서브메뉴
검색
Understanding Insect Midgut Receptors for Bt Protein Cry1Ac and Mechanism of Resistance to Cry1Ac in the Cabbage Looper, Trichoplusia ni
Understanding Insect Midgut Receptors for Bt Protein Cry1Ac and Mechanism of Resistance to Cry1Ac in the Cabbage Looper, Trichoplusia ni
상세정보
- 자료유형
- 학위논문 서양
- 최종처리일시
- 20250211151339
- ISBN
- 9798382843353
- DDC
- 595
- 서명/저자
- Understanding Insect Midgut Receptors for Bt Protein Cry1Ac and Mechanism of Resistance to Cry1Ac in the Cabbage Looper, Trichoplusia ni
- 발행사항
- [Sl] : Cornell University, 2024
- 발행사항
- Ann Arbor : ProQuest Dissertations & Theses, 2024
- 형태사항
- 227 p
- 주기사항
- Source: Dissertations Abstracts International, Volume: 85-12, Section: B.
- 주기사항
- Advisor: Wang, Ping.
- 학위논문주기
- Thesis (Ph.D.)--Cornell University, 2024.
- 초록/해제
- 요약The successful deployment of insecticidal proteins from Bacillus thuringiensis (Bt) via genetically engineered crops has revolutionized pest management practices in agriculture. However, the development of insect resistance to Bt toxins threatens the sustainable application of Bt-biotechnology. Current understanding of Bt resistance has indicated that resistance to Bt in insects is complex, involving multiple midgut proteins that serve as receptors for Bt toxins in the intoxication pathways. In this dissertation, I studied the genetic basis of resistance to Bt protein Cry1Ac in a greenhouse-evolved resistant strain of the cabbage looper, Trichoplusia ni. Using genetic and molecular approaches, I studied the genetic association of altered APN (Aminopeptidase N) expression with the ABCC2 (ABC transporter C2) and the association of Cry1Ac resistance with APNs. The results indicated that the downregulated APN1 expression in resistant T. ni and low expression of APN6 in susceptible T. ni were associated with mutations in APN1 and APN6 genes but were not with ABCC2. The high-level resistance to Cry1Ac in T. ni is associated with both ABCC2 and APN1 mutations and additional factors to be identified. The functional roles of putative Cry1Ac receptors ABCC2, ALP (alkaline phosphatase), APN1, and midgut cadherin (CAD) in larval susceptibility to Cry1Ac were systematically examined, using a series of gene knockout T. ni mutant strains. ABCC2 was confirmed to be a major receptor for Cry1Ac in T. ni, but knockout mutations in the ALP, APN, and CAD receptors resulted in none to low resistance in T. ni. Results also indicated additional resistance genes to be identified. Finally, I studied the role of carbohydrate moieties in the mode of action of Cry1Ac. The interaction of Cry1A with the midgut and Cry1Ac toxicity in larvae were analyzed in vitro and in vivo, using a carbohydrate binding chemical, Calcofluor. The results demonstrated that carbohydrate moieties play critically important roles in the functional specific binding of the toxin to the midgut receptors in the pathway of toxicity. Overall, the findings from this thesis research advanced our understanding of the mode of action of Cry proteins and mechanisms of insect resistance to Cry proteins.
- 일반주제명
- Entomology
- 일반주제명
- Biochemistry
- 일반주제명
- Toxicology
- 일반주제명
- Microbiology
- 일반주제명
- Molecular biology
- 키워드
- Midgut cadherin
- 키워드
- Bt resistance
- 키워드
- Trichoplusia ni
- 기타저자
- Cornell University Entomology
- 기본자료저록
- Dissertations Abstracts International. 85-12B.
- 전자적 위치 및 접속
- 로그인 후 원문을 볼 수 있습니다.
MARC
008250123s2024 us c eng d■001000017161318
■00520250211151339
■006m o d
■007cr#unu||||||||
■020 ▼a9798382843353
■035 ▼a(MiAaPQ)AAI31242077
■040 ▼aMiAaPQ▼cMiAaPQ
■0820 ▼a595
■1001 ▼aCotto Rivera, Rey O.▼0(orcid)0000-0003-4654-4014
■24510▼aUnderstanding Insect Midgut Receptors for Bt Protein Cry1Ac and Mechanism of Resistance to Cry1Ac in the Cabbage Looper, Trichoplusia ni
■260 ▼a[Sl]▼bCornell University▼c2024
■260 1▼aAnn Arbor▼bProQuest Dissertations & Theses▼c2024
■300 ▼a227 p
■500 ▼aSource: Dissertations Abstracts International, Volume: 85-12, Section: B.
■500 ▼aAdvisor: Wang, Ping.
■5021 ▼aThesis (Ph.D.)--Cornell University, 2024.
■520 ▼aThe successful deployment of insecticidal proteins from Bacillus thuringiensis (Bt) via genetically engineered crops has revolutionized pest management practices in agriculture. However, the development of insect resistance to Bt toxins threatens the sustainable application of Bt-biotechnology. Current understanding of Bt resistance has indicated that resistance to Bt in insects is complex, involving multiple midgut proteins that serve as receptors for Bt toxins in the intoxication pathways. In this dissertation, I studied the genetic basis of resistance to Bt protein Cry1Ac in a greenhouse-evolved resistant strain of the cabbage looper, Trichoplusia ni. Using genetic and molecular approaches, I studied the genetic association of altered APN (Aminopeptidase N) expression with the ABCC2 (ABC transporter C2) and the association of Cry1Ac resistance with APNs. The results indicated that the downregulated APN1 expression in resistant T. ni and low expression of APN6 in susceptible T. ni were associated with mutations in APN1 and APN6 genes but were not with ABCC2. The high-level resistance to Cry1Ac in T. ni is associated with both ABCC2 and APN1 mutations and additional factors to be identified. The functional roles of putative Cry1Ac receptors ABCC2, ALP (alkaline phosphatase), APN1, and midgut cadherin (CAD) in larval susceptibility to Cry1Ac were systematically examined, using a series of gene knockout T. ni mutant strains. ABCC2 was confirmed to be a major receptor for Cry1Ac in T. ni, but knockout mutations in the ALP, APN, and CAD receptors resulted in none to low resistance in T. ni. Results also indicated additional resistance genes to be identified. Finally, I studied the role of carbohydrate moieties in the mode of action of Cry1Ac. The interaction of Cry1A with the midgut and Cry1Ac toxicity in larvae were analyzed in vitro and in vivo, using a carbohydrate binding chemical, Calcofluor. The results demonstrated that carbohydrate moieties play critically important roles in the functional specific binding of the toxin to the midgut receptors in the pathway of toxicity. Overall, the findings from this thesis research advanced our understanding of the mode of action of Cry proteins and mechanisms of insect resistance to Cry proteins.
■590 ▼aSchool code: 0058.
■650 4▼aEntomology
■650 4▼aBiochemistry
■650 4▼aToxicology
■650 4▼aMicrobiology
■650 4▼aMolecular biology
■653 ▼aInsecticidal proteins
■653 ▼aMidgut cadherin
■653 ▼aBacillus thuringiensis
■653 ▼aBt resistance
■653 ▼aCry1Ac resistance
■653 ▼aTrichoplusia ni
■690 ▼a0353
■690 ▼a0487
■690 ▼a0383
■690 ▼a0410
■690 ▼a0307
■71020▼aCornell University▼bEntomology.
■7730 ▼tDissertations Abstracts International▼g85-12B.
■790 ▼a0058
■791 ▼aPh.D.
■792 ▼a2024
■793 ▼aEnglish
■85640▼uhttp://www.riss.kr/pdu/ddodLink.do?id=T17161318▼nKERIS▼z이 자료의 원문은 한국교육학술정보원에서 제공합니다.
