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Production of transgenic algal strain harboring novel design for human norovirus G.II.4 shell for vaccine and diagnosis improvement / Mahmoud Ali Abdelatty Ali Elgamal ; Supervised Mohamed Abdelhamid Shalaby , Ausama Abdelraouf A.Yousif , Ahmed Abdelwahed

By: Contributor(s): Material type: TextTextLanguage: English Publication details: Cairo : Mahmoud Ali Abdelatty Ali Elgamal , 2020Description: 97 P. : charts , facsmiles ; 25cmOther title:
  • لإنتاج تحصين و تطوير طرق التشخيص (HuNo. G.II.4 shell)نتاج عطرة من الطحالب تحوى تصميم جديد لجين القشرة لفيروس النورو [Added title page title]
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Dissertation note: Thesis (M.Sc.) - Cairo University - Faculty of Veterinary Medicine - Department of Virology Summary: Norovirus is the leading cause of nonbacterial gastroenteritis all over the world .In developing countries, it accounts for 200000 deaths in children younger than 5 years annually. They belong to family Caliciviridae and contains at least six genogroups with more than 30 genotypes. But only strains from genogroups I, II and, IV infect human, where NoV GII predominate. Noroviruses have single stranded RNA positive sense genome of approximately 7.5 kb in three ORFs. ORF2: encodes the major viral capsid protein and the antigenic determinant (VP1). VP1 is composed of shell (S) and protruding (P) domains. Shell domain is known for relative genetic and antigenic conservancy. The wide genetic and antigenic variation even among the same genogroup renders the species, generally, elusive for sensitive specific diagnosis and vaccine design. Virus uncultivability and lack of a suitable animal model contributed to failure of development of standard sensitive economic diagnosis and commercial vaccine.To overcome uncultivability, several trials for norovirus heterologous protein expression was performed. But all of them showed drawbacks that relates to design of the expressed protein, or to limitations of the utilized host. In this study we designed a multifunctional chimeric construct. It encodes Shell (S) domain of HuNo G.II.4 and NDV fusion (F) domain. Both domains were linked using proper peptide linker. Finally a stabilizer was linked to the C-terminus of the whole construct.The stabilizer was added to enhance the expression of construct in the newly emerging algal system; Chlamydomonas reinharditti But fusion domain was added to ease purification of produced protein by affinity
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Thesis Thesis قاعة الرسائل الجامعية - الدور الاول المكتبة المركزبة الجديدة - جامعة القاهرة Cai01.10.17.M.Sc.2020.Ma.P (Browse shelf(Opens below)) Not for loan 01010110081489000
CD - Rom CD - Rom مخـــزن الرســائل الجـــامعية - البدروم المكتبة المركزبة الجديدة - جامعة القاهرة Cai01.10.17.M.Sc.2020.Ma.P (Browse shelf(Opens below)) 81489.CD Not for loan 01020110081489000

Thesis (M.Sc.) - Cairo University - Faculty of Veterinary Medicine - Department of Virology

Norovirus is the leading cause of nonbacterial gastroenteritis all over the world .In developing countries, it accounts for 200000 deaths in children younger than 5 years annually. They belong to family Caliciviridae and contains at least six genogroups with more than 30 genotypes. But only strains from genogroups I, II and, IV infect human, where NoV GII predominate. Noroviruses have single stranded RNA positive sense genome of approximately 7.5 kb in three ORFs. ORF2: encodes the major viral capsid protein and the antigenic determinant (VP1). VP1 is composed of shell (S) and protruding (P) domains. Shell domain is known for relative genetic and antigenic conservancy. The wide genetic and antigenic variation even among the same genogroup renders the species, generally, elusive for sensitive specific diagnosis and vaccine design. Virus uncultivability and lack of a suitable animal model contributed to failure of development of standard sensitive economic diagnosis and commercial vaccine.To overcome uncultivability, several trials for norovirus heterologous protein expression was performed. But all of them showed drawbacks that relates to design of the expressed protein, or to limitations of the utilized host. In this study we designed a multifunctional chimeric construct. It encodes Shell (S) domain of HuNo G.II.4 and NDV fusion (F) domain. Both domains were linked using proper peptide linker. Finally a stabilizer was linked to the C-terminus of the whole construct.The stabilizer was added to enhance the expression of construct in the newly emerging algal system; Chlamydomonas reinharditti But fusion domain was added to ease purification of produced protein by affinity

Issued also as CD

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