Multiple sclerosis (PP-038)

Zenichiro, K.; Kataoka, Hirotoshi; Shimano, Kyoko; Seki, Noriko; Sugahara, Kazuhiro; Sugita, Takahisa; Chiba, Kenichi; Zhang, S.; Zeng, Xiuya; He, Shasha; Sakata, D.; Esaki, Yusuke; Li, Y.; Yao, Chenxiao; Segi-Nishida, E.; Matsuoka, Takashi; Fukuda, Kouichi; Narumiya, S.; Yen, Jeng-Hsien; Ganea, Doina; Ikeda, Takahiro; Shinya, Hiromi; Satoshi, F.; Takaaki, I.; Makoto, U.; Satoru, S.; Yasuharu, N.; Mosayebi, G.; Ghasami, Keyvan; Ghazavi, Ali; Jand, Yahya; Khazaei, M R; Payani, M H; Mirshafiey, Abbas; Maeda, Y; Funahashi, Yasuhiro; Koyama, Motomichi; Fukunari, Atsushi; Mendesh, M. A.; Balmukhanov, T. S.; Аitkhozhinа, N. А.; Nair, Parameswaran; Patel, Sheel; Vishwakarma, Sandeep Kumar; Melarkode, Ramakrishnan; Montero, Efs; O'Sulllivan, D.; Gibbons, J. L.; Kharkrang, Marie; Connor, Bernadette; Flamme, Anne Camille La; Nuyts, Amber H.; Cools, Nathalie; Camp, K. Van; Lenders, Kevin; Stein, Benjamin; D'hooghe, Marie B; Nagels, Guy; Willekens, Barbara; Berneman, Z. N.; Tendeloo, Viggo F.I. Van; Haas, Jürgen; Korporal, Mirjam; Schwarz, Alexander; Balint, Bettina; Fritz, Benjamin; Wildemann, Brigitte; Ng, Judy King Man; Malotka, Joachim; Derfuss, Tobias; Khademi, Mohsen; Olsson, T.; Sämann, Philipp G.; Weber, Felix; Rasband, Matthew N.; Linington, Christopher; Hohlfeld, Reinhard; Wekerle, Hartmut; Dornmair, Klaus; Meinl, Edgar; Marche, Patrice N.; Dougier-Reynaud, H.; Lomparski, Christina; Bernard, C.; Villiers, Christian; Duperray, Alain; Jouvin‐Marche, Evelyne; Perron, Hervé; Loo, Eileen; Krantz, Mark J.; Agrawal, Bimal K; Dutra, Rafael Cypriano; Leite, Daniela Ferraz Pereira; Manjavachi, Marianne N.; Patrício, Emília; Bento, Alexandra; Figueiredo, Carolina; Pesquero, João Bosco; Calixto, João Β.; Yoshimura, Sakuji; Ochi, Hirofumi; Isobe, Naoko; Matsushita, Tomonaga; Motomura, Kenta; Minohara, Motozumi; Kira, J.; Jeon, Sang-Bok; Jeong, Seong-heon; Seong, Rho Hyun; Kadowaki, Masanori; Tanaka, Satoshi; Miyamoto, Yuya; Okazawa, Takahiro; Yanagida, Maki; Ikeda, Masahiko; H, Uga; Kurata, Hideaki; Смагин, А. А.; Гольдина, И. А.; Ito, Kei; Kurotaki, D.; Matsui, Yohei; Kanayama, Mayuko; Morimoto, J.; T.Uede,; Mohan, Hema; Elliott, Colm; Krumbholz, Markus; Arthur, Ariel; Lassmann, H.; Barnett, Susan C.; Jamshidian, Azam; Nikseresht, Ali Reza; Vessal, Mohamoud; Kamali-Sarvestani, Eskandar; Choi, Hyoung Soo; Hong, J.; Kim, Y.; Hong, David S.; Kim, S.; Lee, G.; Lee, J.; Shin, Myung Sun; Hong, Mei‐Zhu; Bae, Ho; Fitz-Gerald, Leslie; Zastepa, Evelyn; Antel, Jack; Lapierre, Yves; Bar‐Or, Amit; Arnold, D. L.; Haegert, David G.; Chihara, Norio; Sato, Wakako; Aranami, Toshimasa; Miyazaki, Yusei; Miyake, Susumu; Okamoto, Takahiro; Ogawa, Masahiro; Yamamura, Teiichi; Guerreiro-Cacais, André Ortlieb; Beyeen, Amennai Daniel; Jagodic, Maja; Tomita, Akihiro; Li, P.; Duan, Lian; Yang, Yintang; Ma, Wei; Xu, Yu; Fang, Mengjie; Tan, Zheng; Zheng, Fufu; Gong, Fengying; Zhang, D.; Izad, Maryam; Harirchian, Mohammad Hossein; Fard, H. Amiri; Najafi, Fereshteh; Gheflati, Zahra; Lee, L.; Tu, Gang; Logronio, Kathryn; Axtell, Robert C.; Steinman, Lawrence; Lin, Jeffrey; Marecková, H; Havrdová, Eva; Krasulová, Eva; Kovářová, Ivana; Skacikova, L.; Hrušková, Zdenka; Trněný, Marek; Aguirre-Cruz, Lucinda; Flores-Rivera, José; Mader, Simone; Chapul, L.; Cruz-Aguilera, Dora Luz de la; Fragoso, Gladis; Reindl, Markus; Berger, Tamar; Corona, Teresa; Zoghi, Samaneh; Amirghofran, Zahra

doi:10.1093/intimm/dxq125

Cited by 1 publication

(4 citation statements)

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“…In autoimmune diseases, the antigen is autologous. For example, myelin surrounding the nerves in the CNS and destruction leads to paralysis and eventually death (17). Similarities between "vaccine induced" and "autoimmune disease induced" antigen attack, suggest we may be able to learn from emerging vaccine strategies in our design of tolerogenic therapies.…”

Section: Discussionmentioning

confidence: 99%

“…"signal" recognition or stimulation) (28,29). TYSABRI® is non-specific and leads to unwanted immunosuppressive effects and the effectiveness of Copaxone® has been questioned (17,19,27). Enhancing the specificity of these types of therapies (e.g., by combining them) could reduce side effects and improve potency.…”

Section: Discussionmentioning

confidence: 99%

“…Additionally, the much smaller fusion peptide, BPI PLP:LABL , was evaluated. All BPI and SAgA treatments showed significant suppression of EAE disease score (p<0.05) for days [11][12][13][14][15][16][17] (Fig. 2a).…”

Section: Backbone Scaffold Size and Structure Affect Degree Of Eae Sumentioning

confidence: 93%

“…"Antigen-specific immunotherapies" (antigenSITs) also use antigen, most notably in the form of subcutaneous allergy shots. The antigen-SIT approach has also been investigated to reverse the root cause of autoimmune disease by repeatedly injecting low doses of autoantigen (15)(16)(17)(18).…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Structure, Size, and Solubility of Antigen Arrays Determines Efficacy in Experimental Autoimmune Encephalomyelitis

Sestak

Fakhari

Badawi

et al. 2014

AAPS J

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ABSTRACT. Presentation of antigen with immune stimulating "signal" has been a cornerstone of vaccine design for decades. Here, the antigen plus immune "signal" of vaccines is modified to produce antigen-specific immunotherapies (antigen-SITs) that can potentially reprogram the immune response toward tolerance of an autoantigen. The codelivery of antigen with a cell adhesion inhibitor using Soluble Antigen Arrays (SAgAs) was previously shown to slow or halt experimental autoimmune encephalomyelitis (EAE), a murine form of multiple sclerosis (MS). SAgAs are comprised of a hyaluronic acid backbone with cografted intercellular cell adhesion molecule-1 ligand derived from α L -integrin (CD11a 237-246 , "LABL") and an encephalitogenic epitope peptide of proteolipid protein (PLP 139-151 , "PLP"). Here, the physical characteristics of the carrier were investigated to evaluate how structure, size, and solubility drive the immune response when treating EAE. A bifunctional peptide (small, soluble), SAgAs (large, soluble), and PLGA nanoparticles (large, insoluble) all displaying PLP and LABL in equimolar ratios were compared. Maximum EAE suppression was achieved with coincident display of both peptides on a soluble construct.

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Section: Discussionmentioning

confidence: 99%