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PP7 Virus-Like Particles as a Biotechnology Platform.
PP7 Virus-Like Particles as a Biotechnology Platform.
상세정보
- 자료유형
- 학위논문(국외)
- 기본표목-개인명
- 표제와 책임표시사항
- PP7 Virus-Like Particles as a Biotechnology Platform.
- 발행, 배포, 간사 사항
- 발행, 배포, 간사 사항
- 형태사항
- 228 p.
- 일반주기
- Source: Dissertations Abstracts International, Volume: 87-05, Section: B.
- 일반주기
- Includes supplementary digital materials.
- 일반주기
- Advisor: Finn, M. G.
- 학위논문주기
- Thesis (Ph.D.)--Georgia Institute of Technology, 2024.
- 요약 등 주기
- 요약This dissertation explores various aspects of the PP7 virus-like particles (VLPs), leveraging their structural versatility and immunogenic potential for applications ranging from biotechnology to vaccine development. Chapter 2 investigates the assembly tolerance of LeviphagePP7 dimer VLPs, through a library-based approach, for incorporation of random 15-mer peptide sequences on the surface of the capsid. Using protein engineering and molecular biology tools, this study significantly broadened the repertoire of assembly-competent VLP sequences, revealing trends that promotes or disrupts self-assembly. In Chapter 3, we delved into the structural plasticity observed in WT and engineered PP7 VLPs, showcasing a wide range of morphologies influenced by minor alterations in coat protein sequences. This unexpected diversity underscores the adaptability of self-assembling structures and its implications for various applications, shedding light on the evolutionary strategies of viruses. In Chapter 4, we employed PP7 VLPs to display peptide sequences targeting key mutations of SARS-CoV-2 to raise monoclonal antibodies with preferred binding towards key mutations present in several variants of concern. Heterologous prime-boost regimens with VLPpeptide and RBD elicited novel monoclonal antibodies with high affinities towards specific strains. The collective work described in this dissertation is meant to guide the scientific community in exploring the sequence landscape and structure of PP7 while providing an example of its immunological impact.
- 주제명부출표목-일반주제명
- 주제명부출표목-일반주제명
- 주제명부출표목-일반주제명
- 주제명부출표목-일반주제명
- 주제명부출표목-일반주제명
- 주제명부출표목-일반주제명
- 부출표목-단체명
- 기본자료저록
- Dissertations Abstracts International. 87-05B.
- 전자적 위치 및 접속
- 원문정보보기
MARC
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■1001 ▼aKeshavarz-Joud, Parisa.
■24510▼aPP7 Virus-Like Particles as a Biotechnology Platform.
■260 ▼a[S.l.]▼bGeorgia Institute of Technology. ▼c2024
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2024
■300 ▼a228 p.
■500 ▼aSource: Dissertations Abstracts International, Volume: 87-05, Section: B.
■500 ▼aIncludes supplementary digital materials.
■500 ▼aAdvisor: Finn, M. G.
■5021 ▼aThesis (Ph.D.)--Georgia Institute of Technology, 2024.
■520 ▼aThis dissertation explores various aspects of the PP7 virus-like particles (VLPs), leveraging their structural versatility and immunogenic potential for applications ranging from biotechnology to vaccine development. Chapter 2 investigates the assembly tolerance of LeviphagePP7 dimer VLPs, through a library-based approach, for incorporation of random 15-mer peptide sequences on the surface of the capsid. Using protein engineering and molecular biology tools, this study significantly broadened the repertoire of assembly-competent VLP sequences, revealing trends that promotes or disrupts self-assembly. In Chapter 3, we delved into the structural plasticity observed in WT and engineered PP7 VLPs, showcasing a wide range of morphologies influenced by minor alterations in coat protein sequences. This unexpected diversity underscores the adaptability of self-assembling structures and its implications for various applications, shedding light on the evolutionary strategies of viruses. In Chapter 4, we employed PP7 VLPs to display peptide sequences targeting key mutations of SARS-CoV-2 to raise monoclonal antibodies with preferred binding towards key mutations present in several variants of concern. Heterologous prime-boost regimens with VLPpeptide and RBD elicited novel monoclonal antibodies with high affinities towards specific strains. The collective work described in this dissertation is meant to guide the scientific community in exploring the sequence landscape and structure of PP7 while providing an example of its immunological impact.
■590 ▼aSchool code: 0078.
■650 4▼aPhages.
■650 4▼aDesign.
■650 4▼aViruses.
■650 4▼aHepatitis B.
■650 4▼aSymmetry.
■650 4▼aVirology.
■690 ▼a0389
■690 ▼a0720
■71020▼aGeorgia Institute of Technology.
■7730 ▼tDissertations Abstracts International▼g87-05B.
■790 ▼a0078
■791 ▼aPh.D.
■792 ▼a2024
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17360243▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
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