Specific interactions betweeen Nipah virus nucleocapsid (N) protein and Phospho-(P) protein using the yeast two-hybrid system (vector page tiada)
Nipah virus (NiV) which is a member of a new genus, Henipavirus, in the family Paramyxoviridae, encodes an unusually large phospho- (P) protein compared to other known paramyxoviruses. In this study, the region(s) involved in the interaction between this exceptionally large P protein with its nuc...
محفوظ في:
| المؤلف الرئيسي: | |
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| التنسيق: | أطروحة |
| اللغة: | English |
| منشور في: |
2006
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| الموضوعات: | |
| الوصول للمادة أونلاين: | http://psasir.upm.edu.my/id/eprint/177/1/549022_FBSB_2006_11.pdf |
| الوسوم: |
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| الملخص: | Nipah virus (NiV) which is a member of a new genus, Henipavirus, in the family
Paramyxoviridae, encodes an unusually large phospho- (P) protein compared to other
known paramyxoviruses. In this study, the region(s) involved in the interaction between
this exceptionally large P protein with its nucleocapsid (N) protein was investigated in
vivo using the yeast two-hybrid system. Deletion analysis was used to map the domain(s)
of both the N and P proteins involved in N-P and P-N interactions. Mapping of the
domains of N protein involved in its interaction with the P protein revealed that the Cterminal
30 amino acids (423-452 residues) are crucial for N-P interaction. However,
mapping of the domains of P protein involved in the P-N association demonstrated that
both the C-terminal 63 amino acids (470-532 residues) and the immediate N-terminal 62
amino acids (1-62 residues) simultaneously play a major role. Comparison of these
findings with other studies indicates that paramyxoviruses are different in terms of interaction domains(s) between these two essential viral proteins involved in genome
replication. |
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