Central Institute of Medicinal & Aromatic Plants (CIMAP), CIMAP (P.O.), Lucknow-226015, UP.
Abstracts of the papers presented at the 16th Annual Convention and International Symposium of Indian Virological Society on “Management of Vector-Borne Viruses” at International Crops Research Institute for the Semi-Arid Tropics (ICRISAT), Patancheru-502324, Hyderabad, India, February 7–10, 2006.
Among all the conformations, a protein has a unique or nearly unique native conformation, which is the surviving conformation under specific biological conditions. Information concerning the native folded state of the coat protein (CP) has great potential in the elucidation of biochemical pathways and their implications in managing the plant diseases as well as in determining the organism's nature. For secondary structure determination, all the biophysical techniques available so far take a lot of time, great effort, resources, knowledge and experience. Secondary structures of CPs are predicted from amino acid sequence data, using the mathematical method Chou-Fasman table, of CMV isolates from Indian henbane (CMV-H), Amaranthus (CMV-A) and CMV-P strain. All of them belong to subgroup IB and showed high sequence identity (>95%) among themselves in both nt and aa sequence of CP. The secondary structure analysis using Chou-Fasman table showed that CMV-H has no turn/bend at L16 where as CMV-A and CMV-P has bend/turn at that position. CMV-P showed a unique helix structure at D29. Helix structure is absent at L75 of CMV-A while present in both CMV-H and CMV-P. The turn/bend at positions F117, D118 and helix at M187 of CMV-A are absent in other two cases. It is â sheet in both CMV-H and CMV-P at the aforesaid positions. These unique structural modifications in the CP of CMV-H, CMV-A and CMV-P helped them to identify the host cells and evade the defense system of the host cells.
