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Titolo:
Borna disease virus phosphoprotein binds a neurite outgrowth factor, amphoterin/HMG-1
Autore:
Kamitani, W; Shoya, Y; Kobayashi, T; Watanabe, M; Lee, BJ; Zhang, GQ; Tomonaga, K; Ikuta, K;
Indirizzi:
Osaka Univ, Res Inst Microbial Dis, Dept Virol, Suita, Osaka 5650871, Japan Osaka Univ Suita Osaka Japan 5650871 t Virol, Suita, Osaka 5650871, Japan Hokkaido Univ, Inst Immunol Sci, Sect Serol, Kita Ku, Sapporo, Hokkaido 0600815, Japan Hokkaido Univ Sapporo Hokkaido Japan 0600815 oro, Hokkaido 0600815, Japan
Titolo Testata:
JOURNAL OF VIROLOGY
fascicolo: 18, volume: 75, anno: 2001,
pagine: 8742 - 8751
SICI:
0022-538X(200109)75:18<8742:BDVPBA>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
PSYCHIATRIC-PATIENTS; INFECTED-CELLS; NERVOUS-SYSTEM; HMG1 PROTEIN; BRAIN; EXPRESSION; SEQUENCE; RNA; LOCALIZATION; ANTIBODIES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Tomonaga, K Osaka Univ, Res Inst Microbial Dis, Dept Virol, 3-1-Yamadaoka,Suita, Osaka 5650871, Japan Osaka Univ 3-1-Yamadaoka Suita Osaka Japan 5650871 0871, Japan
Citazione:
W. Kamitani et al., "Borna disease virus phosphoprotein binds a neurite outgrowth factor, amphoterin/HMG-1", J VIROLOGY, 75(18), 2001, pp. 8742-8751

Abstract

The Borna disease virus (BDV) p24 phosphoprotein is an abundant protein inBDV-infected cultured cells and animal brains. Therefore, there is a possibility that binding of the p24 protein to cellular factor(s) induces functional alterations of infected neural cells in the brain. To identify a cellular protein(s) that interacts with BDV p24 protein, we performed far-Western blotting with extracts from various cell lines. Using recombinant p24 protein as a probe, we detected a 30-kDa protein in all cell lines examined. Binding between the 30-kDa and BDV p24 proteins was also demonstrated using BDV p24 affinity and ion-exchange chromatography columns. Microsequence analysis of the purified 30-kDa protein revealed that its N terminus showed complete homology with rat amphoterin protein, which is a neurite outgrowth factor abundant in the brain during development. Mammalian two-hybrid and immunoprecipitation analyses also confirmed that amphoterin is a specific target for the p24 protein in vivo. Furthermore, we showed that infection by BDV, as well as purified p24 protein in the medium, significantly decreased cell process outgrowth of cells grown on laminin, indicating the functionalinhibition of amphoterin by interaction with the p24 protein. Immunohistochemical analysis revealed decreased levels of amphoterin protein at the leading edges of BDV-infected cells. Moreover, the expression of the receptor for advanced glycation end products, of which the extracellular moiety is areceptor for amphoterin, was not significantly activated in BDV-infected cells during the process of extension, suggesting that the secretion of amphoterin from the cell surface is inhibited by the binding of the p24 protein. These results suggested that BDV infection may cause direct damage in thedeveloping brain by inhibiting the function of amphoterin due to binding by the p24 phosphoprotein.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/01/20 alle ore 09:24:24