its progress in tumor-targeted therapy in recent years, and discuss its future development direction, in order to provide a reference for the development of clinical tumor-targeted therapy and diagnosis methods.
|
|
Received: 03 January 2023
Published: 04 July 2023
|
|
|
|
|
| [1] |
Sung H, Ferlay J, Siegel R L, et al. Global cancer statistics 2020: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. CA: A Cancer Journal for Clinicians, 2021, 71(3): 209-249.
doi: 10.3322/caac.21660
pmid: 33538338
|
|
|
| [2] |
McKnight J A. Principles of chemotherapy. Clinical Techniques in Small Animal Practice, 2003, 18(2): 67-72.
pmid: 12831063
|
|
|
| [3] |
Tosti A, Piraccini B M, Vincenzi C, et al. Permanent alopecia after busulfan chemotherapy. British Journal of Dermatology, 2005, 152(5): 1056-1058.
pmid: 15888171
|
|
|
| [4] |
Ray J, Mahmood A, Dogar M, et al. Simultaneous cardiotoxicity and neurotoxicity associated with 5-fluorouracil containing chemotherapy: a case report and literature review. American Journal of Medical Case Reports, 2020, 8(3): 73-75.
pmid: 32149185
|
|
|
| [5] |
Krukiewicz K, Zak J K. Biomaterial-based regional chemotherapy: local anticancer drug delivery to enhance chemotherapy and minimize its side-effects. Materials Science and Engineering: C, 2016, 62: 927-942.
doi: 10.1016/j.msec.2016.01.063
|
|
|
| [6] |
Shadidi M, Sioud M. Selective targeting of cancer cells using synthetic peptides. Drug Resistance Updates, 2003, 6(6): 363-371.
pmid: 14744500
|
|
|
| [7] |
Alshaer W, Hillaireau H, Fattal E. Aptamer-guided nanomedicines for anticancer drug delivery. Advanced Drug Delivery Reviews, 2018, 134: 122-137.
doi: S0169-409X(18)30247-3
pmid: 30267743
|
|
|
| [8] |
Yoo J, Park C, Yi G, et al. Active targeting strategies using biological ligands for nanoparticle drug delivery systems. Cancers, 2019, 11(5): 640.
doi: 10.3390/cancers11050640
|
|
|
| [9] |
Kutova O, Guryev E, Sokolova E, et al. Targeted delivery to tumors: multidirectional strategies to improve treatment efficiency. Cancers, 2019, 11(1): 68.
doi: 10.3390/cancers11010068
|
|
|
| [10] |
Liu X S, Jiang J H, Ji Y, et al. Targeted drug delivery using iRGD peptide for solid cancer treatment. Molecular Systems Design & Engineering, 2017, 2(4): 370-379.
|
|
|
| [11] |
Patel A, Sant S. Hypoxic tumor microenvironment: opportunities to develop targeted therapies. Biotechnology Advances, 2016, 34(5): 803-812.
doi: S0734-9750(16)30048-9
pmid: 27143654
|
|
|
| [12] |
Lim Z F, Ma P C. Emerging insights of tumor heterogeneity and drug resistance mechanisms in lung cancer targeted therapy. Journal of Hematology & Oncology, 2019, 12(1): 1-18.
|
|
|
| [13] |
Marusyk A, Janiszewska M, Polyak K. Intratumor heterogeneity: the Rosetta stone of therapy resistance. Cancer Cell, 2020, 37(4): 471-484.
doi: S1535-6108(20)30147-1
pmid: 32289271
|
|
|
| [14] |
Agerbæk M Ø, Bang-Christensen S, Salanti A. Fighting cancer using an oncofetal glycosaminoglycan-binding protein from malaria parasites. Trends in Parasitology, 2019, 35(3): 178-181.
doi: S1471-4922(18)30242-3
pmid: 30551869
|
|
|
| [15] |
Fried M, Duffy P E. Adherence of Plasmodium falciparum to chondroitin sulfate A in the human placenta. Science, 1996, 272(5267): 1502-1504.
doi: 10.1126/science.272.5267.1502
pmid: 8633247
|
|
|
| [16] |
Salanti A, Dahlbäck M, Turner L, et al. Evidence for the involvement of VAR2CSA in pregnancy-associated malaria. Journal of Experimental Medicine, 2004, 200(9): 1197-1203.
doi: 10.1084/jem.20041579
pmid: 15520249
|
|
|
| [17] |
Khunrae P, Higgins M. Structural insights into chondroitin sulfate binding in pregnancy-associated malaria. Biochemical Society Transactions, 2010, 38(5): 1337-1341.
doi: 10.1042/BST0381337
pmid: 20863310
|
|
|
| [18] |
Shulman C E, Graham W J, Jilo H, et al. Malaria is an important cause of anaemia in Primigravidae: evidence from a district hospital in coastal Kenya. Transactions of the Royal Society of Tropical Medicine and Hygiene, 1996, 90(5): 535-539.
doi: 10.1016/s0035-9203(96)90312-0
pmid: 8944266
|
|
|
| [19] |
Verhoeff F H, Brabin B J, Chimsuku L, et al. An analysis of the determinants of anaemia in pregnant women in rural Malawi:a basis for action. Annals of Tropical Medicine & Parasitology, 1999, 93(2): 119-133.
|
|
|
| [20] |
Desai M, ter Kuile F O, Nosten F, et al. Epidemiology and burden of malaria in pregnancy. The Lancet Infectious Diseases, 2007, 7(2): 93-104.
doi: 10.1016/S1473-3099(07)70021-X
|
|
|
| [21] |
Akuze J, Blencowe H, Waiswa P, et al. Randomised comparison of two household survey modules for measuring stillbirths and neonatal deaths in five countries: the Every Newborn-INDEPTH study. The Lancet Global Health, 2020, 8(4): e555-e566.
doi: 10.1016/S2214-109X(20)30044-9
|
|
|
| [22] |
Clausen T M, Christoffersen S, Dahlbäck M, et al. Structural and functional insight into how the Plasmodium falciparum VAR2CSA protein mediates binding to chondroitin sulfate A in placental malaria. Journal of Biological Chemistry, 2012, 287(28): 23332-23345.
doi: 10.1074/jbc.M112.348839
pmid: 22570492
|
|
|
| [23] |
Salanti A, Staalsoe T, Lavstsen T, et al. Selective upregulation of a single distinctly structured var gene in chondroitin sulphate A-adhering Plasmodium falciparum involved in pregnancy-associated malaria. Molecular Microbiology, 2003, 49(1): 179-191.
pmid: 12823820
|
|
|
| [24] |
Viebig N K, Gamain B, Scheidig C, et al. A single member of the Plasmodium falciparum var multigene family determines cytoadhesion to the placental receptor chondroitin sulphate A. EMBO Reports, 2005, 6(8): 775-781.
doi: 10.1038/sj.embor.7400466
|
|
|
| [25] |
Esko J D, Kimata K, Lindahl U. Proteoglycans and sulfated glycosaminoglycans: essentials of glycobiology. 2nd. New York: Cold Spring Harbor Laboratory Press, 2009.
|
|
|
| [26] |
Kawashima H, Atarashi K, Hirose M, et al. Oversulfated chondroitin/dermatan sulfates containing GlcAβ1/IdoAα1-3GalNAc(4, 6-O-disulfate) interact with L- and P-selectin and chemokines. Journal of Biological Chemistry, 2002, 277(15): 12921-12930.
doi: 10.1074/jbc.M200396200
pmid: 11821431
|
|
|
| [27] |
Asimakopoulou A, Theocharis A, Tzanakakis G, et al. The biological role of chondroitin sulfate in cancer and chondroitin-based anticancer agents. In Vivo, 2008, 22(3): 385-389.
pmid: 18610752
|
|
|
| [28] |
Zhou Z H, Karnaukhova E, Rajabi M, et al. Oversulfated chondroitin sulfate binds to chemokines and inhibits stromal cell-derived factor-1 mediated signaling in activated T cells. PLoS One, 2014, 9(4): e94402.
doi: 10.1371/journal.pone.0094402
|
|
|
| [29] |
Mizumoto S, Yamada S, Sugahara K. Molecular interactions between chondroitin-dermatan sulfate and growth factors/receptors/matrix proteins. Current Opinion in Structural Biology, 2015, 34: 35-42.
doi: 10.1016/j.sbi.2015.06.004
pmid: 26164146
|
|
|
| [30] |
Maurel P, Rauch U, Flad M, et al. Phosphacan, a chondroitin sulfate proteoglycan of brain that interacts with neurons and neural cell-adhesion molecules, is an extracellular variant of a receptor-type protein tyrosine phosphatase. Proceedings of the National Academy of Sciences of the United States of America, 1994, 91(7): 2512-2516.
|
|
|
| [31] |
Mikami T, Kitagawa H. Biosynthesis and function of chondroitin sulfate. Biochimica et Biophysica Acta (BBA) - General Subjects, 2013, 1830(10): 4719-4733.
doi: 10.1016/j.bbagen.2013.06.006
|
|
|
| [32] |
Volpi N. Chondroitin sulfate safety and quality. Molecules, 2019, 24(8): 1447.
doi: 10.3390/molecules24081447
|
|
|
| [33] |
Gama C I, Tully S E, Sotogaku N, et al. Sulfation patterns of glycosaminoglycans encode molecular recognition and activity. Nature Chemical Biology, 2006, 2(9): 467-473.
doi: 10.1038/nchembio810
pmid: 16878128
|
|
|
| [34] |
Holtan S G, Creedon D J, Haluska P, et al. Cancer and pregnancy: parallels in growth, invasion, and immune modulation and implications for cancer therapeutic agents. Mayo Clinic Proceedings, 2009, 84(11): 985-1000.
|
|
|
| [35] |
Ma Y L, Zhang P, Wang F, et al. The relationship between early embryo development and tumourigenesis. Journal of Cellular and Molecular Medicine, 2010, 14(12): 2697-2701.
doi: 10.1111/j.1582-4934.2010.01191.x
pmid: 21029369
|
|
|
| [36] |
Salanti A, Clausen T, Agerbæk M, et al. Targeting human cancer by a glycosaminoglycan binding malaria protein. Cancer Cell, 2015, 28(4): 500-514.
doi: S1535-6108(15)00334-7
pmid: 26461094
|
|
|
| [37] |
Bang-Christensen, Pedersen, Pereira, et al. Capture and detection of circulating glioma cells using the recombinant VAR2CSA malaria protein. Cells, 2019, 8(9): 998.
doi: 10.3390/cells8090998
|
|
|
| [38] |
Bang-Christensen S R, Katerov V, Jørgensen A M, et al. Detection of VAR2CSA-captured colorectal cancer cells from blood samples by real-time reverse transcription PCR. Cancers, 2021, 13(23): 5881.
doi: 10.3390/cancers13235881
|
|
|
| [39] |
Wang W W, Wang Z N, Yang X N, et al. The molecular mechanism of cytoadherence to placental or tumor cells through VAR2CSA from Plasmodium falciparum. Cell Discovery, 2021, 7: 94.
doi: 10.1038/s41421-021-00324-8
|
|
|
| [40] |
Xu Y Y, Shi L R, Qin Y, et al. A mutated glycosaminoglycan-binding domain functions as a novel probe to selectively target heparin-like epitopes on tumor cells. Journal of Biological Chemistry, 2022, 298(12): 102609.
doi: 10.1016/j.jbc.2022.102609
|
|
|
| [41] |
Clausen T M, Kumar G, Ibsen E K, et al. A simple method for detecting oncofetal chondroitin sulfate glycosaminoglycans in bladder cancer urine. Cell Death Discovery, 2020, 6(1): 1-7.
|
|
|
| [42] |
Zhang J Z, Sun B N, Zhang K, et al. Screening and surveillance of multiple solid tumours using plasma placental-like chondroitin sulfate A (pl-CSA). International Journal of Medical Sciences, 2020, 17(2): 161-169.
doi: 10.7150/ijms.39444
pmid: 32038099
|
|
|
| [43] |
Zhang P F, Wu Z Y, Zhang W B, et al. Establishment and validation of a plasma oncofetal chondroitin sulfated proteoglycan for pan-cancer detection. Nature Communications, 2023, 14: 645.
doi: 10.1038/s41467-023-36374-7
|
|
|
| [44] |
Clausen T M, Pereira M A, Oo H Z, et al. Real-time and label free determination of ligand binding-kinetics to primary cancer tissue specimens; a novel tool for the assessment of biomarker targeting. Sensing and Bio-Sensing Research, 2016, 9: 23-30.
pmid: 27441183
|
|
|
| [45] |
Sugahara K N, Teesalu T, Karmali P P, et al. Coadministration of a tumor-penetrating peptide enhances the efficacy of cancer drugs. Science, 2010, 328(5981): 1031-1035.
doi: 10.1126/science.1183057
pmid: 20378772
|
|
|
| [46] |
Kang S J, Lee S, Park S. iRGD peptide as a tumor-penetrating enhancer for tumor-targeted drug delivery. Polymers, 2020, 12(9): 1906.
doi: 10.3390/polym12091906
|
|
|
| [47] |
Thakkar S, Sharma D, Kalia K, et al. Tumor microenvironment targeted nanotherapeutics for cancer therapy and diagnosis: a review. Acta Biomaterialia, 2020, 101: 43-68.
doi: S1742-7061(19)30621-X
pmid: 31518706
|
|
|
| [48] |
Davoodi Z, Shafiee F. Internalizing RGD, a great motif for targeted peptide and protein delivery: a review article. Drug Delivery and Translational Research, 2022, 12(10): 2261-2274.
doi: 10.1007/s13346-022-01116-7
pmid: 35015253
|
|
|
| [49] |
Kim S, Bell K, Mousa S A, et al. Regulation of angiogenesis in vivo by ligation of integrin alpha5beta 1 with the central cell-binding domain of fibronectin. The American Journal of Pathology, 2000, 156(4): 1345-1362.
doi: 10.1016/S0002-9440(10)65005-5
|
|
|
| [50] |
Birrer M J, Moore K N, Betella I, et al. Antibody-drug conjugate-based therapeutics: state of the science. JNCI: Journal of the National Cancer Institute, 2019, 111(6): 538-549.
doi: 10.1093/jnci/djz035
|
|
|
| [51] |
Du J Z, Sun T M, Song W J, et al. A tumor-acidity-activated charge-conversional nanogel as an intelligent vehicle for promoted tumoral-cell uptake and drug delivery. Angewandte Chemie International Edition, 2010, 49(21): 3621-3626.
|
|
|
| [52] |
Im S, Lee J, Park D, et al. Hypoxia-triggered transforming immunomodulator for cancer immunotherapy via photodynamically enhanced antigen presentation of dendritic cell. ACS Nano, 2019, 13(1): 476-488.
doi: 10.1021/acsnano.8b07045
pmid: 30563320
|
|
|
| [53] |
Xiao Y, Yu D H. Tumor microenvironment as a therapeutic target in cancer. Pharmacology & Therapeutics, 2021, 221: 107753.
|
|
|
| [54] |
Duo Y H, Yang M, Du Z Y, et al. CX-5461-loaded nucleolus-targeting nanoplatform for cancer therapy through induction of pro-death autophagy. Acta Biomaterialia, 2018, 79: 317-330.
doi: S1742-7061(18)30502-6
pmid: 30172068
|
|
|
| [55] |
He X, Chen X L, Liu L S, et al. Sequentially triggered nanoparticles with tumor penetration and intelligent drug release for pancreatic cancer therapy. Advanced Science, 2018, 5(5): 1701070.
doi: 10.1002/advs.v5.5
|
|
|
| [56] |
Xie S T, Wang Z M, Fu T, et al. Engineering aptamers with selectively enhanced biostability in the tumor microenvironment. Angewandte Chemie International Edition, 2022, 61(31): e202201220.
|
|
|
| [57] |
Wang C K, Nelepcu I, Hui D, et al. Internalization and trafficking of CSPG-bound recombinant VAR2CSA lectins in cancer cells. Scientific Reports, 2022, 12: 3075.
doi: 10.1038/s41598-022-07025-6
pmid: 35197518
|
|
|
| [58] |
Seiler R, Oo H Z, Tortora D, et al. An oncofetal glycosaminoglycan modification provides therapeutic access to cisplatin-resistant bladder cancer. European Urology, 2017, 72(1): 142-150.
doi: S0302-2838(17)30232-4
pmid: 28408175
|
|
|
| [59] |
Oo H Z, Lohinai Z, Khazamipour N, et al. Oncofetal chondroitin sulfate is a highly expressed therapeutic target in non-small cell lung cancer. Cancers, 2021, 13(17): 4489.
doi: 10.3390/cancers13174489
|
|
|
| [60] |
Middelburg J, Kemper K, Engelberts P, et al. Overcoming challenges for CD3-bispecific antibody therapy in solid tumors. Cancers, 2021, 13(2): 287.
doi: 10.3390/cancers13020287
|
|
|
| [61] |
Nordmaj M A, Roberts M E, Sachse E S, et al. Development of a bispecific immune engager using a recombinant malaria protein. Cell Death & Disease, 2021, 12(4): 353.
|
|
|
| [62] |
Zhou M, Lai W J, Li G B, et al. Platelet membrane-coated and VAR2CSA malaria protein-functionalized nanoparticles for targeted treatment of primary and metastatic cancer. ACS Applied Materials & Interfaces, 2021, 13(22): 25635-25648.
|
|
|
| [63] |
Clausen T M, Pereira M A, Al Nakouzi N, et al. Oncofetal chondroitin sulfate glycosaminoglycans are key players in integrin signaling and tumor cell motility. Mol Cancer Res, 2016, 14(12): 1288-1299.
pmid: 27655130
|
|
|
| [64] |
Yu S Y, Yang H, Li T D, et al. Efficient intracellular delivery of proteins by a multifunctional chimaeric peptide in vitro and in vivo. Nature Communications, 2021, 12: 5131.
doi: 10.1038/s41467-021-25448-z
|
|
|
|
Viewed |
|
|
|
Full text
|
|
|
|
|
Abstract
|
|
|
|
|
Cited |
|
|
|
|
| |
Shared |
|
|
|
|
| |
Discussed |
|
|
|
|
