239
Views
49
CrossRef citations to date
0
Altmetric
Original Articles

Sulfated Fibroin, a Novel Sulfated Peptide Derived from Silk, Inhibits Human Immunodeficiency Virus Replication in Vitro

, , , &
Pages 1664-1670 | Received 01 Feb 2000, Accepted 13 Apr 2000, Published online: 22 May 2014

  • 1) Condra, J. H., Schleif, W. A., Blahy, O. M., Gabryelski, L. J., Graham, D. J., Quintero, J. C., Rhodes, A., Robbins, H. L., Roth, E., Shivaprakash, M., Titus, D., Yang, T., Teppler, H., Squires, K. E., Deutsch, P. J., and Emini, E. A., In vivo emergence of HIV-1 variants resistant to multiple protease inhibitors. Nature, 374, 569-571 (1995).
  • 2) Richman, D. D., Fischl, M. A., Grieco, M. H., Gottlieb, M. S., Volberding, P. A., Liskin, O. L., Leedom, J. M., Groopman, J. E., Mildvan, D., Hirsch, M. S., Jackson, G. G., Durack, D. T., and Phil, D., Nusinoff-Lehrman, S., and the AZT collaborative working group, The toxicity of azidothymidine (AZT) in the treatment of patients with AIDS and AIDS-related complex, a double blind, placebo controlled trial. N. Engl. J. Med., 317, 192-197 (1987).
  • 3) Lang, W., Osmond, D., Page-Bodkin, K., Moss, A., and Winkelstein, W. Jr., Population-based estimates of antiretroviral therapy and anti-pneumocystis prophylaxis in San Francisco: 1991. J. Acquir. Immune Defic. Syndr., 6, 191-195 (1993).
  • 4) Yoshida, O., Nakashima, H., Yoshida, T., Kaneko, Y., Yamamoto, I., Matsuzaki, K., Uryu, T., and Yamamoto, N., Sulfation of the immunomodulating polysaccharide lentinan: A novel strategy for antivirals to human immunodeficiency virus (HIV). Biochem. Pharm., 37, 2887-2891 (1988).
  • 5) Jagodzinski, P. P., Wiaderkiewicz, R., Kurzawski, G., Kloczrwiak, M., Nakashima, H., Hyjek, E., Yamamoto, N., Uryu, T., Kaneko, Y., and Posner, M. R., Mechanism of the inhibitory effect of curdlan sulfate on HIV-1 infection in vitro. Virology, 202, 735-745 (1994).
  • 6) Nakashima, H., Inazawa, K., Ichiyama, K., Ito, M., Ikushima, N., Shoji, T., Katsuraya, K., Uryu, T., Yamamoto, N., Juodawlkis, A. S., and Schinazi, R. F., Sulfated alkyl oligosaccharides inhibit human immunodeficiency virus in vitro and provide sustained drug levels in mammals. Antiviral Chem. Chemother., 6, 271-280 (1995).
  • 7) Uryu, T., Katsuraya, K., and Nakashima, H., Synthesis of sulfated alkyl oligosaccharides with potent anti-HIV activity. Macromol. Symp., 120, 147-158 (1997).
  • 8) Nakashima, H., Matsui, T., Yoshida, O., Isowa, Y., Kido, Y., Motoki, Y., Ito, M., Shigeta, S., Mori, T., and Yamamoto, N., A new anti-human immunodeficiency virus substance, glycyrrhizin surfate; endowment of glycyrrhzin with reverse transcriptase-inhibitory activity by chemical modification. Jpn. J. Cancer. Res., 78, 767-771 (1987).
  • 9) Nakashima, H., Yoshida, O., Tochikura, T. S., Yoshida, T., Mimura, T., Kido, Y., Motoki, Y., Kaneko, Y., Uryu, T., and Yamamoto, N., Sulfation of polysaccharides generates potent and selective inhibitors of human immunodeficiency virus infection and replication in vitro. Jpn. J. Cancer. Res., 78, 1164-1168 (1987).
  • 10) Abrams, D. I., Kuno, S., Wong, R., Jeffords, K., Nash, M., Molaghan, J. B., Gorter, R., and Ueno, R., Oral dextran sulfate (UA001) in the treatment of the acquired immunodeficiency syndrome (AIDS) and AIDS-related complex. Ann. Intern. Med., 110, 183-188 (1989).
  • 11) Lorentsen, K. J., Hendrix, C. W., Collins, J. M., Kornhauser, D. M., Petty, B. G., Klecker, R. W., Flexner, C., Eckel, R. H., and Leitman, P. S., Dextran sulfate is poorly absorbed after oral administration. Ann. Int. Med., 111, 561-566 (1989).
  • 12) Flexner, C., Barditch, C. P. A., Kornhauser, D. M., Farzadegan, H., Nerhood, L. J., Chaisson, R. E., Bell, K. M., Lorentsen, K. J., Hendrix, C. W., Petty, B. G., and Leitman, P. S., Pharmacokinetics, toxicity, and activity of intravenous dextran sulfate in human immunodeficiency virus infection. Antimicrob. Agents Chemother., 35, 2544-2550 (1991).
  • 13) Mita, K., Ichimura, S., and Tharappel, C. J., Highly repetitive sutructure and its organization of the silk fibroin gene. J. Molecular. Evolution, 38, 583-592 (1994).
  • 14) Chackerian, B., Long, E. M., Luciw, P. A., and Overbaugh, J., HIV-1 co-receptors participates in postentry stages of the virus replication cycle and function in SIV infection. J. Virol., 71, 3932-3939 (1997).
  • 15) Nakashima, H., Masuda, M., Murakami, T., Koyanagi, Y., Matsumoto, A., Fujii, N., and Yamamoto, N., Anti-human immunodeficiency virus of a novel synthetic peptide, T22 ([Tyr-5, 12, Lys-7]polyphemusin II): a possible inhibitor of virus-cell fusion. Antimicrob. Agents. Chemother., 36, 1249-1255 (1992).
  • 16) Kimpton, J. and Emerman, M., Detection of replication-competent and pseudotyped human immunodeficiency virus with a sensitive cell line on the basis of activation of an integrated β-galactosidase gene. J. Virol., 166, 2232-2239 (1992).
  • 17) Arakaki, R., Tamamura, H., Premanathan, M., Kanbara, K., Ramanan, S., Mochizuki, K., Baba, M., Fujii, N., and Nakashima, H., T134, a small-molecule CXCR4 inhibitor, has no cross-drug resistance with AMD3100, a CXCR4 antagonist with a different structure. J. Virol., 73, 1719-1723 (1999).
  • 18) Tochikura, T. S., Nakashima, H., Tanabe, A., and Yamamoto, N., Human immunodeficiency virus (HIV)-induced cell fusion: quantification and its application for the simple and rapid screening of anti-HIV substances in vitro. Virology, 164, 542-546 (1988).
  • 19) Schols, D., Baba, M., Pauwels, R., and De Clercq, E., Flow cytometric method to demonstrate whether anti-HIV-1 agents inhibit virion binding to T4+ cells. J. Acquire. Immune. Defic. Syndr., 2, 10-15 (1989).
  • 20) Nakashima, H., Ichiyama, K., Hirayama, F., Uchino, K., Ito, M., Saitoh, T., Ueki, M., Yamamoto, N., and Ogawara, H., Sulfated pentagalloyl glucose (Y-ART-3) inhibits HIV replication and cytopathic effects in vitro, and reduces HIV infection in hu-PBL-SCID mice. Antiviral. Res., 30, 95-108 (1996).
  • 21) Dalgleish, A. G., Beverley, P. C., Clapham, P. R., Crawford, D. H., Greaves, M. F., and Weiss, R. A., The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus. Nature, 312, 763-767 (1984).
  • 22) Klatzmann, D., Champagne, E., Chamaret, S., Gruest, J., Guetard, D., Hercend, T., Gluckman, J. C., and Montagnier, L., T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV. Nature, 312, 767-768 (1984).
  • 23) Pearce, P. R. and Phillips, D. M., Studies of adhesion of lymphocytic cells: implications for sexual transmission of human immunodeficiency virus. Biol. Reprod., 48, 431-445 (1993).
  • 24) Stafford, M. K., Cain, D., Rosenstein, I., Fontaine, E. A., McClure, M., Flanagan, A. M., Smith, J. R., Taylor, R. D., Weber, J., and Kitchen, V. S., A placebo-controlled, double-blind prospective study in healthy female volunteers of dextrin sulphate gel: a novel potential intravaginal virucide. J. Acquir. Immune. Defic. Syndr. Hum. Retrovirol., 14, 213-218 (1997).
  • 25) Berger, E. A., HIV entry and tropism: the chemokine receptor connection. AIDS., 11, S3-16 (1997).
  • 26) Cairns, J. S. and D’Souza, M. P., Chemokines and HIV-1 second receptors: the therapeutic connection. Nat. Med., 4, 563-568 (1998).
  • 27) Berger, E. A., Doms, R. W., Fenyo, E. M., Korber, B. T., Littman, D. R., Moore, J. P., Sattentau, Q. J., Schuitemaker, H., Sodroski, J., and Weiss, R. A., A new classification for HIV-1. Nature, 15, 391, 240 (1998).
  • 28) Deng, H., Liu, R., Ellmeier, W., Choe, S., Unutmaz, D., Burkhart, M., Di Marzio, P., Marmon, S., Sutton, R. E., Hill, C. M., Davis, C. B., Schall, T. J., Littman, D. R., and Landau, N. R., Identification of a major co-receptor for primary isolates of HIV-1. Nature, 381, 661-666 (1996).
  • 29) Dragic, T., Litwin, V., Allaway, G. P., Martin, S. R., Huang, Y., Nagashima, K. A., Cayanan, C., Maddon, P. J., Koup, R. A., Moore, J. P., and Paxton, W. A., HIV-1 entry into CD4+ cells is mediated by the chemokine receptor CC-CKR-5. Nature, 381, 667-673 (1996).
  • 30) Alkhatib, G., Combadiere, C., Broder, C. C., Feng, Y., Kennedy, P. E., Murphy, P. M., and Berger, E. A., CC CKR5: a RANTES, MIP-1α, MIP-1β receptor as a fusion cofactor for macrophage-tropic HIV-1. Science, 272, 1955-1958 (1996).
  • 31) Choe, H., Farzan, M., Sun, Y., Sullivan, N., Rollins, B., Ponath, P. D., Wu, L., Mackay, C. R., LaRosa, G., Newman, W., Gerard, N., Gerard, C., and Sodrroski, J., The β-chemokine receptors CCR3 and CCR5 facilitate infection by primary HIV-1 isolates. Cell, 85, 1135-1148 (1996).
  • 32) Doranz, B. J., Rucker, J., Yi, Y., Smyth, R. J., Samson, M., Peiper, S. C., Parmentier, M., Collman, R. G., and Doms, R. W., A dual-tropic primary HIV-1 isolate that uses fusin and the β-chemokine receptors CKR-5, CKR-3, and CKR-2b as fusion cofactors. Cell, 85, 1149-1158 (1996).
  • 33) Oberlin, E., Amara, A., Bachelerie, F., Bessia, C., and Virelizier, J. L., The CXC chemokine SDF-1 is the ligand for LESTR/fusion and prevents infection by T-cell-line-adapted HIV-1. Nature, 382, 833-835 (1996).
  • 34) Connor, R. I., Increased viral burden and cytopathicity correlate temporally with CD4+ T-lymphocyte decline and clinical progression in human immunodeficiency virus type 1-infected individuals. J. Virol., 67, 1772-1777 (1993).
  • 35) Schuitemaker, H., Koot, M., Kootstra, N. A., Dercksen, M. W., de Goede, R. E., van Steenwijk, R. P., Lange, J. M., Schattenkerk, J. K., Miedema, F., and Tersmette, M., Biological phenotype of human immunodeficiency virus type 1 clones at different stages of infection: progression of disease is associated with a shift from monocytotropic to T-cell-tropic virus population. J. Virol., 66, 1354-1360 (1992).
  • 36) Richman, D. D. and Bozzette S. A., The impact of the syncytium-inducing phenotype of human immunodeficiency virus on disease progression. J. Infect. Dis., 169, 968-74 (1994).
  • 37) Connor, R. I., Sheridan, K. E., Ceradini, D., Choe, S., and Landau, N. R., Change in coreceptor use correlates with disease progression in HIV-1-infected individuals. J. Exp. Med., 185, 621-628 (1997).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.