1. ICTV Taxonomy history: Bovine leukemia virus. International Committee on Taxonomy of Viruses (ICTV). (https://talk.ictvonline.org/taxonomy/, accessed on 2021, November, 5).
2. Sagata, N., Yasunaga, T., Tsuzuku-Kawamura, J., Ohishi, K., Ogawa, Y. and Ikawa, Y. (1985). Complete nucleotide sequence of the genome of bovine leukemia virus: its evolutionary relationship to other retroviruses. Proc. Natl. Acad. Sci. U.S.A. 82, 677–681.
3. Gillet, N., Florins, A., Boxus, M., Burteau, C., Nigro, A., Vandermeers, F., Balon, H., Bouzar, A. B., Defoiche, J., Burny, A., Reichert, M., Kettmann, R. and Willems, L. (2007). Mechanisms of leukemogenesis induced by bovine leukemia virus: Prospects for novel anti-retroviral therapies in human. Retrovirology 4: 18.
4. Office International des Epizooties (OIE), (2018). Enzootic bovine leukosis. In manual of diagnostic tests and vaccines for terrestrial animals. OIE: Paris, France, 2018, 1113–1124. Available online: https://www.oie.int/standard-setting/ terrestrial- manual/access-online/ (accessed on 2020, August, 11).
5. Frie, M. C. and Coussens, P. M. (2015). Bovine leukemia virus: A major silent threat to proper immune responses in cattle. Vet. Immunol. Immunopathol. 163, 103– 114.
6. Miller, J. M., Miller, L. D., Olson, C. and Gillette, K. G. (1969). Virus-like particles in phytohemagglutinin-stimulated lymphocyte cultures with reference to bovine lymphosarcoma. J. Natl. Cancer Inst. 43, 1297-1305.
7. Lassauzet, M.L., Thurmond, M. C., Johnson, W. O., Stevens, F. and Picanso, J. P. (1990). Effect of brucellosis vaccination and dehorning on transmission of bovine leukemia virus in heifers on a California dairy. Canadian J. Vet. Res. 54, 184-189.
8. Meas, S., Usui T., Ohashi, K., Sugimoto, C. and Onuma, M. (2002). Vertical transmission of bovine leukemia virus and bovine immunodeficiency virus in dairy cattle herds. Vet. Microbiol. 84, 275-282.
9. Sajiki, Y., Konnai, S., Nishimori, A., Okagawa, T., Maekawa, N., Goto, S., Nagano, M., Kohara, J., Kitano, N., Takahashi, T., Tajima, M., Mekata, H., Horii, Y., Murata, S. and Ohashi, K. (2017). Intrauterine infection with bovine leukemia virus in pregnant dam with high viral load. J. Vet. Med. Sci. 79, 2036–2039.
10. Hopkins, S. G. and DiGiacomo, R.F. (1997). Natural transmission of bovine leukemia virus in dairy and beef cattle. Vet. Clin. North Am. Food Anim. 13 107-128.
11. Bech-Nielsen, S., Piper, C. E. and Ferrer, J. F. (1978). Natural mode of transmission of the bovine leukemia virus: role of blood sucking insects. Am. J. Vet. Res. 39, 1089–1092.
12. Bartlett, P. C., Sordillo, L. M., Byrem, T. M., Norby, B., Grooms, D. L., Swenson, C. L., Zalucha, J. and Erskine, R. J. (2014). Options for the control of bovine leukemia virus in dairy cattle. Am. Vet. Med. Assoc. 244, 914–922.
13. European Commission, 2017. Bovine and swine diseases situation 2017 (https://ec. europa.eu/food/system/files/2018-12/la_annual-situation_2017.pdf, accessed on 2021, October, 20).
14. Nuotio, L., Rusanen, H., Sihvonen, L. and Neuvonen, E. (2003). Eradication of enzootic bovine leukosis from Finland. Prev. Vet. Med. 59, 43–49.
15. LaDronka, R. M., Ainsworth, S., Wilkins, M. J., Norby, B., Byrem, T. M. and Bartlett, P. C. (2018). Prevalence of bovine leukemia virus antibodies in us dairy cattle. Vet. Med. Int. 2018, 5831278.
16. Yang, Y., Fan, W., Mao, Y., Yang, Z., Lu, G., Zhang, R., Zhang, H., Szeto, C. and Wang, C. (2016). Bovine leukemia virus infection in cattle of China: Association with reduced milk production and increased somatic cell score. J. Dairy Sci. 99, 3688–3697.
17. Murakami, K., Kobayashi, S., Konishi, M., Kameyama, K.-I. and Tsutsui, T. (2013). Nationwide survey of bovine leukemia virus infection among dairy and beef breeding cattle in Japan from 2009-2011. J. Vet. Med. Sci. 75, 1123–1126.
18. Beier, D., Riebe, R., Blankenstein, P., Starick, E., Bondzio, A. and Marquardt, O. (2004). Establishment of a new bovine leukosis virus producing cell line. J. Virol. Methods. 121, 239-246.
19. Jimba, M., Takeshima, S. N., Murakami, H., Kohara, j., Kobayashi, N., Matsuhashi, T., Ohmori, T., Nunoya, T. and Aida, Y. (2012). BLV CoCoMo- qPCR: A useful tool for evaluating bovine leukemia virus infection status. BMC Vet. Res. 8, 167.
20. Nishiike, M., Haoka, M., Doi, T., Kohda, T. and Mukamoto, M. (2016). Development of a preliminary diagnostic measure for bovine leukosis in dairy cows using peripheral white blood cell and lymphocyte counts. J. Vet. Med. Sci. 78, 1145– 1151.
21. Ohno, A., Takeshima, S. N., Matsumoto, Y. and Aida, Y. (2015). Risk factors associated with increased bovine leukemia virus proviral load in infected cattle in Japan from 2012 to 2014. Virus Res. 210, 283–290.
22. Ferrer, J. F. (1980). Bovine lymphosarcoma. Adv. Vet. Sci. Comp. Med. 24, 1–68.
23. Burny, A., Cleuter, Y., Kettmann, R., Mammerickx, M., Marbaix, G., Portetelle, D., van den Broeke, A., Willems, L. and Thomaset, R. (1988). Bovine leukemia: facts and hypotheses derived from the study of an infectious cancer. Vet. Microbiol. 17, 197-218.
24. Ott, S. L., Johnson, R. and Wells, S. J. (2003). Association between bovine-leukosis virus seroprevalence and herd-level productivity on US dairy farms. Prevent. Vet. Med. 61, 249-262.
25. Shaghayegh, A. R. (2019). Detection and identification of enzootic bovine leukosis (EBL) in calves in Iran. Arch. Razi Inst. 74, 321-325.
26. Emanuelson, U., Scherling, K. and Pettersson, H. (1992). Relationships between herd bovine leukemia virus infection status and reproduction, disease incidence, and productivity in Swedish dairy herds. Prevent. Vet. Med. 12, 121–131.
27. Trainin, Z., Brenner, J., Meirom, R. and Ungar-Waron, H. (1996). Detrimental effect of bovine leukemia virus (BLV) on the immunological state of cattle. Vet. Immunol. Immunopathol. 54, 293–302.
28. Watanabe, A., Murakami, H., Kakinuma, S., Murao, K., Ohmae, K., Isobe, N., Akamatsu, H., Seto, T., Hashimura, S., Konda, K., Shinozuka, Y. and Kawai, K. (2019). Association between bovine leukemia virus proviral load and severity of clinical mastitis. J. Vet. Med. Sci. 81, 1431–1437.
29. Nekouei, O., VanLeeuwen, J., Stryhn, H., Kelton, D. and Keefe, G. (2016). Lifetime effects of infection with bovine leukemia virus on longevity and milk production of dairy cows. Prev. Vet. Med. 133, 1–9.
30. Rodríguez, S. M., Florins, A., Gillet, N., de Brogniez, A., Sánchez-Alcaraz, M. T., Boxus, M., Boulanger, F., Gutiérrez, G., Trono, K., Alvarez, I., Vagnoni, L. and Willems L. (2011). Preventive and therapeutic strategies for bovine leukemia virus: Lessons for HTLV. Viruses 3, 1210-1248.
31. MAFF, 2015. Guidelines for Biosecurity Measures of Enzootic Bovine Leukosis. (www.maff.go.jp/j/syouan/douei/pdf/ebl_guide.pdf, accessed on 2017, September, 5)
32. Kobayashi, S., Tsutsui, T., Yamamoto, T., Hayama, Y., Kameyama, K., Konishi, M. and Murakami, K. (2010). Risk factors associated with within-herd transmission of bovine leukemia virus on dairy farms in Japan. BMC Vet. Res. 6, 1.
33. Kobayashi, T., Inagaki, Y., Ohnuki, N., Sato, R., Murakami, S. and Imakawa, K. (2019). Increasing bovine leukemia virus (BLV) proviral load is a risk factor for progression of enzootic bovine leucosis: a prospective study in Japan. Prev. Vet. Med. 178, 104680.
34. Kalra, H., Drummen, G. P. and Mathivanan, S. (2016). Focus on extracellular vesicles: Introducing the next small big thing. Int. J. Mol. Sci. 17, 170.
35. Gheinani, A. H., Vögeli, M., Baumgartner, U., Vassella, E., Draeger, A., Burkhard, F. C. and Monastyrskaya, k. (2018). Improved isolation strategies to increase the yield and purity of human urinary exosomes for biomarker discovery. Sci. Rep. 8, 3945.
36. Lässer, C., Alikhani, V. S., Ekström, K., Eldh, M., Paredes, P. T., Bossios, A., Sjöstrand, M., Gabrielsson, S., Lötvall, J. and Valadi, H. (2011). Human saliva, plasma and breast milk exosomes contain RNA: uptake by macrophages. J. Transl. Med. 9, 9.
37. Théry, C., Witwer, K. W., Aikawa, E., Alcaraz, M. J., Anderson, J. D., Andriantsitohaina, R., Antoniou, A., Arab, T., Archer, F., Atkin-Smith, G. K., Ayre, D. C., Bach, J. M., Bachurski, D., Baharvand, H., Balaj, L., Baldacchino, S., Bauer, N. N., Baxter, A. A., Bebawy, M., Beckham, C., Bedina Zavec, A., Benmoussa, A., Berardi, A. C., Bergese, P., Bielska, E., Blenkiron, C., Bobis- Wozowicz, S., Boilard, E., Boireau, W., Bongiovanni, A., Borràs, F. E., Bosch, S., Boulanger, C. M., Breakefield, X., Breglio, A. M., Brennan, M. Á., Brigstock, D. R., Brisson, A., Broekman, M. L., Bromberg, J. F., Bryl-Górecka, P., Buch, S., Buck, A. H., Burger, D., Busatto, S., Buschmann, D., Bussolati, B., Buzás, E. I., Byrd, J. B., Camussi, G., Carter, D. R., Caruso, S., Chamley, L. W., Chang, Y. T., Chen, C., Chen, S., Cheng, L., Chin, A. R., Clayton, A., Clerici, S. P., Cocks, A., Cocucci, E., Coffey, R. J., Cordeiro-da-Silva, A., Couch, Y., Coumans, F. A., Coyle, B., Crescitelli, R., Criado, M. F., D'Souza-Schorey, C., Das, S., Datta, Chaudhuri, A., de Candia, P., De Santana, E. F., De Wever, O., Del Portillo, H. A., Demaret, T., Deville, S., Devitt, A., Dhondt, B., Di Vizio, D., Dieterich, L. C., Dolo, V., Dominguez Rubio, A. P., Dominici, M., Dourado, M. R., Driedonks, T. A., Duarte, F. V., Duncan, H. M., Eichenberger, R. M., Ekström, K., El Andaloussi, S., Elie-Caille, C., Erdbrügger, U., Falcón-Pérez, J. M., Fatima, F., Fish, J. E., Flores-Bellver, M., Försönits, A., Frelet-Barrand, A., Fricke, F., Fuhrmann, G., Gabrielsson, S., Gámez-Valero, A., Gardiner, C., Gärtner, K., Gaudin, R., Gho, Y. S., Giebel, B., Gilbert, C., Gimona, M., Giusti, I., Goberdhan, D. C., Görgens, A., Gorski, S. M., Greening, D. W., Gross, J. C., Gualerzi, A., Gupta, G. N., Gustafson, D., Handberg, A., Haraszti, R. A., Harrison, P., Hegyesi, H., Hendrix, A., Hill, A. F., Hochberg, F. H., Hoffmann, K. F., Holder, B., Holthofer, H., Hosseinkhani, B., Hu, G., Huang, Y., Huber, V., Hunt, S., Ibrahim, A. G., Ikezu, T., Inal, J. M., Isin, M., Ivanova, A., Jackson, H. K., Jacobsen, S., Jay, S. M., Jayachandran, M., Jenster, G., Jiang, L., Johnson, S. M., Jones, J. C., Jong, A., Jovanovic-Talisman, T., Jung, S., Kalluri, R., Kano, S. I., Kaur, S., Kawamura, Y., Keller, E. T., Khamari, D., Khomyakova, E., Khvorova, A., Kierulf, P., Kim, K. P., Kislinger, T., Klingeborn, M., Klinke, D. J., Kornek, M., Kosanović, M. M., Kovács, Á. F., Krämer-Albers, E. M., Krasemann, S., Krause, M., Kurochkin, I. V., Kusuma, G. D., Kuypers, S., Laitinen, S., Langevin, S. M., Languino, L. R., Lannigan, J., Lässer, C., Laurent, L. C., Lavieu, G., Lázaro- Ibáñez, E., Le Lay, S., Lee, M. S., Lee, Y. X. F., Lemos, D. S., Lenassi, M., Leszczynska, A., Li, I. T., Liao, K., Libregts, S. F., Ligeti, E., Lim, R., Lim, S. K., Linē, A., Linnemannstöns, K., Llorente, A., Lombard, C. A., Lorenowicz, M. J., Lörincz, Á. M, Lötvall, J., Lovett, J., Lowry, M. C., Loyer, X., Lu, Q., Lukomska, B., Lunavat, T. R., Maas, S. L., Malhi, H., Marcilla, A., Mariani, J., Mariscal, J., Martens-Uzunova, E. S., Martin-Jaular, L., Martinez, M. C., Martins, V. R., Mathieu, M., Mathivanan, S., Maugeri, M., McGinnis, L. K., McVey, M. J., Meckes, D. G. Jr., Meehan, K. L., Mertens, I., Minciacchi, V. R., Möller, A., Møller Jørgensen, M., Morales-Kastresana, A., Morhayim, J., Mullier, F., Muraca, M., Musante, L., Mussack, V., Muth, D. C., Myburgh, K. H., Najrana, T., Nawaz, M., Nazarenko, I., Nejsum, P., Neri, C., Neri, T., Nieuwland, R., Nimrichter, L., Nolan, J. P., Nolte-'t Hoen, E. N., Noren Hooten, N., O'Driscoll, L., O'Grady, T., O'Loghlen, A., Ochiya, T., Olivier, M., Ortiz, A., Ortiz, L. A., Osteikoetxea, X., Østergaard, O., Ostrowski, M., Park, J, Pegtel, D. M., Peinado, H., Perut, F., Pfaffl, M. W., Phinney, D. G., Pieters, B. C., Pink, R. C., Pisetsky, D. S., Pogge von Strandmann, E., Polakovicova, I., Poon, I. K., Powell, B. H., Prada, I., Pulliam, L., Quesenberry, P., Radeghieri, A., Raffai, R. L., Raimondo, S., Rak, J., Ramirez, M. I., Raposo, G., Rayyan, M. S., Regev-Rudzki, N., Ricklefs, F. L., Robbins, P. D., Roberts, D. D., Rodrigues, S. C., Rohde, E., Rome, S., Rouschop, K. M., Rughetti, A., Russell, A. E., Saá, P., Sahoo, S., Salas-Huenuleo, E., Sánchez, C., Saugstad, J. A., Saul, M. J., Schiffelers, R. M., Schneider, R., Schøyen, T. H., Scott, A., Shahaj, E., Sharma, S., Shatnyeva, O., Shekari, F., Shelke, G. V., Shetty, A. K., Shiba, K., Siljander, P. R., Silva, A. M., Skowronek, A., Snyder, O. L., Soares, R. P., Sódar, B. W., Soekmadji, C., Sotillo, J., Stahl, P. D., Stoorvogel, W., Stott, S. L., Strasser, E. F., Swift, S., Tahara, H., Tewari, M., Timms, K., Tiwari, S., Tixeira, R., Tkach, M., Toh, W. S., Tomasini, R., Torrecilhas, A. C., Tosar, J. P., Toxavidis, V., Urbanelli, L., Vader, P., van Balkom, B. W., van der Grein, S. G., Van Deun, J., van Herwijnen, M. J., Van Keuren-Jensen, K., van Niel, G., van Royen, M. E., van Wijnen, A. J., Vasconcelos, M. H., Vechetti, I. J. Jr., Veit, T. D., Vella, L. J., Velot, É., Verweij, F. J., Vestad, B., Viñas, J. L., Visnovitz, T., Vukman, K. V., Wahlgren, J., Watson, D. C., Wauben, M. H., Weaver, A., Webber, J. P., Weber, V., Wehman, A. M., Weiss, D. J., Welsh, J. A., Wendt, S., Wheelock, A. M., Wiener, Z., Witte, L., Wolfram, J., Xagorari, A., Xander, P., Xu, J., Yan, X., Yáñez-Mó, M., Yin, H., Yuana, Y., Zappulli, V., Zarubova, J., Žėkas, V., Zhang, J. Y., Zhao, Z., Zheng, L., Zheutlin, A. R., Zickler, A. M., Zimmermann, P., Zivkovic, A. M., Zocco, D. and Zuba-Surma, E. K. (2018). Minimal information for studies of extracellular vesicles 2018 (MISEV2018): A position statement of the International Society for Extracellular Vesicles and update of the MISEV2014 guidelines. J. Extracell. Vesicles 7, 1535750.
38. Pap, E., Ṕallinger, É., Ṕasztói, M. and Falus, A. (2009). Highlights of a new type of intercellular communication: microvesicle-based information transfer. J. Inflamm. Res. 58, 1–8.
39. Valadi, H., Ekström, K., Bossios, A., Sjöstrand, M., Lee, J. J. and Lötvall, J. O. (2007). Exosome-mediated transfer of mRNAs and microRNAs is a novel mechanism of genetic exchange between cells. Nature Cell Biol. 9, 654–659.
40. Luga, V., Zhang, L., Viloria-Petit, A. M., Ogunjimi, A. A., Inanlou, M. R., Chiu, E., Buchanan, M., Hosein, A. N., Basik, M. and Wrana, J. L. (2012). Exosomes mediate stromal mobilization of autocrine WNT-PCP signaling in breast cancer cell migration. Cell 151, 1542–1566.
41. Gould, S. J. and Raposo, G. (2013). As we wait: Coping with an imperfect nomenclature for extracellular vesicles. J. Extracell. Vesicles 2, 20389.
42. Haug, A., Hostmark, A. T. and Harstad, O. M. (2007). Bovine milk in human nutrition. A review. Lipids Health Dis. 6, 25.
43. Hata, T., Murakami, K., Nakatani, H., Yamamoto, Y., Matsuda, T. and Aoki, N. (2010). Isolation of bovine milk-derived microvesicles carrying mRNAs and microRNAs. Biochem. Biophys. Res. Commun. 396, 528–533.
44. Izumi, H., Kosaka, N., Shimizu, T., Sekine, K., Ochiya, T. and Takase, M. (2012). Bovine milk contains microRNA and messenger RNA that are stable under degradative conditions. J. Dairy Sci. 95, 4831–4841.
45. Reinhardt, T. A., Lippolis, J. D., Nonnecke, B. J. and Sacco R. E. (2012). Bovine milk exosome proteome. J. Proteom. 75, 1486–1492.
46. Sanwlani, R., Fonseka Chitti, P. S. V. and Mathivanan, S. (2020). Milk-derived extracellular vesicles in inter-organism, cross-species communication and drug delivery. Proteomes 8, 11.
47. Samuel, M., Chisanga, D., Liem, M., Keerthikumar, S., Anand, S., Ang, C-S., Adda, C. G., Versteegen, E., Jois, M. and Mathivanan S. (2017). Bovine milk-derived exosomes from colostrum are enriched with proteins implicated in immune response and growth. Sci. Rep. 7, 5933.
48. Donnet-Hughes, A., Duc, N., Serrant, P., Vidal, K. and Schiffrin, E. (2000). Bioactive molecules in milk and their role in health and disease: The role of transforming growth factor-β. Immunol. Cell Biol. 78, 74–79.
49. Crookenden, M. A., Walker, C. G., Peiris, H., Koh, Y., Heiser, A., Loor, J. J., Moyes, K. M., Murray, A., Dukkipati, V. S. R., Kay, J. K., Meier, S., Roche, J. R. and Mitchell, M. D. (2016). Proteins from circulating exosomes represent metabolic state in transition dairy cows. J. Dairy Sci. 99, 7661–7668.
50. Yamada, T., Shigemura, H., Ishiguro, N. and Inoshima, Y. (2013). Cell infectivity in relation to bovine leukemia virus gp51 and p24 in bovine milk exosomes. PLoS One 8, e77359.
51. Cai, M., He, H., Jia, X., Chen, S., Wang, J., Shi, Y., Liu, B., Xiao, W. and Lai, S. (2018). Genome-wide microRNA profiling of bovine milk-derived exosomes infected with Staphylococcus aureus. Cell Stress Chaperone. 23, 663–672.
52. Glass, E. J., Baxter, R., Leach, R. and Taylor, G. (2010). Bovine viral diseases: the role of host genetics, Chap. 6. In: Bishop, S. C., Axford, R. F. E., Nicholas, F. W., and Owen, J. B. (ed) Breeding for disease resistance in farm animals, 3rd ed. CAB International Oxfordshire, UK, 88–140.
53. Klener, P. Jr., Andera, L., Klener, P., Necas, E. and Zivný, J. (2006). Cell death signalling pathways in the pathogenesis and therapy of haematologic malignancies: overview of apoptotic pathways. Folia Biol. (Praha). 52, 34-44.
54. Polat, M., Takeshima, S-N. and Aida, Y. (2017). Epidemiology and genetic diversity of bovine leukemia virus. Virol. J. 14, 209.
55. Evermann, J. F. and Jackson, M. K. (1997). Laboratory diagnostic tests for retroviral infections in dairy and beef cattle. Vet. Clin. North Am. Food Anim. Pract. 13, 87–106.
56. Naif, H. M., Brandon, R. B., Daniel, R. C. W. and Lavin, M. F. (1990). Bovine leukemia proviral dna detection in cattle using the polymerase chain-reaction. Vet. Microbiol. 25, 117-129.
57. Shettigara, P. T., Samagh, B. S. and Lobinowich, E. M. (1989). Control of bovine leukemia virus infection in dairy herds by agar gel immunodiffusion test and segregation of reactors. Can. J. Vet. Res. 53, 108–110.
58. CABI, (2021). Enzootic bovine leukosis. In: Invasive species compendium. Wallingford, UK: CAB International. (https://www.cabi.org/isc, accessed on 2022, October, 25).
59. Hishamnuri, W. N. A. D., Nakagun, S., Maezawa, M., Sakaguchi, K., Akiyama, N., Watanabe, K. I., Horiuchi, N., Kobayashi, Y. and Inokuma, H. (2019). Disseminated thymic B-cell lymphoma in a Holstein heifer. J. Vet. Diagn. Invest. 31, 852-855.
60. Benmoussaa, A., Gottib, C., Bourassab, S., Gilbert, C. and Provost, P. (2019). Identification of protein markers for extracellular vesicle (EV) subsets in cow’s milk. J. Proteom. 192, 78–88.
61. Benmoussa, A. and Provost, P. (2019). Milk MicroRNAs in health and disease. Compr. Rev. Food Sci. Food Saf. 18, 703–722.
62. Izumi, H., Tsuda, M., Sato, Y., Kosaka, N., Ochiya, T., Iwamoto, H., Namba, K. and Takeda, Y. (2015). Bovine milk exosomes contain microRNA and mRNA and are taken up by human macrophages. J. Dairy Sci. 98, 2920-2933.
63. McMahon, D. J. and Oommen, B. S. (2008). Supramolecular structure of the casein micelle. J. Dairy Sci. 91, 1709–1721.
64. Lönnerdal, B. (2003). Nutritional and physiologic significance of human milk proteins. Am. J. Clin. Nutr. 77, 1537S-1543S.
65. Van der Pol, E., Coumans, F. A., Grootemaat, A. E., Gardiner, C., Sargent, I. L., Harrison, P., Sturk, A., van Leeuwen, T. G. and Nieuwland, R. (2014). Particle size distribution of exosomes and microvesicles determined by transmission electron microscopy, flow cytometry, nanoparticle tracking analysis, and resistive pulse sensing. J. Thromb. Haemost. 12, 1182–1192.
66. Webber, J. and Clayton, A. (2013). How pure are your vesicles? J. Extracell. Vesicles 2, 1–6.
67. Yamada, T., Inoshima, Y., Matsuda, T. and Ishiguro, N. (2012). Comparison of methods for isolating exosomes from bovine milk. J. Vet. Med. Sci. 74, 1523– 1525.
68. Ban, J. J., Lee, M., Im, W. and Kim, M. (2015). Low pH increases the yield of exosome isolation. Biochem. Biophys. Res. Commun. 461, 76–79.
69. Somiya, M., Yoshioka, Y. and Ochiya T. (2018). Biocompatibility of highly purified bovine milk derived extracellular vesicles. J. Extracell. Vesicles 7, 1440132.
70. Yamauchi, M., Shimizu, K., Rahman, M., Ishikawa, H., Takase, H., Ugawa, S., Okada, A. and Inoshima Y. (2019). Efficient method for isolation of exosomes from raw bovine milk. Drug Dev. Ind. Pharm. 45, 359-364.
71. Schacterle, G. R. and Pollack, R. L. A. (1973). simplified method for the quantitative assay of small amounts of protein in biologic material. Anal. Biochem. 51, 654– 655.
72. Vaswani, K., Koh, Y. Q., Almughlliq, F. B., Peiris, H. N. and Mitchell, M. D. (2015). A method for the isolation and enrichment of purified bovine milk exosomes. Reprod. Biol. 17, 341-348.
73. Schwartz, I. and Levy, D. (1994). Pathobiology of bovine leukemia virus. Vet. Res. 25, 521-536.
74. Brym, P. and Kamiński, S. (2016). Microarray analysis of differential gene expression profiles in blood cells of naturally BLV-infected and uninfected Holstein- Friesian cows. Mol. Biol. Rep. 44, 109–127.
75. Cha, B. S., Park, K. S. and Park, J. S. (2020). Signature mRNA markers in extracellular vesicles for the accurate diagnosis of colorectal cancer. J. Biol. Eng. 14, 4.
76. Fechner, H., Blankenstein, P., Looman, A.C., Elwert, J., Geue, L., Albrecht, C., Kurg, A., Beier, D., Marquardt, O. and Ebner, D. (1997). Provirus variants of the bovine leukemia virus and their relation to the serological status of naturally infected cattle. Virology 237, 261–269.
77. Murakami, K.; Okada, K.; Ikawa, Y. and Aida, Y. (1994). Bovine Leukemia Virus Induces CD5- B Cell lymphoma in sheep despite temporarily increasing CD5+ B cells in asymptomatic stage. Virology 202, 458–465.
78. Smyth, G. K. (2004). Linear models and empirical bayes methods for assessing differential expression in microarray experiments. Stat. Appl. Genet. Mol. Biol. 3, 3.
79. Benjamini, Y. and Hochberg, Y. (1995). Controlling the false discovery rate: a practical and powerful approach to multiple testing. J. R. Stat. Soc. Series B 57, 289–300.
80. Kanehisa, M., Furumichi, M., Tanabe, M., Sato, Y. and Morishima, K. (2017). KEGG: new perspectives on genomes, pathways, diseases and drugs. Nucleic Acids Res. 45, D353–D361.
81. Huang, D. W., Sherman, B. T. and Lempicki, R. A. (2009). Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources. Nat. Protoc. 4, 44–57.
82. Vandesompele, J., De Preter, K., Pattyn, F., Poppe, B., Van Roy, N., De Paepe, A. and Speleman, F. (2002). Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol. 3, research0034.1–0034.11.
83. Andersen, C. L., Jensen, J. L. and Ørntoft, T. F. (2004). Normalization of real-time quantitative reverse transcription-PCR data: a model-based variance estimation approach to identify genes suited for normalization, applied to bladder and colon cancer data sets. Cancer Res. 64, 5245-5250.
84. Pfaffl, M. W., Tichopad, A., Prgomet, C. and Neuvians, T. P. (2004). Determination of stable housekeeping genes, differentially regulated target genes and sample integrity: BestKeeper-Excel-based tool using pair-wise correlations. Biotechnol. Lett., 26, 509-515.
85. Silver, N., Best, S., Jiang, J. and Thein, S. L. (2006). Selection of housekeeping genes for gene expression studies in human reticulocytes using real-time PCR. BMC Mol. Biol. 7, 33.
86. Xie, F., Xiao, P., Chen, D., Xu, L. and Zhang, B. (2012). miRDeepFinder: a miRNA analysis tool for deep sequencing of plant small RNAs. Plant Mol. Biol. 80, 75- 84.
87. Schmittgen, T. D. and Livak, K. J. (2008). Analyzing real-time PCR data by the comparative CT method. Nat. Protoc. 3, 1101–1108.
88. Kanda, Y. (2013). Investigation of the freely available easy-to-use software ‘EZR’ for medical statistics. Bone Marrow Transplant. 48, 452–458.
89. Takeshima, S. N.; Ohno, A. and Aida, Y. (2019). Bovine leukemia virus proviral load is more strongly associated with bovine major histocompatibility complex class II DRB3 polymorphism than with DQA1 polymorphism in Holstein cow in Japan. Retrovirology 16, 14.
90. Bendixen, H. J. (1963). Preventive measures in cattle leukemia: leukosis enzootica bovis. Ann. N. Y. Acad. Sci. 108, 1241-1267.
91. Raab-Traub, N. and Dittmer, D. P. (2017). Viral effects on the content and function of extracellular vesicles. Nat. Rev. Genet. 15, 559–572.
92. Jaworski, E., Narayanan, A., Van Duyne, R., Shabbeer-Meyering, S., Iordanskiy, S., Saifuddin, M., Das, R., Afonso, P. V., Sampey, G. C., Chung, M., Popratiloff, A., Shrestha, B., Sehgal, M., Jain, P., Vertes, A., Mahieux, R. and Kashanchi, F. (2014). Human T-lymphotropic virus type 1-infected cells secrete exosomes that contain Tax protein. J. Biol. Chem. 289, 22284–22305.
93. Armogida, S. A., Yannaras, N. M., Melton, A. L. and Srivastava, M. D. (2004). Identification and quantification of innate immune system mediators in human breast milk. Allergy Asthma Proc. 25, 297–304.
94. Kuang, M., Tao, X., Peng, Y., Zhang, W., Pan, Y., Cheng, L., Yuan, C., Zhao, Y., Mao, H., Zhuge, L., Zhou, Z., Chen, H. and Sun, Y. (2019). Proteomic analysis of plasma exosomes to differentiate malignant from benign pulmonary nodules. Clin. Proteomics 16, 5–11.
95. Zhang, N. and Zhang, S. (2019). Identification of differentially expressed genes between primary lung cancer and lymph node metastasis via bioinformatic analysis. Oncol. Lett. 18, 3754–3768.
96. Frie, M. C., Droscha, C. J., Greenlick, A. E. and Coussens, P. M. (2017). MicroRNAs encoded by bovine leukemia virus (BLV) are associated with reduced expression of B cell transcriptional regulators in dairy cattle naturally infected with BLV. Front. Vet. Sci. 4, 245.
97. Li, Y., Zhang, C., Qin, L., Li, D., Zhou, G., Dang, D., Chen, S., Sun, T., Zhang, R., Wu, W., Xi, Y., Jin, Y. and Duan, G. (2018). Characterization of critical functions of long non-coding RNAs and mRNAs in rhabdomyosarcoma cells and mouse skeletal muscle infected by enterovirus 71 using RNA-seq. Viruses 10, 556.
98. Cheishvili, D., Stefanska, B., Yi, C., Li, C. C., Yu, P., Arakelian, A., Tanvir, I., Khan, H. A., Rabbani, S. and Szyf, M. (2015). A common promoter hypomethylation signature in invasive breast, liver and prostate cancer cell lines reveals novel targets involved in cancer invasiveness. Oncotarget 6, 33253.
99. Carles, A., Millon, R., Cromer, A., Ganguli, G., Lemaire, F., Young, J., Wasylyk, C., Muller, D., Schultz, I., Rabouel, Y., Dembélé, D., Zhao, C., Marchal, P., Ducray, C., Bracco, L., Abecassis, J., Poch, O. and Wasylyk, B. (2005). Head and neck squamous cell carcinoma transcriptome analysis by comprehensive validated differential display. Oncogene 25, 1821–1831.
100. Marx, S., Dal Maso, T., Chen, J. W., Bury, M., Wouters, J., Michiels, C. and Le, Calvé B. (2020). Transmembrane (TMEM) protein family members: Poorly characterized even if essential for the metastatic process. Sem. Cancer Biol. 60, 96–106.
101. Wrzesiński, T., Szelag, M., Cieślikowski, W. A., Ida, A., Giles, R., Zodro, E., Szumska, J., Poźniak, J., Kwias, Z., Bluyssen, H. A. and Wesoly, J. (2015). Expression of pre-selected TMEMs with predicted ER localization as potential classifiers of ccRCC tumors. BMC Cancer 15, 518.
102. Meng, X., Brachova, P., Yang, S., Xiong, Z., Zhang, Y., Thiel, K. W. and Leslie, K. K. (2011). Knockdown of MTDH sensitizes endometrial cancer cells to cell death induction by death receptor ligand TRAIL and HDAC inhibitor LBH589 co-treatment. PLoS One 6, e20920.
103. Huang, Z, Fan, G. and Wang, D. (2017). Downregulation of calbindin 1, a calcium- binding protein, reduces the proliferation of osteosarcoma cells. Oncol. Lett. 13, 3727.
104. Panei, C. J., Suzuki, K., Echeverría, M. G., Serena, M. S., Metz, G. E. and González, E. T. (2009). Association of BOLA-DRB3.2 alleles with resistance and susceptibility to persistent lymphocytosis in BLV infected cattle in Argentina. Int. J. Dairy Sci. 4, 123–128.
105. Lo, C. W., Borjigin, L., Saito, S., Fukunaga, K., Saitou, E., Okazaki, K., Mizutani, T., Wada, S., Takeshima, S. N. and Aida, Y. (2020). BoLA-DRB3 polymorphism is associated with differential susceptibility to bovine leukemia virus-induced lymphoma and proviral load. Viruses 12, 352.
106. Wang, Y. T., Shi, T., Srivastava, S., Kagan, J., Liu, T. and Rodland, K. D. (2020). Proteomic analysis of exosomes for discovery of protein biomarkers for prostate and bladder cancer. Cancers 12, 2335.
107. Overbye, A., Skotland, T., Koehler, C. J., Thiede, B., Seierstad, T., Berge, V., Sandvig, K. and Llorente, A. (2015). Identification of prostate cancer biomarkers in urinary exosomes. Oncotarget 6, 30357–30376.
108. Reinhardt, T. A., Sacco, R. E., Nonnecke, B. J. and Lippolis, J. D. (2013). Bovine milk proteome: Quantitative changes in normal milk exosomes, milk fat globule membranes and whey proteomes resulting from Staphylococcus aureus mastitis. J. Proteom. 82, 141–154.
109. Nguyen, E. V., Centenera, M. M., Moldovan, M., Das, R., Irani, S., Vincent, A. D., Chan, H., Horvath, L. G., Lynn, D. J., Daly, R. J. and Butler, L. M. (2018). Identification of novel response and predictive biomarkers to hsp90 inhibitors through proteomic profiling of patient-derived prostate. Mol. Cell. Proteomics 17, 1470-1486.
110. Delosière, M., Pires, J.A., Bernard, L., Cassar-Malek, I. and Bonnet, M. (2020). Dataset reporting 4654 cow milk proteins listed according to lactation stages and milk fractions. Data Brief 29, 105105.
111. Wilson, S. R., Vehus, T., Berg, H. S. and Lundanes, E. Nano-LC in proteomics: recent advances and approaches. Bioanalysis 7, 1799–1815.
112. Lu, H., Tang, X., Sibley, M., Coburn, J., Rao, R., Shyama, Prasad., Ahsan, N. and Ramratnam, B. (2019). Impact of exosomal HIV-1 Tat expression on the human cellular proteome. Oncotarget 10, 5632-5644.
113. Dreesen, O. and Brivanlou, A. H. (2007). Signaling pathways in cancer and embryonic stem cells. Stem Cell Rev. 3, 7–17.
114. Takemoto, S., Mulloy, J. C., Cereseto, A., Migone, T. S., Patel, B. K., Matsuoka, M., Yamaguchi, K., Takatsuki, K., Kamihira, S., White, J. D., Leonard, W. J., Waldmann, T. and Franchini, G. (1997). Proliferation of adult T cell leukemia/lymphoma cells is associated with the constitutive activation of JAK/STAT proteins. Proc. Natl. Acad. Sci. U.S.A. 94, 13897-13902.
115. Sawada, N. (2013). Tight junction-related human diseases. Pathol. Int. 63, 1–12.
116. Hülsemann, M., Sanchez, C., Verkhusha, P. V., Des Marais, V., Mao, S. P. H., Donnelly, S. K., Segall, J. E. and Hodgson, L. (2021). TC10 regulates breast cancer invasion and metastasis by controlling membrane type-1 matrix metalloproteinase at invadopodia. Commun. Biol. 2021, 4: 1091.
117. Hu, X., Addlagatta, A., Lu, J., Matthews, B. W. and Liu, J. O. (2006). Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression. Proc. Natl. Acad. Sci. U.S.A. 103, 18148-18153.
118. Singh, S., Saraya, A., Das, P. and Sharma, R. (2017). Increased expression of MARCH8, an E3 ubiquitin ligase, is associated with growth of esophageal tumor. Cancer Cell Int. 17, 116.
119. Tada, T., Zhang, Y., Koyama, T., Tobiume, M., Tsunetsugu-Yokota, Y., Yamaoka, S., Fujita, H. and Tokunaga, K. (2015). MARCH8 inhibits HIV-1 infection by reducing virion incorporation of envelope glycoproteins. Nat. Med. 21, 1502- 1507.
120. Oyama, K., Fushida, S., Kinoshita, J., Okamoto, K., Makino, I., Nakamura, K., Hayashi, H., Inokuchi, M., Nakagawara, H., Tajima, H., Fujita, H., Takamura, H., Ninomiya, I., Kitagawa, H., Fujimura, T. and Ohta, T. (2013). Serum cytokeratin 18 as a biomarker for gastric cancer. Clin. Exp. Med. 13, 289-295.
121. Peduk, S., Tatar, C., Dincer, M., Ozer, B., Kocakusak, A., Citlak, G., Akinci, M. and Tuzun, I. S. (2018). The role of serum CK18, TIMP1, and MMP-9 levels in predicting R0 resection in patients with gastric cancer. Dis. Markers 2018, 5604702.
122. Han, W., Hu, C., Fan, Z. J. and Shen, G. L. (2021). Transcript levels of keratin 1/5/6/14/15/16/17 as potential prognostic indicators in melanoma patients. Sci. Rep. 11, 1023.
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