초록 ▼

가시아메바 (Acanthamoeba spp.)는 자유생활아메바의 하나로 서울시내 청계천, 논, 웅덩이, 저수지등에서 검출되었으며 병원성인 가시아메바는 수막뇌염이나 각막염 등을 일으킬수 있는데 최근 국내에서는 가시아메바에 의한 폐렴, 각막염등의 보고가 증가 추세이다.
병원성 가시아메바가 병변을 일으키는 기전은 아직까지 정확히 모르나 단백분해효소가 관여될 것이라고 추측되고 있는데 병원성이 강한 쿨버트손가시아메바( Acanthamoeba culbertsoni)로 부터 분리정제한 세포독성물질이 단백분해효소라는 보고가 있고 이 아메바로

가시아메바 (Acanthamoeba spp.)는 자유생활아메바의 하나로 서울시내 청계천, 논, 웅덩이, 저수지등에서 검출되었으며 병원성인 가시아메바는 수막뇌염이나 각막염 등을 일으킬수 있는데 최근 국내에서는 가시아메바에 의한 폐렴, 각막염등의 보고가 증가 추세이다.
병원성 가시아메바가 병변을 일으키는 기전은 아직까지 정확히 모르나 단백분해효소가 관여될 것이라고 추측되고 있는데 병원성이 강한 쿨버트손가시아메바( Acanthamoeba culbertsoni)로 부터 분리정제한 세포독성물질이 단백분해효소라는 보고가 있고 이 아메바로부터 단백분해효소를 분리한 보고가 있을 뿐이다.

Abstract ▼

Free living amoebas including pathogenic Aamthamoeba cuIbertsoni and nonpathogenic Acxznthamoeba royreba are widely distributed in soil and fresh water. The pathogenic mechanisms of Acantiamoeba spp. were not been fully recognized yet Amoebae destroy host tissue rapidly during the process of amoebic

Free living amoebas including pathogenic Aamthamoeba cuIbertsoni and nonpathogenic Acxznthamoeba royreba are widely distributed in soil and fresh water. The pathogenic mechanisms of Acantiamoeba spp. were not been fully recognized yet Amoebae destroy host tissue rapidly during the process of amoebic meningoencephalitis and keratitis, so their pathogenic mechanisms were supposed to be related to cytotoxicity. It was reported that the cytotoxicity of A. culbertsoni is mainly related to the proteinase activity in vitro. This suggests that the proteinase activity is one of the important pathogenic mechanism of A. cuIbertsoni.Cysteine proteinase eDNA fragment from Aamthamoeba culbertsoni westermani was amplified by reverse transcription-polymerase chain reaction (RT-PCR) using degenerate oligonucleotide primers derived from conserved cysteine proteinase sequences. The amplified product was approximately 500 bp in length 5$\prime$ and the 3$\prime$ regions of the cysteine proteinase gene were amplified using the PCR protocol for the rapid amplification of eDNA ends (RACE-PCR). It has an open reading frame of 1538 bp. The deduced amino acid sequence has the sequence homology with the cysteine proteinase gene of metacercaria of Paragonimus uiestermani, Schistosoma mansoni, Human cathepsin L and Fasciola hepatica, each by 45.3%, 45.9%, 57.9% and 50.8%. Sequence analysis and alignment showed significant similarity to other eukaryotic cysteine proteinases and conservation of the cysteine, histidine, and asparagine residues that form the catalytic triad. An 1.5kbp mRNA was detected on northern blot analysis using full-length cysteine proteinase eDNA as a probe.
The gene(AcCP2) have found a ExxxRxxxWxxN instead of ExxxRxxxFxxN at proregion and also proline/threonine-rich C-terminal extension. So it has a cathepsin L-like characteristics.Phylogenetic analysis by the PAUP indicated that the cysteine proteinase gene(AcCP2) were closed related for papaya, while Schistosoma sp. gene were more distant from the gene

목차 Contents

• 표지...1
• 목차...2
• 제출문...3
• 2. 연구계획서 요약문(국문)...4
• 3. 연구내용...5
• 가. 연구결과 요약문(국.영문)...5
• 나. 서론...7
• 다. 연구방법 및 이론...8
• 라. 결과 및 고찰...13
• 마. 결론...23
• 바. 인용문헌...24
• 논문발표 목록서...26
• 자체평가서...27