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رسائل ماجيستير الانجليزية 2009 0ae3835d-878b-4103-8d94-cb3ba4d8e453

The Role of Human Cytomegalovirus UL16 Glycoprotein and pp65 Phosphoprotein on Tegument Site, Membrane and Raft Association in Human Fibroblast Infected Cells

خضر محمد ابراهيم زواهرة, ميساء العزة

كلية الدراسات العليا-جامعة القدس · فلسطين

الموضوعات

علوم بحتة وطبيعية

الملخص

Herpes viruses are double stranded DNA viruses, classified under three sub-groups; alpha-, beta- (to which human cytomegaloviruses belong), and gammaherpesviruses. HCMV structure consists of icosahedral capsid encasing 235-kbp genome. The capsid is surrounded by the tegument, which is surrounded by the envelope. pp65 is a major viral tegument proteins with multiple phosphorylation sits. UL97 is also a tegument protein and encodes the only viral kinase, which is a serine/threonine protein kinase that plays a role in phosphorylation events of viral and cellular proteins. The viral envelop contains a large number of virus-encoded glycoproteins. UL16 is an envelope glycoprotein, which interferes with the immune response by inter action with MICB (MHC Class I-Related chains)ULBPs (UL16-binding proteins). The critical functions of UL16 and pp65 in viral life cycle encouraged us to study these proteins and their roles in viral assembly, membrane and raft association, and their interaction with UL97 viral kinase in infected HF cells. Further more, the influence of cellular kinase inhibitors, wortmannin and polymyxin B, was tested in infected cells. Our immunofluorescence experiments using UL16 polyclonal antibodies, revealed that UL16 distributed differently in AD169 (wt) infected HF cells, compared with ΔUL97 deletion mutant infected cells. UL16 distributed as a “bulb like” compact juxtnuclear structure in (wt) viruses infected cells and as a “crown like”diffuse perinuclear Structure highly punctuated with vacuoles in ΔUL97 infected cells. UL16 also co-localized with the major assembly site building proteins. Inhibitors of cellular kinase PI-3 and C affected the subcellular distribution of UL16 in (wt) virus infected cells as well as the resulted viral titer. These inhibitors did not result in major effects on UL16 subcellular distribution or on the viral titer in Δpp65 or ΔUL97 infected cells.

التعريف والنوع

رقم الوثيقة
0ae3835d-878b-4103-8d94-cb3ba4d8e453
رقم العقد
0
نوع الوسائط
Crawler
نوع المحتوى
الرسائل العلمية
صيغة المصدر
رسائل ماجيستير
نوع الملف
pdf text
أسماء الملفات
1696908_1.pdf

بيانات النشر

ألقاب المؤلفين
[{"name_ar":"خضر محمد ابراهيم زواهرة","title_ar":"اعداد","title_en":"Preparation"},{"name_ar":"ميساء العزة","title_ar":"اشراف","title_en":"Supervision"}]
اللغة
English

المصدر والدورية

اسم المصدر
The Role of Human Cytomegalovirus UL16 Glycoprotein and pp65 Phosphoprotein on Tegument Site, Membrane and Raft Association in Human Fibroblast Infected Cells

المحتوى والصفحات

عدد الصفحات
0

إشراف وإعداد

الإشراف
ميساء العزة
الإعداد
خضر محمد ابراهيم زواهرة

الاقتباسات الببليوغرافية

APA

خضر محمد ابراهيم زواهرة و ميساء العزة. (2009). The Role of Human Cytomegalovirus UL16 Glycoprotein and pp65 Phosphoprotein on Tegument Site, Membrane and Raft Association in Human Fibroblast Infected Cells. أطروحة(رسائل ماجيستير). كلية الدراسات العليا-جامعة القدس. فلسطين.

MLA

خضر محمد ابراهيم زواهرة و ميساء العزة. The Role of Human Cytomegalovirus UL16 Glycoprotein and pp65 Phosphoprotein on Tegument Site, Membrane and Raft Association in Human Fibroblast Infected Cells. 2009. كلية الدراسات العليا-جامعة القدس، رسائل ماجيستير.