Anti-PrP antibodies detected at terminal stage of prion-affected mouse

被引：14

作者：

Sassa, Yukiko ^{[1
]}

Kataoka, Natsumi ^{[2
]}

Inoshima, Yasuo ^{[1
]}

Ishiguro, Naotaka ^{[1
]}

机构：

[1] Gifu Univ, Lab Food & Environm Hyg, Dept Vet Med, Fac Appl Biol Sci, Gifu 5011193, Japan

[2] Obihiro Univ Agr & Vet Med, Lab Vet Publ Hlth, Obihiro, Hokkaido 0808555, Japan

来源：

CELLULAR IMMUNOLOGY | 2010年 / 263卷 / 02期

关键词：

Anti-PrP antibody; Immune response; Prion; HUMORAL IMMUNE-RESPONSE; SCRAPIE-AFFECTED ANIMALS; MONOCLONAL-ANTIBODIES; PROLONGS SURVIVAL; PROTEIN; MICE; DISEASE; IMMUNIZATION; AGENT; PEPTIDE;

D O I：

10.1016/j.cellimm.2010.03.018

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The causative agent of priori diseases is the pathological isoform (PrPSc) of the host-encoded cellular prion protein (PrPC) PrPSc has an identical amino acid sequence to PrPC; thus, it has been assumed that an immune response against PrPSc could not be found in priori-affected animals In this study, we found the anti-prion protein (PrP) antibody at the terminal stage of mouse scrape. Several sera from mice in the terminal stage of scrapie reacted to the recombinant mouse PrP (rMPrP) molecules and brain homogenates of mouse priori diseases These results indicate that mouse could recognize PrPC or PrPSc as antigens by the host immune system Furthermore, immunization with rMPrP generates high titers of anti-PrP antibodies in wild-type mice. Some anti-PrP antibodies immunized with rMPrP prevent PrPSc replication in vitro The mouse sera from terminal priori disease have several wide epitopes, although mouse sera immunized with rMPrP possess narrow epitopes (C) 2010 Elsevier Inc All rights reserved

引用

页码：212 / 218

页数：7

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